NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1721979389|ref|XP_030234747|]
View 

sorting nexin-5 [Gadus morhua]

Protein Classification

PX and BAR domain-containing protein( domain architecture ID 36833)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 180-397 8.41e-127

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


The actual alignment was detected with superfamily member cd07663:

Pssm-ID: 472257  Cd Length: 218  Bit Score: 364.26  E-value: 8.41e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 180 GFFKNMVKTADEVIISGIKEVDDFFEQEKTFLLDYYSKIKDSTIKAEKMTRSHKNVADDYIHISATLSSISADDSTAIKK 259
Cdd:cd07663     1 GFFKNMVKSADEVLFSGVKEVDEFFEQEKTFLVNYYNRIKDSCAKADKMTRSHKNVADDYIHISAALNSVAAEEPTVIKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 260 HFEKLADLFEKLRKVEGRVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKALDKARLKSRDIPQAEEQQQ 339
Cdd:cd07663    81 YLLKVAELFEKLRKVEDRVASDQDLKLTELLRYYMLNIEAAKDLLYRRARALADYENSNKALDKARLKSKDVKQAEAHQQ 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1721979389 340 LCLQKFDKLSESGKRELTSFKGRRVVAFRKNLIEMAELEIKHAKNNVALLQGCIDLMK 397
Cdd:cd07663   161 ECCQKFEKLSESAKQELISFKRRRVAAFRKNLIEMTELEIKHAKNNVSLLQSCIDLFK 218
PX_domain super family cl02563
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 25-164 1.98e-103

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.


The actual alignment was detected with superfamily member cd07291:

Pssm-ID: 470617  Cd Length: 141  Bit Score: 301.98  E-value: 1.98e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  25 ALIIDIPDALCERDKVKFTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLVETEEYAGLIIPPAPPKPDFESPREKMHKL 104
Cdd:cd07291     2 SLQIDIPDALSERDKVKFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETEDYAGLIIPPAPPKPDFDGPREKMQKL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 105 GEGEATMTKEEYTKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPILSKDRNFHIFLEYD 164
Cdd:cd07291    82 GEGEGSMTKEEFAKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEYD 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 ...
 180-397 8.41e-127

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: 364.26  E-value: 8.41e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 180 GFFKNMVKTADEVIISGIKEVDDFFEQEKTFLLDYYSKIKDSTIKAEKMTRSHKNVADDYIHISATLSSISADDSTAIKK 259
Cdd:cd07663     1 GFFKNMVKSADEVLFSGVKEVDEFFEQEKTFLVNYYNRIKDSCAKADKMTRSHKNVADDYIHISAALNSVAAEEPTVIKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 260 HFEKLADLFEKLRKVEGRVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKALDKARLKSRDIPQAEEQQQ 339
Cdd:cd07663    81 YLLKVAELFEKLRKVEDRVASDQDLKLTELLRYYMLNIEAAKDLLYRRARALADYENSNKALDKARLKSKDVKQAEAHQQ 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1721979389 340 LCLQKFDKLSESGKRELTSFKGRRVVAFRKNLIEMAELEIKHAKNNVALLQGCIDLMK 397
Cdd:cd07663   161 ECCQKFEKLSESAKQELISFKRRRVAAFRKNLIEMTELEIKHAKNNVSLLQSCIDLFK 218
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
 25-164 1.98e-103

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: 301.98  E-value: 1.98e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  25 ALIIDIPDALCERDKVKFTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLVETEEYAGLIIPPAPPKPDFESPREKMHKL 104
Cdd:cd07291     2 SLQIDIPDALSERDKVKFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETEDYAGLIIPPAPPKPDFDGPREKMQKL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 105 GEGEATMTKEEYTKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPILSKDRNFHIFLEYD 164
Cdd:cd07291    82 GEGEGSMTKEEFAKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEYD 141
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 175-383 2.17e-13

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: 69.23  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 175 KEMFGGFFKNMVKTADEViisgiKEVDDFFEQEKTFLLDYYSKIKdSTIKAEKMTRSHKNVADDYIH-ISATLSSISA-D 252
Cdd:pfam09325   2 SSLFGKFFSSVSKSSYKF-----NEPDEWFIDKKQYIDSLESQLK-KLYKALELLVSQRKELASATGeFAKSLASLASlE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 253 DSTAIKKHFEKLADLFEKLRKVEGRVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKAL-------DKAR 325
Cdd:pfam09325  76 LSTGLSRALSQLAEVEERIKELLERQALQDVLTLGETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELskkkeqlEKLL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721979389 326 LKSRDIPQ-----------AEEQQQLCLQKFDKLSESGKRELTSFKGRRVVAFRKNLIEMAELEIKHAK 383
Cdd:pfam09325 156 RANKSQNDklqqakkeveeLERRVQQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIESQK 224
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 50-164 2.13e-11

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 59.56  E-value: 2.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  50 LSSFQKPDFSVPRQHEDFIWLHDTLVETeeYAGLIIPPAPPKpdfesprekmhklgegeatmtkeeytKMKQELEAEYLa 129
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRK--FPSVIIPPLPPK--------------------------RWLGRYNEEFI- 51

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1721979389 130 vfKKTVQVHEVFLQRLSSHPILSKDRNFHIFLEYD 164
Cdd:pfam00787  52 --EKRRKGLEQYLQRLLQHPELRNSEVLLEFLESD 84
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 2-385 1.51e-09

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 59.43  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389   2 TTALGESDKEKTRSVSVDLNNDTALIIDIPDALCERDKVKFT-----VHTKTTLSSFQK---PDFSVPRQHEDFIWLHDT 73
Cdd:COG5391   109 SLLLPTSLQPPLSTSHTILDYFISSTVSNPQSLTLLVDSRDKhtsyeIITVTNLPSFQLresRPLVVRRRYSDFESLHSI 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  74 LVetEEYAGLIIPPAPPKPDF-ESPREKMHklgegeatmtkEEYTKMKQELEaeylavfkktvqvhEVFLQRLSSHPILS 152
Cdd:COG5391   189 LI--KLLPLCAIPPLPSKKSNsEYYGDRFS-----------DEFIEERRQSL--------------QNFLRRVSTHPLLS 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 153 KDRNFHIFLEYDQDLTVRRKNAKEMFGGFFKNMVKTADEViISGIKEVD------------DFFEQEKTFLL-----DYY 215
Cdd:COG5391   242 NYKNSKSWESHSTLLSSFIENRKSVPTPLSLDLTSTTQEL-DMERKELNestskaihnilsIFSLFEKILIQleseeESL 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 216 SKIKDSTIKAEKMTRSHKNVADDYIH--ISATLSSISADDSTAIKKHFEKLADLFEKLRKVEGRVASDQELKLTELLRYY 293
Cdd:COG5391   321 TRLLESLNNLLLLVLNFSGVFAKRLEqnQNSILNEGVVQAETLRSSLKELLTQLQDEIKSRESLILTDSNLEKLTDQNLE 400

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 294 MRDIQAAKDLLYRRARA--LADYENSNKALDKARL-------KSR---------DIPQAEEQQQLCLQKFDKLSESGKRE 355
Cdd:COG5391   401 DVEELSRSLRKNSSQRAvvSQQPEGLTSFSKLSYKlrdfvqeKSRsksieslqqDKEKLEEQLAIAEKDAQEINEELKNE 480

                         410       420       430
                  ....*....|....*....|....*....|
gi 1721979389 356 LTSFKGRRVVAFRKNLIEMAELEIKHAKNN 385
Cdd:COG5391   481 LKFFFSVRNSDLEKILKSVADSHIEWAEEN 510
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 42-162 1.27e-04

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: 40.79  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389   42 FTVHTKTTLSSFQkpdfsVPRQHEDFIWLHDTLveTEEYAGLIIPPAPPKpdfesprekmhKLGEGEATMTKEEYTKMKQ 121
Cdd:smart00312  17 IEIETKTGLEEWT-----VSRRYSDFLELHSKL--KKHFPRSILPPLPGK-----------KLFGRLNNFSEEFIEKRRR 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1721979389  122 ELEaeylavfkktvqvheVFLQRLSSHPILSK-DRNFHIFLE 162
Cdd:smart00312  79 GLE---------------KYLQSLLNHPELINhSEVVLEFLE 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 ...
 180-397 8.41e-127

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: 364.26  E-value: 8.41e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 180 GFFKNMVKTADEVIISGIKEVDDFFEQEKTFLLDYYSKIKDSTIKAEKMTRSHKNVADDYIHISATLSSISADDSTAIKK 259
Cdd:cd07663     1 GFFKNMVKSADEVLFSGVKEVDEFFEQEKTFLVNYYNRIKDSCAKADKMTRSHKNVADDYIHISAALNSVAAEEPTVIKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 260 HFEKLADLFEKLRKVEGRVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKALDKARLKSRDIPQAEEQQQ 339
Cdd:cd07663    81 YLLKVAELFEKLRKVEDRVASDQDLKLTELLRYYMLNIEAAKDLLYRRARALADYENSNKALDKARLKSKDVKQAEAHQQ 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1721979389 340 LCLQKFDKLSESGKRELTSFKGRRVVAFRKNLIEMAELEIKHAKNNVALLQGCIDLMK 397
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, ...
 180-397 3.74e-114

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: 332.37  E-value: 3.74e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 180 GFFKNMVKTADE-VIISGIKEVDDFFEQEKTFLLDYYSKIKDSTIKAEKMTRSHKNVADDYIHISATLSSISADDSTAIK 258
Cdd:cd07621     1 GFLKSISKSADEeLLLSGQKDVDEFFEQEKNFLVEYHNRIKDATAKADKMTRKHKDVADSYIKISAALTQLATSEPTPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 259 KHFEKLADLFEKLRKVEGRVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKALDKARLKSRDIPQAEEQQ 338
Cdd:cd07621    81 KFLLKVAETFEKLRKLEGRVASDEDLKLSDTLRYYMRDTQAAKDLLYRRLRCLANYENANKNLEKARAKNKDVHAAEAAQ 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1721979389 339 QLCLQKFDKLSESGKRELTSFKGRRVVAFRKNLIEMAELEIKHAKNNVALLQGCIDLMK 397
Cdd:cd07621   161 QEACEKFESMSESAKQELLDFKTRRVAAFRKNLVELAELEIKHAKAQIQLLKNCLAALK 219
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
 25-164 1.98e-103

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: 301.98  E-value: 1.98e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  25 ALIIDIPDALCERDKVKFTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLVETEEYAGLIIPPAPPKPDFESPREKMHKL 104
Cdd:cd07291     2 SLQIDIPDALSERDKVKFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETEDYAGLIIPPAPPKPDFDGPREKMQKL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 105 GEGEATMTKEEYTKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPILSKDRNFHIFLEYD 164
Cdd:cd07291    82 GEGEGSMTKEEFAKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEYD 141
BAR_SNX6 cd07662
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid ...
 181-397 1.96e-91

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: 274.61  E-value: 1.96e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 181 FFKNMVKTADEVIISGIKEVDDFFEQEKTFLLDYYSKIKDSTIKAEKMTRSHKNVADDYIHISATLSSISADDSTAIKKH 260
Cdd:cd07662     2 FFKNVVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDSSAKSDRMTRSHKSAADDYNRIGSSLYTLGTQDSTDICKF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 261 FEKLADLFEKLRKVEGRVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKALDKARLKSRDIPQAEEQQQL 340
Cdd:cd07662    82 FLKVSELFDKTRKIEARVAADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETTQQL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1721979389 341 CLQKFDKLSESGKRELTSFKGRRVVAFRKNLIEMAELEIKHAKNNVALLQGCIDLMK 397
Cdd:cd07662   162 CCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQSCLAVLN 218
PX_SNX5_like cd06892
The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is ...
 24-164 5.02e-83

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: 250.04  E-value: 5.02e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  24 TALIIDIPDALCERDKVKFTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLVETEEYAGLIIPPAPPKPDFESPREKMHK 103
Cdd:cd06892     1 SSLQVDISDALSERDKVKFTVHTKTTLPTFQKPEFSVTRQHEEFVWLHDTLVENEDYAGLIIPPAPPKPDFDASREKLQK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721979389 104 LGEGEATMTKEEYTKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPILSKDRNFHIFLEYD 164
Cdd:cd06892    81 LGEGEGSMTKEEFEKMKQELEAEYLAIFKKTVAMHEVFLRRLASHPVLRNDANFRVFLEYE 141
PX_SNX6 cd07292
The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a ...
 25-164 5.83e-69

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: 214.19  E-value: 5.83e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  25 ALIIDIPDALCERDKVKFTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLVETEEYAGLIIPPAPPKPDFESPREKMHKL 104
Cdd:cd07292     2 ALQVDISDALSERDKVKFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPDFDASREKLQKL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 105 GEGEATMTKEEYTKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPILSKDRNFHIFLEYD 164
Cdd:cd07292    82 GEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 141
BAR_SNX_like cd07630
The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized Sorting Nexins; BAR domains are ...
 199-393 2.96e-23

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: 96.04  E-value: 2.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 199 EVDDFFEQEKTFLLDYYSKIKDSTIKAEKMTRSHKNVADDYIHISATLSSISADD---STAIKKHFEKLADLFEKLRKVE 275
Cdd:cd07630     1 DVDEFFQKERDMNTKLSANMKEAAEKFLKIVNTEQRLANALGHLSSSLQLCVGLDeasVVALNRLCTKLSEALEEAKENI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 276 GRVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKALDKARLKSRDipQAEEQQQLCLQKFDKLSESGKRE 355
Cdd:cd07630    81 EVVAGNNENTLGLTLDLYSRYSESEKDMLFRRTCKLIEFENASKALEKAKPQKKE--QAEEAKKKAETEFEEISSLAKKE 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1721979389 356 LTSFKGRRVVAFRKNLIEMAELEIKHAKNNVALLQGCI 393
Cdd:cd07630   159 LERFHRQRVLELQSALVCYAESQIKNAKEAAAVLTKTL 196
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 199-393 5.31e-21

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: 90.49  E-value: 5.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 199 EVDDFFEQEKTFLLDYYSKIKDSTIKAEKMTRSHKNVADDYIHISATLSSISADDSTA---IKKHFEKLADLFEKLRKVE 275
Cdd:cd07596     1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEVggeLGEALSKLGKAAEELSSLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 276 GRVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKALDKARLK------------------SRDIPQAEEQ 337
Cdd:cd07596    81 EAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQleklkaapgikpakveelEEELEEAESA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1721979389 338 QQLCLQKFDKLSESGKRELTSFKGRRVVAFRKNLIEMAELEIKHAKNNVALLQGCI 393
Cdd:cd07596   161 LEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLL 216
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 40-164 1.15e-19

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: 83.78  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  40 VKFTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLVetEEYAGLIIPPAPPKPDFESPREKMHKLGEGEATMtkeeytkm 119
Cdd:cd06859    19 VVYRVTTKTNLPDFKKSEFSVLRRYSDFLWLYERLV--EKYPGRIVPPPPEKQAVGRFKVKFEFIEKRRAAL-------- 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1721979389 120 kqeleaeylavfkktvqvhEVFLQRLSSHPILSKDRNFHIFLEYD 164
Cdd:cd06859    89 -------------------ERFLRRIAAHPVLRKDPDFRLFLESD 114
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
 40-161 8.15e-15

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: 70.06  E-value: 8.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  40 VKFTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLVEteEYAGLIIPPAPPKpdfesprekmHKLgegeatmtKEEYTKM 119
Cdd:cd06860    19 ITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEE--SHPTHIIPPLPEK----------HSV--------KGLLDRF 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1721979389 120 KQE-LEAEYLAVFKktvqvhevFLQRLSSHPILSKDRNFHIFL 161
Cdd:cd06860    79 SPEfVATRMRALHK--------FLNRIVEHPVLSFNEHLKVFL 113
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 175-383 2.17e-13

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: 69.23  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 175 KEMFGGFFKNMVKTADEViisgiKEVDDFFEQEKTFLLDYYSKIKdSTIKAEKMTRSHKNVADDYIH-ISATLSSISA-D 252
Cdd:pfam09325   2 SSLFGKFFSSVSKSSYKF-----NEPDEWFIDKKQYIDSLESQLK-KLYKALELLVSQRKELASATGeFAKSLASLASlE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 253 DSTAIKKHFEKLADLFEKLRKVEGRVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKAL-------DKAR 325
Cdd:pfam09325  76 LSTGLSRALSQLAEVEERIKELLERQALQDVLTLGETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELskkkeqlEKLL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721979389 326 LKSRDIPQ-----------AEEQQQLCLQKFDKLSESGKRELTSFKGRRVVAFRKNLIEMAELEIKHAK 383
Cdd:pfam09325 156 RANKSQNDklqqakkeveeLERRVQQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIESQK 224
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
 40-164 3.40e-13

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: 65.45  E-value: 3.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  40 VKFTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLVETeeYAGLIIPPAPPKpdfesprekmHKLGEGEAtmtkeeytkm 119
Cdd:cd06861    19 TVYTVRTRTTSPNFEVSSFSVLRRYRDFRWLYRQLQNN--HPGVIVPPPPEK----------QSVGRFDD---------- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1721979389 120 kQELEAEYLAVfkktvqvhEVFLQRLSSHPILSKDRNFHIFLEYD 164
Cdd:cd06861    77 -NFVEQRRAAL--------EKMLRKIANHPVLQKDPDFRLFLESE 112
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
 42-162 8.54e-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: 64.69  E-value: 8.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  42 FTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLVETEEYAGLIIPPAPPKPDFespreKMHKLGEGEATMTKEEYTKMKQ 121
Cdd:cd07282    21 YRVTTKTSLSMFSRSEFSVRRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIV-----GMTKVKVGKEDSSSTEFVEKRR 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1721979389 122 eleaeylavfkktvQVHEVFLQRLSSHPILSKDRNFHIFLE 162
Cdd:cd07282    96 --------------AALERYLQRTVKHPTLLQDPDLRQFLE 122
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
 40-162 4.48e-12

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: 62.69  E-value: 4.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  40 VKFTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLVetEEYAGLIIPPAPPKPDFESPRekmhklGEgeaTMTKEEYTKM 119
Cdd:cd06863    20 ISYLITTKTNLPSFSRKEFKVRRRYSDFVFLHECLS--NDFPACVVPPLPDKHRLEYIT------GD---RFSPEFITRR 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1721979389 120 KQELEAeylavfkktvqvhevFLQRLSSHPILSKDRNFHIFLE 162
Cdd:cd06863    89 AQSLQR---------------FLRRISLHPVLSQSKILHQFLE 116
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 50-164 2.13e-11

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 59.56  E-value: 2.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  50 LSSFQKPDFSVPRQHEDFIWLHDTLVETeeYAGLIIPPAPPKpdfesprekmhklgegeatmtkeeytKMKQELEAEYLa 129
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRK--FPSVIIPPLPPK--------------------------RWLGRYNEEFI- 51

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1721979389 130 vfKKTVQVHEVFLQRLSSHPILSKDRNFHIFLEYD 164
Cdd:pfam00787  52 --EKRRKGLEQYLQRLLQHPELRNSEVLLEFLESD 84
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 40-164 2.04e-10

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: 58.15  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  40 VKFTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLVETEEYAGLIIPPAPPKPDFespreKMHKLGEGEATMTKEEYtkm 119
Cdd:cd07281    19 VVYKVTTQTSLLMFRSKHFTVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEKSLI-----GMTKVKVGKEDSSSAEF--- 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1721979389 120 kqeLEAEYLAVfkktvqvhEVFLQRLSSHPILSKDRNFHIFLEYD 164
Cdd:cd07281    91 ---LERRRAAL--------ERYLQRIVSHPSLLQDPDVREFLEKE 124
BAR_SNX1_2 cd07623
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, ...
 243-391 1.37e-09

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: 57.67  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 243 SATLSSisADDSTAIKKHFEKLADLFEKLRKVEGRVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKALD 322
Cdd:cd07623    56 AAMLSN--CEEHTSLSRALSQLAEVEEKIEQLHGEQADTDFYILAELLKDYIGLIGAIKDVFHERVKVWQNWQNAQQTLT 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 323 KAR-LKSR---------------DIPQAEEQQQLCLQKFDKLSESGKRELTSFKGRRVVAFRKNLIEMAELEIKHAKNNV 386
Cdd:cd07623   134 KKReAKAKlelsgrtdkldqaqqEIKEWEAKVDRGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYLESLLNTQQQLI 213


                  ....*
gi 1721979389 387 ALLQG 391
Cdd:cd07623   214 KYWEA 218
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 2-385 1.51e-09

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 59.43  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389   2 TTALGESDKEKTRSVSVDLNNDTALIIDIPDALCERDKVKFT-----VHTKTTLSSFQK---PDFSVPRQHEDFIWLHDT 73
Cdd:COG5391   109 SLLLPTSLQPPLSTSHTILDYFISSTVSNPQSLTLLVDSRDKhtsyeIITVTNLPSFQLresRPLVVRRRYSDFESLHSI 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  74 LVetEEYAGLIIPPAPPKPDF-ESPREKMHklgegeatmtkEEYTKMKQELEaeylavfkktvqvhEVFLQRLSSHPILS 152
Cdd:COG5391   189 LI--KLLPLCAIPPLPSKKSNsEYYGDRFS-----------DEFIEERRQSL--------------QNFLRRVSTHPLLS 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 153 KDRNFHIFLEYDQDLTVRRKNAKEMFGGFFKNMVKTADEViISGIKEVD------------DFFEQEKTFLL-----DYY 215
Cdd:COG5391   242 NYKNSKSWESHSTLLSSFIENRKSVPTPLSLDLTSTTQEL-DMERKELNestskaihnilsIFSLFEKILIQleseeESL 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 216 SKIKDSTIKAEKMTRSHKNVADDYIH--ISATLSSISADDSTAIKKHFEKLADLFEKLRKVEGRVASDQELKLTELLRYY 293
Cdd:COG5391   321 TRLLESLNNLLLLVLNFSGVFAKRLEqnQNSILNEGVVQAETLRSSLKELLTQLQDEIKSRESLILTDSNLEKLTDQNLE 400

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 294 MRDIQAAKDLLYRRARA--LADYENSNKALDKARL-------KSR---------DIPQAEEQQQLCLQKFDKLSESGKRE 355
Cdd:COG5391   401 DVEELSRSLRKNSSQRAvvSQQPEGLTSFSKLSYKlrdfvqeKSRsksieslqqDKEKLEEQLAIAEKDAQEINEELKNE 480

                         410       420       430
                  ....*....|....*....|....*....|
gi 1721979389 356 LTSFKGRRVVAFRKNLIEMAELEIKHAKNN 385
Cdd:COG5391   481 LKFFFSVRNSDLEKILKSVADSHIEWAEEN 510
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
 41-161 9.54e-09

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: 53.19  E-value: 9.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  41 KFTVHTKttLSSFQKPDFSVPRQHEDFIWLHDTLveTEEYAGLIIPPAPPKPDFESPRekmhklgegeatMTKEEYtkmk 120
Cdd:cd06865    27 KVTTRTN--IPSYTHGEFTVRRRFRDVVALADRL--AEAYRGAFVPPRPDKSVVESQV------------MQSAEF---- 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1721979389 121 qeleaeylaVFKKTVQVhEVFLQRLSSHPILSKDRNFHIFL 161
Cdd:cd06865    87 ---------IEQRRVAL-EKYLNRLAAHPVIGLSDELRVFL 117
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
 40-161 2.54e-08

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: 51.90  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  40 VKFTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLveTEEYAGLIIPPAPpkpdfesprEKMHKLGegeatmtkeeytkM 119
Cdd:cd07284    19 ITYRVMTKTSRSEFDSSEFEVRRRYQDFLWLKGRL--EEAHPTLIIPPLP---------EKFVMKG-------------M 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1721979389 120 KQELEAEYLAVFKKTVQVhevFLQRLSSHPILSKDRNFHIFL 161
Cdd:cd07284    75 VERFNEDFIETRRKALHK---FLNRIADHPTLTFNEDFKIFL 113
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 38-162 1.14e-07

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: 49.66  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  38 DKVKFTVHTKTTLssfqKPDFSVPRQHEDFIWLHDTLVETeeYAGLIIPPAPPKPDFESprekmhklgegeatMTKEEYT 117
Cdd:cd06093    16 KYVVYIIEVTTQG----GEEWTVYRRYSDFEELHEKLKKK--FPGVILPPLPPKKLFGN--------------LDPEFIE 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1721979389 118 KMKQELEAeylavfkktvqvhevFLQRLSSHPILSKDRNFHIFLE 162
Cdd:cd06093    76 ERRKQLEQ---------------YLQSLLNHPELRNSEELKEFLE 105
PX_SNX30 cd07283
The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; The PX domain is a ...
 40-161 1.13e-06

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: 47.00  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  40 VKFTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDTLVETEEYAglIIPPAPPKpdfesprekmhKLGEGEATMTKEEYTKM 119
Cdd:cd07283    19 ITYRVTTKTTRTEFDLPEYSVRRRYQDFDWLRNKLEESQPTH--LIPPLPEK-----------FVVKGVVDRFSEEFVET 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1721979389 120 KQeleaeylavfkktvQVHEVFLQRLSSHPILSKDRNFHIFL 161
Cdd:cd07283    86 RR--------------KALDKFLKRIADHPVLSFNEHFNVFL 113
BAR_SNX2 cd07664
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid ...
 187-376 2.61e-05

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: 45.04  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 187 KTADEVIISGIK--EVDDFFEQEKTFLLDYYSKIKDSTIKAEKMTRSHKNVADDYIHISATLSSI-SADDSTAIKKHFEK 263
Cdd:cd07664     5 KAADAVNKMTIKmnESDAWFEEKQQQFENLDQQLRKLHASVESLVCHRKELSANTAAFAKSAAMLgNSEDHTALSRALSQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 264 LADLFEKLRKVEGRVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKAL----------------DKARLK 327
Cdd:cd07664    85 LAEVEEKIDQLHQDQAFADFYLFSELLGDYIRLIAAVKGVFDQRMKCWQKWQDAQVTLqkkreaeaklqyankpDKLQQA 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1721979389 328 SRDIPQAEEQQQLCLQKFDKLSESGKRELTSFKGRRVVAFRKNLIEMAE 376
Cdd:cd07664   165 KDEIKEWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLE 213
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 42-162 1.27e-04

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: 40.79  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389   42 FTVHTKTTLSSFQkpdfsVPRQHEDFIWLHDTLveTEEYAGLIIPPAPPKpdfesprekmhKLGEGEATMTKEEYTKMKQ 121
Cdd:smart00312  17 IEIETKTGLEEWT-----VSRRYSDFLELHSKL--KKHFPRSILPPLPGK-----------KLFGRLNNFSEEFIEKRRR 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1721979389  122 ELEaeylavfkktvqvheVFLQRLSSHPILSK-DRNFHIFLE 162
Cdd:smart00312  79 GLE---------------KYLQSLLNHPELINhSEVVLEFLE 105
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
 53-161 4.00e-04

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: 40.04  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  53 FQKPDfSVPRQHEDFIWLHDTLVETeeYAGLIIPPAPpkpdfESPREKMHKLGEGEaTMTKEEYTKMKQELEAeylavfk 132
Cdd:cd06864    42 SKKLS-SLWRRYSEFELLRNYLVVT--YPYVIVPPLP-----EKRAMFMWQKLSSD-TFDPDFVERRRAGLEN------- 105

                          90       100
                  ....*....|....*....|....*....
gi 1721979389 133 ktvqvhevFLQRLSSHPILSKDRNFHIFL 161
Cdd:cd06864   106 --------FLLRVAGHPELCQDKIFLEFL 126
BAR_Vps5p cd07627
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ...
 199-371 1.11e-03

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: 39.98  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 199 EVDDFFEQEKTFLLDYYSKIKdSTIKAEKMTRSHKNVADDYIH-ISATLSSISADD-STAIKKHFEKLADLFEKLRKVEG 276
Cdd:cd07627     1 EPDEWFIEKKQYLDSLESQLK-QLYKSLELVSSQRKELASATEeFAETLEALSSLElSKSLSDLLAALAEVQKRIKESLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 277 RVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKALDKARLK------------------SRDIPQAEEQQ 338
Cdd:cd07627    80 RQALQDVLTLGVTLDEYIRSIGSVRAAFAQRQKLWQYWQSAESELSKKKAQleklkrqgktqqeklnslLSELEEAERRA 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1721979389 339 QLCLQKFDKLSESGKRELTSFKGRRVVAFRKNL 371
Cdd:cd07627   160 SELKKEFEEVSELIKSELERFERERVEDFRNSV 192
PX_SNX12 cd07294
The phosphoinositide binding Phox Homology domain of Sorting Nexin 12; The PX domain is a ...
 42-162 1.28e-03

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: 38.87  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389  42 FTVHTKTTLSSFQKPDFSVPRQHEDFIWLHDtlvETEEYAGLIIPPAPPKPdfeSPREKMHKLGEG--EATMTKEEYTKM 119
Cdd:cd07294    24 YEVRMRTNLPIFKLKESCVRRRYSDFEWLKN---ELERDSKIVVPPLPGKA---LKRQLPFRGDEGifEESFIEERRQGL 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1721979389 120 KQeleaeylavfkktvqvhevFLQRLSSHPILSKDRNFHIFLE 162
Cdd:cd07294    98 EQ-------------------FINKIAGHPLAQNERCLHMFLQ 121
BAR_SNX1 cd07665
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; BAR domains are dimerization, lipid ...
 183-376 1.51e-03

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: 39.67  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 183 KNMVKTADEVIISGIK--EVDDFFEQEKTFLLDYYSKIKDSTIKAEKMTRSHKNVADDYIHISATLSSI-SADDSTAIKK 259
Cdd:cd07665     1 KMFNKATDAVSKMTIKmnESDVWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTALFAKSLAMLgSSEDNTALSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 260 HFEKLADLFEKLRKVEGRVASDQELKLTELLRYYMRDIQAAKDLLYRRARALADYENSNKALDKARLKSRDIPQAEEQQQ 339
Cdd:cd07665    81 ALSQLAEVEEKIEQLHQEQANNDFFLLAELLADYIRLLSAVRGAFDQRMKTWQRWQDAQAMLQKKREAEARLLWANKPDK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1721979389 340 LCLQK----------------FDKLSESGKRELTSFKGRRVVAFRKNLIEMAE 376
Cdd:cd07665   161 LQQAKdeiaewesrvtqyerdFERISATVRKEVIRFEKEKSKDFKNHIIKYLE 213
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 217-380 2.80e-03

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 38.58  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 217 KIKDSTIKAEKMTRSHKNVADDYIHISATLSSISADD----STAIKKHFEKLADLFEKLRKVEGRVASDQELKLTELLR- 291
Cdd:cd07307     8 LLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELpdlsNTDLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKe 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721979389 292 YYMRDIQAAKDLLYRRARALADYENSNKALDKARLKSRD---IPQAEEQQQLCLQKFDKLSESGKRELTSFKGRRVVAFR 368
Cdd:cd07307    88 YLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDsskLAEAEEELQEAKEKYEELREELIEDLNKLEEKRKELFL 167

                         170
                  ....*....|..
gi 1721979389 369 KNLIEMAELEIK 380
Cdd:cd07307   168 SLLLSFIEAQSE 179
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH