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Conserved domains on  [gi|7657599|ref|NP_055241|]
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sorting nexin-5 isoform a [Homo sapiens]

Protein Classification

PX and BAR domain-containing protein( domain architecture ID 10163626)

PX (Phox homology) and BAR (Bin/Amphiphysin/Rvs) domain-containing protein, similar to sorting nexins that are involved in regulating membrane traffic and protein sorting in the endosomal system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_SNX5 cd07663
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid ...
 185-402 2.28e-141

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153347  Cd Length: 218  Bit Score: 401.62  E-value: 2.28e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  185 GFFKSVVKSADEVLFTGVKEVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKK 264
Cdd:cd07663   1 GFFKNMVKSADEVLFSGVKEVDEFFEQEKTFLVNYYNRIKDSCAKADKMTRSHKNVADDYIHISAALNSVAAEEPTVIKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  265 YLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAEAHQQ 344
Cdd:cd07663  81 YLLKVAELFEKLRKVEDRVASDQDLKLTELLRYYMLNIEAAKDLLYRRARALADYENSNKALDKARLKSKDVKQAEAHQQ 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7657599  345 ECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFK 402
Cdd:cd07663 161 ECCQKFEKLSESAKQELISFKRRRVAAFRKNLIEMTELEIKHAKNNVSLLQSCIDLFK 218
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
 29-169 1.31e-108

The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels.


:

Pssm-ID: 132824  Cd Length: 141  Bit Score: 315.46  E-value: 1.31e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   29 PSLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDYAGLIIPPAPTKPDFDGPREKMQK 108
Cdd:cd07291   1 PSLQIDIPDALSERDKVKFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETEDYAGLIIPPAPPKPDFDGPREKMQK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7657599  109 LGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYD 169
Cdd:cd07291  81 LGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEYD 141
 
Name Accession Description Interval E-value
BAR_SNX5 cd07663
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid ...
 185-402 2.28e-141

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153347  Cd Length: 218  Bit Score: 401.62  E-value: 2.28e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  185 GFFKSVVKSADEVLFTGVKEVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKK 264
Cdd:cd07663   1 GFFKNMVKSADEVLFSGVKEVDEFFEQEKTFLVNYYNRIKDSCAKADKMTRSHKNVADDYIHISAALNSVAAEEPTVIKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  265 YLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAEAHQQ 344
Cdd:cd07663  81 YLLKVAELFEKLRKVEDRVASDQDLKLTELLRYYMLNIEAAKDLLYRRARALADYENSNKALDKARLKSKDVKQAEAHQQ 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7657599  345 ECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFK 402
Cdd:cd07663 161 ECCQKFEKLSESAKQELISFKRRRVAAFRKNLIEMTELEIKHAKNNVSLLQSCIDLFK 218
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
 29-169 1.31e-108

The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels.


Pssm-ID: 132824  Cd Length: 141  Bit Score: 315.46  E-value: 1.31e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   29 PSLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDYAGLIIPPAPTKPDFDGPREKMQK 108
Cdd:cd07291   1 PSLQIDIPDALSERDKVKFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETEDYAGLIIPPAPPKPDFDGPREKMQK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7657599  109 LGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYD 169
Cdd:cd07291  81 LGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEYD 141
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 179-386 7.77e-16

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 76.17  E-value: 7.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599    179 TKEMFGGFFKSVVKSAdevlfTGVKEVDDFFEQEKNFLINYYNRIKdSCVKADKMTRSHKN----VADDYihtAACLHSL 254
Cdd:pfam09325   1 LSSLFGKFFSSVSKSS-----YKFNEPDEWFIDKKQYIDSLESQLK-KLYKALELLVSQRKelasATGEF---AKSLASL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599    255 A-LEEPTVIKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKAL------- 326
Cdd:pfam09325  72 AsLELSTGLSRALSQLAEVEERIKELLERQALQDVLTLGETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELskkkeql 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7657599    327 -----------DKARLKSKDVKLAEAHQQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKH 386
Cdd:pfam09325 152 ekllranksqnDKLQQAKKEVEELERRVQQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIES 222
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 55-169 1.86e-14

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 68.04  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599     55 LPTFQSPEFSVTRQHEDFVWLHDTLIETtdYAGLIIPPAPTKPDFdgprekmqklgegeGSMTKEEFAKMKQELEaeyla 134
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRK--FPSVIIPPLPPKRWL--------------GRYNEEFIEKRRKGLE----- 59

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 7657599    135 vfkktvssheVFLQRLSSHPVLSKDRNFHVFLEYD 169
Cdd:pfam00787  60 ----------QYLQRLLQHPELRNSEVLLEFLESD 84
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 35-292 2.62e-06

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 49.41  E-value: 2.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   35 IPDALSERDKVKFT-----VHTKTTLPTFQ---SPEFSVTRQHEDFVWLHDTLIEttDYAGLIIPPAPTKpdfdgprekm 106
Cdd:COG5391 137 NPQSLTLLVDSRDKhtsyeIITVTNLPSFQlreSRPLVVRRRYSDFESLHSILIK--LLPLCAIPPLPSK---------- 204

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  107 QKLGEGEGSMTKEEFAKMKQELEaeylavfkktvsshEVFLQRLSSHPVLSKDRNFHVFLEYDQDLSVRRKNTKEMFGGF 186
Cdd:COG5391 205 KSNSEYYGDRFSDEFIEERRQSL--------------QNFLRRVSTHPLLSNYKNSKSWESHSTLLSSFIENRKSVPTPL 270

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  187 FKSVVKSADEVLfTGVKEVDDFFEQEKNFLINYYNRIKDSCVKADkmtRSHKNVAdDYIHTAACLH--SLALEEPTVIKK 264
Cdd:COG5391 271 SLDLTSTTQELD-MERKELNESTSKAIHNILSIFSLFEKILIQLE---SEEESLT-RLLESLNNLLllVLNFSGVFAKRL 345

                       250       260
                ....*....|....*....|....*...
gi 7657599  265 YLLKVAELFEKLRKVEGRVSSDEDLKLT 292
Cdd:COG5391 346 EQNQNSILNEGVVQAETLRSSLKELLTQ 373
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 62-167 6.33e-05

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 41.95  E-value: 6.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599      62 EFSVTRQHEDFVWLHDTLIEttDYAGLIIPPAPTKpdfdgprekmqKLGEGEGSMTKEEFAKMKQELeaeylavfkktvs 141
Cdd:smart00312  27 EWTVSRRYSDFLELHSKLKK--HFPRSILPPLPGK-----------KLFGRLNNFSEEFIEKRRRGL------------- 80

                           90       100
                   ....*....|....*....|....*..
gi 7657599     142 shEVFLQRLSSHPVLSK-DRNFHVFLE 167
Cdd:smart00312  81 --EKYLQSLLNHPELINhSEVVLEFLE 105
 
Name Accession Description Interval E-value
BAR_SNX5 cd07663
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid ...
 185-402 2.28e-141

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153347  Cd Length: 218  Bit Score: 401.62  E-value: 2.28e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  185 GFFKSVVKSADEVLFTGVKEVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKK 264
Cdd:cd07663   1 GFFKNMVKSADEVLFSGVKEVDEFFEQEKTFLVNYYNRIKDSCAKADKMTRSHKNVADDYIHISAALNSVAAEEPTVIKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  265 YLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAEAHQQ 344
Cdd:cd07663  81 YLLKVAELFEKLRKVEDRVASDQDLKLTELLRYYMLNIEAAKDLLYRRARALADYENSNKALDKARLKSKDVKQAEAHQQ 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7657599  345 ECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFK 402
Cdd:cd07663 161 ECCQKFEKLSESAKQELISFKRRRVAAFRKNLIEMTELEIKHAKNNVSLLQSCIDLFK 218
BAR_SNX5_6 cd07621
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, ...
 185-402 5.67e-121

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Members of this subfamily include SNX5, SNX6, the mammalian SNX32, and similar proteins. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. The function of SNX32 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153305  Cd Length: 219  Bit Score: 349.71  E-value: 5.67e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  185 GFFKSVVKSADE-VLFTGVKEVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIK 263
Cdd:cd07621   1 GFLKSISKSADEeLLLSGQKDVDEFFEQEKNFLVEYHNRIKDATAKADKMTRKHKDVADSYIKISAALTQLATSEPTPLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  264 KYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAEAHQ 343
Cdd:cd07621  81 KFLLKVAETFEKLRKLEGRVASDEDLKLSDTLRYYMRDTQAAKDLLYRRLRCLANYENANKNLEKARAKNKDVHAAEAAQ 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7657599  344 QECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFK 402
Cdd:cd07621 161 QEACEKFESMSESAKQELLDFKTRRVAAFRKNLVELAELEIKHAKAQIQLLKNCLAALK 219
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
 29-169 1.31e-108

The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels.


Pssm-ID: 132824  Cd Length: 141  Bit Score: 315.46  E-value: 1.31e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   29 PSLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDYAGLIIPPAPTKPDFDGPREKMQK 108
Cdd:cd07291   1 PSLQIDIPDALSERDKVKFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETEDYAGLIIPPAPPKPDFDGPREKMQK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7657599  109 LGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYD 169
Cdd:cd07291  81 LGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEYD 141
PX_SNX5_like cd06892
The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is ...
 29-169 3.77e-92

The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Members of this subfamily include SNX5, SNX6, and similar proteins. They contain a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p.


Pssm-ID: 132802  Cd Length: 141  Bit Score: 273.54  E-value: 3.77e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   29 PSLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDYAGLIIPPAPTKPDFDGPREKMQK 108
Cdd:cd06892   1 SSLQVDISDALSERDKVKFTVHTKTTLPTFQKPEFSVTRQHEEFVWLHDTLVENEDYAGLIIPPAPPKPDFDASREKLQK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7657599  109 LGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYD 169
Cdd:cd06892  81 LGEGEGSMTKEEFEKMKQELEAEYLAIFKKTVAMHEVFLRRLASHPVLRNDANFRVFLEYE 141
BAR_SNX6 cd07662
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid ...
 186-402 6.88e-92

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153346  Cd Length: 218  Bit Score: 275.77  E-value: 6.88e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  186 FFKSVVKSADEVLFTGVKEVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKKY 265
Cdd:cd07662   2 FFKNVVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDSSAKSDRMTRSHKSAADDYNRIGSSLYTLGTQDSTDICKF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  266 LLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAEAHQQE 345
Cdd:cd07662  82 FLKVSELFDKTRKIEARVAADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETTQQL 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7657599  346 CCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFK 402
Cdd:cd07662 162 CCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQSCLAVLN 218
PX_SNX6 cd07292
The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a ...
 30-169 3.66e-72

The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). SNX6 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs.


Pssm-ID: 132825  Cd Length: 141  Bit Score: 222.67  E-value: 3.66e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   30 SLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDYAGLIIPPAPTKPDFDGPREKMQKL 109
Cdd:cd07292   2 ALQVDISDALSERDKVKFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPDFDASREKLQKL 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  110 GEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYD 169
Cdd:cd07292  82 GEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 141
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 204-398 2.32e-26

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 105.13  E-value: 2.32e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  204 EVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKKY---LLKVAELFEKLRKVE 280
Cdd:cd07596   1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEVGGELgeaLSKLGKAAEELSSLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  281 GRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLK------------------SKDVKLAEAH 342
Cdd:cd07596  81 EAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQleklkaapgikpakveelEEELEEAESA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7657599  343 QQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCI 398
Cdd:cd07596 161 LEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLL 216
BAR_SNX_like cd07630
The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized Sorting Nexins; BAR domains are ...
 204-398 6.24e-24

The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of uncharacterized proteins with similarity to sorting nexins (SNXs), which are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153314  Cd Length: 198  Bit Score: 97.96  E-value: 6.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  204 EVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVADDYIHTAACLH-SLALEEPTV--IKKYLLKVAELFEKLRKVE 280
Cdd:cd07630   1 DVDEFFQKERDMNTKLSANMKEAAEKFLKIVNTEQRLANALGHLSSSLQlCVGLDEASVvaLNRLCTKLSEALEEAKENI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  281 GRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVklAEAHQQECCQKFEQLSESAKEE 360
Cdd:cd07630  81 EVVAGNNENTLGLTLDLYSRYSESEKDMLFRRTCKLIEFENASKALEKAKPQKKEQ--AEEAKKKAETEFEEISSLAKKE 158

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7657599  361 LINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCI 398
Cdd:cd07630 159 LERFHRQRVLELQSALVCYAESQIKNAKEAAAVLTKTL 196
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 45-169 9.73e-21

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 86.86  E-value: 9.73e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   45 VKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETtdYAGLIIPPAPTKpdfdgprekmQKLGegegsMTKEEFakm 124
Cdd:cd06859  19 VVYRVTTKTNLPDFKKSEFSVLRRYSDFLWLYERLVEK--YPGRIVPPPPEK----------QAVG-----RFKVKF--- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 7657599  125 kQELEAEYLAVfkktvsshEVFLQRLSSHPVLSKDRNFHVFLEYD 169
Cdd:cd06859  79 -EFIEKRRAAL--------ERFLRRIAAHPVLRKDPDFRLFLESD 114
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
 45-166 2.16e-16

The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. This subfamily consists of SNX7, SNX30, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of the sorting nexins in this subfamily has yet to be elucidated.


Pssm-ID: 132770  Cd Length: 116  Bit Score: 74.68  E-value: 2.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   45 VKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETtdYAGLIIPPAPTKPDFDGPREKMQKlgegegsmtkeEFakm 124
Cdd:cd06860  19 ITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEES--HPTHIIPPLPEKHSVKGLLDRFSP-----------EF--- 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7657599  125 kqeLEAEYLAVFKktvsshevFLQRLSSHPVLSKDRNFHVFL 166
Cdd:cd06860  83 ---VATRMRALHK--------FLNRIVEHPVLSFNEHLKVFL 113
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
 45-169 6.87e-16

The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. The PX domain of Vps5p binds phosphatidylinositol-3-phosphate (PI3P). Similar to SNX1, Vps5p contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1.


Pssm-ID: 132771  Cd Length: 112  Bit Score: 73.16  E-value: 6.87e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   45 VKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETtdYAGLIIPPAPTKpdfdgprekmQKLGEGEgsmtkEEFakm 124
Cdd:cd06861  19 TVYTVRTRTTSPNFEVSSFSVLRRYRDFRWLYRQLQNN--HPGVIVPPPPEK----------QSVGRFD-----DNF--- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 7657599  125 kqeLEAEYLAVfkktvsshEVFLQRLSSHPVLSKDRNFHVFLEYD 169
Cdd:cd06861  79 ---VEQRRAAL--------EKMLRKIANHPVLQKDPDFRLFLESE 112
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 179-386 7.77e-16

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 76.17  E-value: 7.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599    179 TKEMFGGFFKSVVKSAdevlfTGVKEVDDFFEQEKNFLINYYNRIKdSCVKADKMTRSHKN----VADDYihtAACLHSL 254
Cdd:pfam09325   1 LSSLFGKFFSSVSKSS-----YKFNEPDEWFIDKKQYIDSLESQLK-KLYKALELLVSQRKelasATGEF---AKSLASL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599    255 A-LEEPTVIKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKAL------- 326
Cdd:pfam09325  72 AsLELSTGLSRALSQLAEVEERIKELLERQALQDVLTLGETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELskkkeql 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7657599    327 -----------DKARLKSKDVKLAEAHQQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKH 386
Cdd:pfam09325 152 ekllranksqnDKLQQAKKEVEELERRVQQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIES 222
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
 45-167 1.44e-14

The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation protein; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The yeast Atg24p is a sorting nexin (SNX) which is involved in membrane fusion events at the vacuolar surface during pexophagy. This is facilitated via binding of Atg24p to phosphatidylinositol 3-phosphate (PI3P) through its PX domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132773  Cd Length: 118  Bit Score: 69.62  E-value: 1.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   45 VKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIEttDYAGLIIPPAPTKpdfdgprekmQKLGEGEGSMTKEEFakm 124
Cdd:cd06863  20 ISYLITTKTNLPSFSRKEFKVRRRYSDFVFLHECLSN--DFPACVVPPLPDK----------HRLEYITGDRFSPEF--- 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 7657599  125 kqeleaeylaVFKKTVSSHEvFLQRLSSHPVLSKDRNFHVFLE 167
Cdd:cd06863  85 ----------ITRRAQSLQR-FLRRISLHPVLSQSKILHQFLE 116
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 55-169 1.86e-14

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 68.04  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599     55 LPTFQSPEFSVTRQHEDFVWLHDTLIETtdYAGLIIPPAPTKPDFdgprekmqklgegeGSMTKEEFAKMKQELEaeyla 134
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRK--FPSVIIPPLPPKRWL--------------GRYNEEFIEKRRKGLE----- 59

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 7657599    135 vfkktvssheVFLQRLSSHPVLSKDRNFHVFLEYD 169
Cdd:pfam00787  60 ----------QYLQRLLQHPELRNSEVLLEFLESD 84
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
 47-167 1.97e-13

The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. Similar to SNX1, SNX2 contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX domain of SNX2 preferentially binds phosphatidylinositol-3-phosphate (PI3P), but not PI(3,4,5)P3. Studies on mice deficient with SNX1 and/or SNX2 suggest that they provide an essential function in embryogenesis and are functionally redundant.


Pssm-ID: 132815  Cd Length: 124  Bit Score: 66.62  E-value: 1.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   47 FTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDYAGLIIPPAPTKPDFDgprekMQKLGEGEGSMTKEEFAKMKQ 126
Cdd:cd07282  21 YRVTTKTSLSMFSRSEFSVRRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVG-----MTKVKVGKEDSSSTEFVEKRR 95

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 7657599  127 eleaeylavfkktvSSHEVFLQRLSSHPVLSKDRNFHVFLE 167
Cdd:cd07282  96 --------------AALERYLQRTVKHPTLLQDPDLRQFLE 122
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 45-169 7.07e-13

The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX1 is both membrane associated and a cytosolic protein that exists as a tetramer in protein complexes. It can associate reversibly with membranes of the endosomal compartment, thereby coating these vesicles. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 contains a Bin/Amphiphysin/Rvs (BAR) domain C-terminal to the PX domain. The PX domain of SNX1 specifically binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,5)P2, while the BAR domain detects membrane curvature. Both domains help determine the specific membrane-targeting of SNX1, which is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network.


Pssm-ID: 132814  Cd Length: 124  Bit Score: 65.08  E-value: 7.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   45 VKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDYAGLIIPPAPTKPDFDgprekMQKLGEGEGSMTKEEFAKM 124
Cdd:cd07281  19 VVYKVTTQTSLLMFRSKHFTVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEKSLIG-----MTKVKVGKEDSSSAEFLER 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 7657599  125 KQeleaeylavfkktvSSHEVFLQRLSSHPVLSKDRNFHVFLEYD 169
Cdd:cd07281  94 RR--------------AALERYLQRIVSHPSLLQDPDVREFLEKE 124
BAR_SNX1_2 cd07623
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, ...
 245-386 5.17e-10

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX1, SNX2, and similar proteins. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153307  Cd Length: 224  Bit Score: 59.21  E-value: 5.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  245 IHTAACLHSLAL----EEPTVIKKYLLKVAELFEKLRKVEGRvSSDEDL-KLTELLRYYMLNIEAAKDLLYRRTKALIDY 319
Cdd:cd07623  47 LNTGSFAKSAAMlsncEEHTSLSRALSQLAEVEEKIEQLHGE-QADTDFyILAELLKDYIGLIGAIKDVFHERVKVWQNW 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  320 ENSNKALDKAR-LKSK---------------DVKLAEAHQQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELE 383
Cdd:cd07623 126 QNAQQTLTKKReAKAKlelsgrtdkldqaqqEIKEWEAKVDRGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYLESL 205


                ...
gi 7657599  384 IKH 386
Cdd:cd07623 206 LNT 208
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
 46-166 7.26e-10

The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. This subfamily is composed of uncharacterized proteins, predominantly from plants, with similarity to sorting nexins. A few members show a similar domain architecture as a subfamily of sorting nexins, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit is known to determine specific membrane localization.


Pssm-ID: 132775  Cd Length: 120  Bit Score: 56.27  E-value: 7.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   46 KFTVHTKttLPTFQSPEFSVTRQHEDFVWLHDTLIETtdYAGLIIPPAPTKPDFDGPRekmqklgegegsMTKEEFAKMK 125
Cdd:cd06865  27 KVTTRTN--IPSYTHGEFTVRRRFRDVVALADRLAEA--YRGAFVPPRPDKSVVESQV------------MQSAEFIEQR 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7657599  126 -QELeaeylavfkktvsshEVFLQRLSSHPVLSKDRNFHVFL 166
Cdd:cd06865  91 rVAL---------------EKYLNRLAAHPVIGLSDELRVFL 117
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
 45-166 2.90e-09

The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX7 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, SNX30, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX7 has yet to be elucidated.


Pssm-ID: 132817  Cd Length: 116  Bit Score: 54.60  E-value: 2.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   45 VKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETtdYAGLIIPPAPTKPDFDGPREKMQklgegegsmtkEEFakm 124
Cdd:cd07284  19 ITYRVMTKTSRSEFDSSEFEVRRRYQDFLWLKGRLEEA--HPTLIIPPLPEKFVMKGMVERFN-----------EDF--- 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7657599  125 kqeLEAEYLAVFKktvsshevFLQRLSSHPVLSKDRNFHVFL 166
Cdd:cd07284  83 ---IETRRKALHK--------FLNRIADHPTLTFNEDFKIFL 113
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 32-167 9.07e-09

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 52.75  E-value: 9.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   32 QIDIPDALSERDK----VKFTVHTKTTLptfqSPEFSVTRQHEDFVWLHDTLIETtdYAGLIIPPAPTKPDFdgprekmq 107
Cdd:cd06093   1 SVSIPDYEKVKDGgkkyVVYIIEVTTQG----GEEWTVYRRYSDFEELHEKLKKK--FPGVILPPLPPKKLF-------- 66

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  108 klgegeGSMTKEEFAKMKQELEAeylavfkktvsshevFLQRLSSHPVLSKDRNFHVFLE 167
Cdd:cd06093  67 ------GNLDPEFIEERRKQLEQ---------------YLQSLLNHPELRNSEELKEFLE 105
PX_SNX30 cd07283
The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; The PX domain is a ...
 45-166 1.11e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX30 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX30 has yet to be elucidated.


Pssm-ID: 132816  Cd Length: 116  Bit Score: 50.08  E-value: 1.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   45 VKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDYAglIIPPAPTKPDFDGPREKMQklgegegsmtkEEFAKM 124
Cdd:cd07283  19 ITYRVTTKTTRTEFDLPEYSVRRRYQDFDWLRNKLEESQPTH--LIPPLPEKFVVKGVVDRFS-----------EEFVET 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7657599  125 KQEleaeylavfkktvsSHEVFLQRLSSHPVLSKDRNFHVFL 166
Cdd:cd07283  86 RRK--------------ALDKFLKRIADHPVLSFNEHFNVFL 113
PX_SNX3_like cd06894
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3 and related proteins; The ...
 31-167 1.84e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 3 and related proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily is composed of SNX3, SNX12, and fungal Grd19. Grd19 is involved in the localization of late Golgi membrane proteins in yeast. SNX3/Grp19 associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer.


Pssm-ID: 132804  Cd Length: 123  Bit Score: 46.68  E-value: 1.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   31 LQIDIPDALSERD-KVKFT---VHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDyagLIIPPAPTKPdfdgprEKM 106
Cdd:cd06894   2 LEIDVVNPQTHGVgKKRFTdyeVRMRTNLPVFKKKESSVRRRYSDFEWLRSELERDSK---IVVPPLPGKA------LKR 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7657599  107 QKLGEGEGSMTKEEFAKMKQeleaeylavfkktvSSHEVFLQRLSSHPVLSKDRNFHVFLE 167
Cdd:cd06894  73 QLPFRGDDGIFEEEFIEERR--------------KGLETFINKVAGHPLAQNEKCLHMFLQ 119
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 35-292 2.62e-06

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 49.41  E-value: 2.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   35 IPDALSERDKVKFT-----VHTKTTLPTFQ---SPEFSVTRQHEDFVWLHDTLIEttDYAGLIIPPAPTKpdfdgprekm 106
Cdd:COG5391 137 NPQSLTLLVDSRDKhtsyeIITVTNLPSFQlreSRPLVVRRRYSDFESLHSILIK--LLPLCAIPPLPSK---------- 204

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  107 QKLGEGEGSMTKEEFAKMKQELEaeylavfkktvsshEVFLQRLSSHPVLSKDRNFHVFLEYDQDLSVRRKNTKEMFGGF 186
Cdd:COG5391 205 KSNSEYYGDRFSDEFIEERRQSL--------------QNFLRRVSTHPLLSNYKNSKSWESHSTLLSSFIENRKSVPTPL 270

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  187 FKSVVKSADEVLfTGVKEVDDFFEQEKNFLINYYNRIKDSCVKADkmtRSHKNVAdDYIHTAACLH--SLALEEPTVIKK 264
Cdd:COG5391 271 SLDLTSTTQELD-MERKELNESTSKAIHNILSIFSLFEKILIQLE---SEEESLT-RLLESLNNLLllVLNFSGVFAKRL 345

                       250       260
                ....*....|....*....|....*...
gi 7657599  265 YLLKVAELFEKLRKVEGRVSSDEDLKLT 292
Cdd:COG5391 346 EQNQNSILNEGVVQAETLRSSLKELLTQ 373
PX_SNX12 cd07294
The phosphoinositide binding Phox Homology domain of Sorting Nexin 12; The PX domain is a ...
 47-176 5.06e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 12; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. The specific function of SNX12 has yet to be elucidated.


Pssm-ID: 132827  Cd Length: 132  Bit Score: 45.80  E-value: 5.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   47 FTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDyagLIIPPAPtkpdfdGPREKMQKLGEGEGSMTKEEFAKMKQ 126
Cdd:cd07294  24 YEVRMRTNLPIFKLKESCVRRRYSDFEWLKNELERDSK---IVVPPLP------GKALKRQLPFRGDEGIFEESFIEERR 94

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 7657599  127 EleaeylavfkktvsSHEVFLQRLSSHPVLSKDRNFHVFLeydQDLSVRR 176
Cdd:cd07294  95 Q--------------GLEQFINKIAGHPLAQNERCLHMFL---QDETIDR 127
PX_SNX3 cd07293
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a ...
 47-167 6.04e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX3 associates with early endosomes through a PX domain-mediated interaction with phosphatidylinositol-3-phosphate (PI3P). It associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer. SNX3 is required for the formation of multivesicular bodies, which function as transport intermediates to late endosomes. It also promotes cell surface expression of the amiloride-sensitive epithelial Na+ channel (ENaC), which is critical in sodium homeostasis and maintenance of extracellular fluid volume.


Pssm-ID: 132826  Cd Length: 123  Bit Score: 45.37  E-value: 6.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   47 FTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDyagLIIPPAPTKPDFdgprekMQKLGEGEGSMTKEEF-AKMK 125
Cdd:cd07293  22 YEIRLKTNLPIFKLKESTVRRRYSDFEWLRSELERESK---VVVPPLPGKALF------RQLPFRGDDGIFDDSFiEERK 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7657599  126 QELEAeylavfkktvsshevFLQRLSSHPVLSKDRNFHVFLE 167
Cdd:cd07293  93 QGLEQ---------------FLNKVAGHPLAQNERCLHMFLQ 119
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
 48-166 6.27e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It shows a similar domain architecture as SNX1-2, among others, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. SNX4 is implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and the long form of the leptin receptor.


Pssm-ID: 132774  Cd Length: 129  Bit Score: 45.44  E-value: 6.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   48 TVHTKTTLPTFQSPE-FSVTRQHEDFVWLHDTLIETtdYAGLIIPPAPTKpdfdgprekmqklgegegsmtKEEFakMKQ 126
Cdd:cd06864  30 TKIVEHESEEGLSKKlSSLWRRYSEFELLRNYLVVT--YPYVIVPPLPEK---------------------RAMF--MWQ 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7657599  127 ELEAEYL-AVF-KKTVSSHEVFLQRLSSHPVLSKDRNFHVFL 166
Cdd:cd06864  85 KLSSDTFdPDFvERRRAGLENFLLRVAGHPELCQDKIFLEFL 126
BAR_SNX2 cd07664
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid ...
 188-381 7.24e-06

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153348 [Multi-domain]  Cd Length: 234  Bit Score: 46.97  E-value: 7.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  188 KSVVKSADEVLFTGVK--EVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVAddyIHTAACLHSLAL----EEPTV 261
Cdd:cd07664   1 RMVNKAADAVNKMTIKmnESDAWFEEKQQQFENLDQQLRKLHASVESLVCHRKELS---ANTAAFAKSAAMlgnsEDHTA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  262 IKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLA-- 339
Cdd:cd07664  78 LSRALSQLAEVEEKIDQLHQDQAFADFYLFSELLGDYIRLIAAVKGVFDQRMKCWQKWQDAQVTLQKKREAEAKLQYAnk 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7657599  340 --------------EAHQQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSE 381
Cdd:cd07664 158 pdklqqakdeikewEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLE 213
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 62-167 6.33e-05

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 41.95  E-value: 6.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599      62 EFSVTRQHEDFVWLHDTLIEttDYAGLIIPPAPTKpdfdgprekmqKLGEGEGSMTKEEFAKMKQELeaeylavfkktvs 141
Cdd:smart00312  27 EWTVSRRYSDFLELHSKLKK--HFPRSILPPLPGK-----------KLFGRLNNFSEEFIEKRRRGL------------- 80

                           90       100
                   ....*....|....*....|....*..
gi 7657599     142 shEVFLQRLSSHPVLSK-DRNFHVFLE 167
Cdd:smart00312  81 --EKYLQSLLNHPELINhSEVVLEFLE 105
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
 64-166 4.62e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX9, SNX18, and similar proteins. They contain an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1.


Pssm-ID: 132772  Cd Length: 125  Bit Score: 39.99  E-value: 4.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   64 SVTRQHEDFVWLHDTLIETtdYAGLIIPPAPTKpdfdgprekmQKLGEGEgsmtkEEFAKM-KQELEAeylavfkktvss 142
Cdd:cd06862  33 TVSRRYKHFDWLYERLVEK--YSCIAIPPLPEK----------QVTGRFE-----EDFIEKrRERLEL------------ 83

                        90       100
                ....*....|....*....|....
gi 7657599  143 hevFLQRLSSHPVLSKDRNFHVFL 166
Cdd:cd06862  84 ---WMNRLARHPVLSQSEVFRHFL 104
BAR_SNX1 cd07665
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; BAR domains are dimerization, lipid ...
 192-381 7.22e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153349 [Multi-domain]  Cd Length: 234  Bit Score: 40.82  E-value: 7.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  192 KSADEVLFTGVK--EVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVAddyIHTAACLHSLAL----EEPTVIKKY 265
Cdd:cd07665   5 KATDAVSKMTIKmnESDVWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELA---LNTALFAKSLAMlgssEDNTALSRA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  266 LLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDK-----ARL--KSKDVKL 338
Cdd:cd07665  82 LSQLAEVEEKIEQLHQEQANNDFFLLAELLADYIRLLSAVRGAFDQRMKTWQRWQDAQAMLQKkreaeARLlwANKPDKL 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 7657599  339 AEAHQQ---------ECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSE 381
Cdd:cd07665 162 QQAKDEiaewesrvtQYERDFERISATVRKEVIRFEKEKSKDFKNHIIKYLE 213
BAR_Vps5p cd07627
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ...
 204-376 9.47e-04

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153311 [Multi-domain]  Cd Length: 216  Bit Score: 40.37  E-value: 9.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  204 EVDDFFEQEKNFLINYYNRIKdSCVKADKMTRSHKNVADDYIHT-AACLHSLALEEPT-VIKKYLLKVAELFEKLRKVEG 281
Cdd:cd07627   1 EPDEWFIEKKQYLDSLESQLK-QLYKSLELVSSQRKELASATEEfAETLEALSSLELSkSLSDLLAALAEVQKRIKESLE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  282 RVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLK------------------SKDVKLAEAHQ 343
Cdd:cd07627  80 RQALQDVLTLGVTLDEYIRSIGSVRAAFAQRQKLWQYWQSAESELSKKKAQleklkrqgktqqeklnslLSELEEAERRA 159

                       170       180       190
                ....*....|....*....|....*....|...
gi 7657599  344 QECCQKFEQLSESAKEELINFKRKRVAAFRKNL 376
Cdd:cd07627 160 SELKKEFEEVSELIKSELERFERERVEDFRNSV 192
BAR_SNX7_30 cd07624
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30; BAR domains are dimerization, ...
 266-396 2.80e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX7, SNX30, and similar proteins. The specific functions of SNX7 and SNX30 have not been elucidated. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153308  Cd Length: 200  Bit Score: 38.90  E-value: 2.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  266 LLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLK-SKDVKLAEahqq 344
Cdd:cd07624  72 LEGVSSAVERCTAALEVLLSDHEFVFLPPLREYLLYSDAVKDVLKRRDQFQIEYELSVEELNKKRLElLKEVEKLQ---- 147

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 7657599  345 eccQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQS 396
Cdd:cd07624 148 ---DKLECANADLKADLERWKQNKRQDLKKILLDMAEKQIQYYEQCLAAWEE 196
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
 56-168 3.57e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX19 contains an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. These domains are also found in SNX13 and SNX14, which also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNX19 interacts with IA-2, a major autoantigen found in type-1 diabetes. It inhibits the conversion of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to PI(3,4,5)P3, which leads in the decrease of protein phosphorylation in the Akt signaling pathway, resulting in apoptosis. SNX19 may also be implicated in coronary heart disease and thyroid oncocytic tumors.


Pssm-ID: 132803 [Multi-domain]  Cd Length: 132  Bit Score: 37.52  E-value: 3.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599   56 PTFQSPEFSVTRQHEDFVWLHDTLIETTDYAGLIIPPAPTKPDFDGPrekmqklgegEGSMTKEEFAKMKQELEAeylav 135
Cdd:cd06893  44 SEQPLATHTVNRRFREFLTLQTRLEENPKFRKIMNVKGPPKRLFDLP----------FGNMDKDKIEARRGLLET----- 108

                        90       100       110
                ....*....|....*....|....*....|...
gi 7657599  136 fkktvsshevFLQRLSSHPVLSKDRNFHVFLEY 168
Cdd:cd06893 109 ----------FLRQLCSIPEISNSEEVQEFLAY 131
BAR_Atg20p cd07629
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Atg20p; BAR domains are ...
 204-396 5.31e-03

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Atg20p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The function of Atg20p is unknown but it has been shown to interact with Atg11p, which plays a role in linking cargo molecules with vesicle-forming components. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153313  Cd Length: 187  Bit Score: 37.76  E-value: 5.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  204 EVDDFFEQEKNFLINYYNRIKDSCVK-ADKMTRSHKNVADDYIHTAACLHSLALEEPTVikkyllKVAELFEKLrkveGR 282
Cdd:cd07629   1 EPDDEFTDIEAETKKYEQLLHGGMEKvNRRITKRLGDLAEDMADLGGRFNAFSLEEQKS------ELAEALEKV----GQ 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657599  283 VSSDEDLKLTELLRYYMLNIE-----------AAKDLL-YRRTKAlIDYENSNKALDKARL--KSKDVKLAeahqqeccq 348
Cdd:cd07629  71 AVDSTYLATEALVGSLYYNINeplsesaqfagVVRELLkYRKLKH-VQYEMTKDSLLESALvaASDDLVIS--------- 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 7657599  349 kfeqlSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQS 396
Cdd:cd07629 141 -----STIKQKDLPRFQREREADLREILKNYSKYHKDWAKQNLEAWKE 183
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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