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Conserved domains on  [gi|23111026|ref|NP_037455|]
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sorting nexin-11 isoform 1 [Homo sapiens]

Protein Classification

PX domain-containing protein( domain architecture ID 10160897)

PX (Phox Homology) domain-containing protein may bind phosphoinositides and may function in targeting proteins to membranes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
 18-129 8.49e-60

The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; 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. SNX10 may be involved in the regulation of endosome homeostasis. Its expression induces the formation of giant vacuoles in mammalian cells.


:

Pssm-ID: 132808  Cd Length: 113  Bit Score: 185.23  E-value: 8.49e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  18 TVRVQDPRVQNEGSWNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDE-FI 96
Cdd:cd06898   1 SVEVRDPRTHKEDDWGSYTDYEIFLHTNSMCFTLKTSCVRRRYSEFVWLRNRLQKNALLIQLPSLPPKNLFGRFNNEgFI 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 23111026  97 EKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQSQ 129
Cdd:cd06898  81 EERQQGLQDFLEKVLQTPLLLSDSRLHLFLQTQ 113
 
Name Accession Description Interval E-value
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
 18-129 8.49e-60

The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; 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. SNX10 may be involved in the regulation of endosome homeostasis. Its expression induces the formation of giant vacuoles in mammalian cells.


Pssm-ID: 132808  Cd Length: 113  Bit Score: 185.23  E-value: 8.49e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  18 TVRVQDPRVQNEGSWNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDE-FI 96
Cdd:cd06898   1 SVEVRDPRTHKEDDWGSYTDYEIFLHTNSMCFTLKTSCVRRRYSEFVWLRNRLQKNALLIQLPSLPPKNLFGRFNNEgFI 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 23111026  97 EKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQSQ 129
Cdd:cd06898  81 EERQQGLQDFLEKVLQTPLLLSDSRLHLFLQTQ 113
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 49-129 6.38e-28

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 102.32  E-value: 6.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026    49 FTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQS 128
Cdd:pfam00787   4 FSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFLES 83


                  .
gi 23111026   129 Q 129
Cdd:pfam00787  84 D 84
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 33-127 3.03e-20

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: 83.16  E-value: 3.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026     33 NSYVDYKIFLHTNSKAFTaktscVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGT---SDEFIEKRRQGLQHFLEK 109
Cdd:smart00312  12 HYYYVIEIETKTGLEEWT-----VSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGRLnnfSEEFIEKRRRGLEKYLQS 86

                           90
                   ....*....|....*....
gi 23111026    110 VLQSVVLLSDS-QLHLFLQ 127
Cdd:smart00312  87 LLNHPELINHSeVVLEFLE 105
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 17-174 1.67e-12

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 66.74  E-value: 1.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  17 ITVRVQDPRVQNEGSWNSYVDYKIFLHTNSKAFTAKTSC---VRRRYREFVWLRKQLQRNAGLVPVPELPGK---STFFG 90
Cdd:COG5391 133 STVSNPQSLTLLVDSRDKHTSYEIITVTNLPSFQLRESRplvVRRRYSDFESLHSILIKLLPLCAIPPLPSKksnSEYYG 212

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  91 T--SDEFIEKRRQGLQHFLEKV-----LQSVVLLSDSQLHL-----FLQSQLSVPEieacvqgrstmTVSDAILRYAMSN 158
Cdd:COG5391 213 DrfSDEFIEERRQSLQNFLRRVsthplLSNYKNSKSWESHStllssFIENRKSVPT-----------PLSLDLTSTTQEL 281

                       170
                ....*....|....*.
gi 23111026 159 CGWAQEERQSSSHLAK 174
Cdd:COG5391 282 DMERKELNESTSKAIH 297
 
Name Accession Description Interval E-value
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
 18-129 8.49e-60

The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; 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. SNX10 may be involved in the regulation of endosome homeostasis. Its expression induces the formation of giant vacuoles in mammalian cells.


Pssm-ID: 132808  Cd Length: 113  Bit Score: 185.23  E-value: 8.49e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  18 TVRVQDPRVQNEGSWNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDE-FI 96
Cdd:cd06898   1 SVEVRDPRTHKEDDWGSYTDYEIFLHTNSMCFTLKTSCVRRRYSEFVWLRNRLQKNALLIQLPSLPPKNLFGRFNNEgFI 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 23111026  97 EKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQSQ 129
Cdd:cd06898  81 EERQQGLQDFLEKVLQTPLLLSDSRLHLFLQTQ 113
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 49-129 6.38e-28

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 102.32  E-value: 6.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026    49 FTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQS 128
Cdd:pfam00787   4 FSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFLES 83


                  .
gi 23111026   129 Q 129
Cdd:pfam00787  84 D 84
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 18-128 1.15e-26

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: 100.12  E-value: 1.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  18 TVRVQDPRVQNEGSwNSYVDYKIFLHTNSKaftaKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFIE 97
Cdd:cd06093   1 SVSIPDYEKVKDGG-KKYVVYIIEVTTQGG----EEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNLDPEFIE 75

                        90       100       110
                ....*....|....*....|....*....|.
gi 23111026  98 KRRQGLQHFLEKVLQSVVLLSDSQLHLFLQS 128
Cdd:cd06093  76 ERRKQLEQYLQSLLNHPELRNSEELKEFLEL 106
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 17-129 2.90e-25

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: 96.49  E-value: 2.90e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  17 ITVRVQDPRVQNEGSwNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQ-RNAGLVpVPELPGKSTF--FGTSD 93
Cdd:cd06859   1 FEISVTDPVKVGDGM-SAYVVYRVTTKTNLPDFKKSEFSVLRRYSDFLWLYERLVeKYPGRI-VPPPPEKQAVgrFKVKF 78

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 23111026  94 EFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQSQ 129
Cdd:cd06859  79 EFIEKRRAALERFLRRIAAHPVLRKDPDFRLFLESD 114
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
 17-128 2.45e-23

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: 91.58  E-value: 2.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  17 ITVRVQDPRVQNEGSWNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTF-------F 89
Cdd:cd06863   1 LECLVSDPQKELDGSSDTYISYLITTKTNLPSFSRKEFKVRRRYSDFVFLHECLSNDFPACVVPPLPDKHRLeyitgdrF 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 23111026  90 gtSDEFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQS 128
Cdd:cd06863  81 --SPEFITRRAQSLQRFLRRISLHPVLSQSKILHQFLES 117
PX_SNX3 cd07293
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a ...
 17-130 2.97e-21

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: 86.20  E-value: 2.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  17 ITVRVQDPRVQNEGSwNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVpVPELPGKSTFFGT----- 91
Cdd:cd07293   2 LEIDVTNPQTVGVGR-GRFTTYEIRLKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVV-VPPLPGKALFRQLpfrgd 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 23111026  92 ----SDEFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQSQL 130
Cdd:cd07293  80 dgifDDSFIEERKQGLEQFLNKVAGHPLAQNERCLHMFLQDEI 122
PX_SNX3_like cd06894
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3 and related proteins; The ...
 33-129 3.20e-21

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: 86.36  E-value: 3.20e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  33 NSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVpVPELPGKS-----TFFGT----SDEFIEKRRQGL 103
Cdd:cd06894  17 KRFTDYEVRMRTNLPVFKKKESSVRRRYSDFEWLRSELERDSKIV-VPPLPGKAlkrqlPFRGDdgifEEEFIEERRKGL 95

                        90       100
                ....*....|....*....|....*.
gi 23111026 104 QHFLEKVLQSVVLLSDSQLHLFLQSQ 129
Cdd:cd06894  96 ETFINKVAGHPLAQNEKCLHMFLQEE 121
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
 19-126 6.89e-21

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: 85.08  E-value: 6.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  19 VRVQDPRvQNEGSWNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGT----SDE 94
Cdd:cd06860   3 ITVDNPE-KHVTTLETYITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSVKGLldrfSPE 81

                        90       100       110
                ....*....|....*....|....*....|..
gi 23111026  95 FIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFL 126
Cdd:cd06860  82 FVATRMRALHKFLNRIVEHPVLSFNEHLKVFL 113
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 33-127 3.03e-20

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: 83.16  E-value: 3.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026     33 NSYVDYKIFLHTNSKAFTaktscVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGT---SDEFIEKRRQGLQHFLEK 109
Cdd:smart00312  12 HYYYVIEIETKTGLEEWT-----VSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGRLnnfSEEFIEKRRRGLEKYLQS 86

                           90
                   ....*....|....*....
gi 23111026    110 VLQSVVLLSDS-QLHLFLQ 127
Cdd:smart00312  87 LLNHPELINHSeVVLEFLE 105
PX_Grd19 cd07295
The phosphoinositide binding Phox Homology domain of fungal Grd19; The PX domain is a ...
 19-128 1.19e-18

The phosphoinositide binding Phox Homology domain of fungal Grd19; 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. Grd19 is involved in the localization of late Golgi membrane proteins in yeast. 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: 132828  Cd Length: 116  Bit Score: 79.08  E-value: 1.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  19 VRVQDPRVQNEGSwNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFIEK 98
Cdd:cd07295   4 IEVRNPKTHGIGR-GMFTDYEIVCRTNIPAFKLRVSSVRRRYSDFEYFRDILERESPRVMIPPLPGKIFTNRFSDEVIEE 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 23111026  99 RRQGLQHFLEKVLQSVVLLSDSQ-LHLFLQS 128
Cdd:cd07295  83 RRQGLETFLQSVAGHPLLQTGSKvLAAFLQD 113
PX_SNX12 cd07294
The phosphoinositide binding Phox Homology domain of Sorting Nexin 12; The PX domain is a ...
 17-129 4.00e-18

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: 78.16  E-value: 4.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  17 ITVRVQDPRVQNEGSwNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVpVPELPGKS-----TFFGT 91
Cdd:cd07294   4 LEIDIFNPQTVGVGR-NRFTTYEVRMRTNLPIFKLKESCVRRRYSDFEWLKNELERDSKIV-VPPLPGKAlkrqlPFRGD 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 23111026  92 ----SDEFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQSQ 129
Cdd:cd07294  82 egifEESFIEERRQGLEQFINKIAGHPLAQNERCLHMFLQDE 123
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
 19-129 4.62e-18

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: 77.39  E-value: 4.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  19 VRVQDP-RVQNEGSwnSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFIE 97
Cdd:cd06861   3 ITVGDPhKVGDLTS--AHTVYTVRTRTTSPNFEVSSFSVLRRYRDFRWLYRQLQNNHPGVIVPPPPEKQSVGRFDDNFVE 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 23111026  98 KRRQGLQHFLEKVLQSVVLLSDSQLHLFLQSQ 129
Cdd:cd06861  81 QRRAALEKMLRKIANHPVLQKDPDFRLFLESE 112
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
 18-129 5.96e-17

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: 74.76  E-value: 5.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  18 TVRVQDPRVQNE-----GSWNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGT- 91
Cdd:cd06865   1 KITVSDPKKEQEpsrvpLGGPPYISYKVTTRTNIPSYTHGEFTVRRRFRDVVALADRLAEAYRGAFVPPRPDKSVVESQv 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 23111026  92 --SDEFIEKRRQGLQHFLEK-VLQSVVLLSDsQLHLFLQSQ 129
Cdd:cd06865  81 mqSAEFIEQRRVALEKYLNRlAAHPVIGLSD-ELRVFLTLQ 120
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 17-129 1.81e-14

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: 68.16  E-value: 1.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  17 ITVRVQDPRVQNEGsWNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQL----QRNAGLVPVPelPGKSTFFGT- 91
Cdd:cd07281   1 LKVSITDPEKIGDG-MNAYVVYKVTTQTSLLMFRSKHFTVKRRFSDFLGLYEKLsekhSQNGFIVPPP--PEKSLIGMTk 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 23111026  92 ---------SDEFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQSQ 129
Cdd:cd07281  78 vkvgkedssSAEFLERRRAALERYLQRIVSHPSLLQDPDVREFLEKE 124
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
 17-128 3.90e-14

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: 67.39  E-value: 3.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  17 ITVRVQDPRVQNEGsWNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQR---NAGLVpVPELPGKSTFFGT-- 91
Cdd:cd07282   1 IEIGVSDPEKVGDG-MNAYMAYRVTTKTSLSMFSRSEFSVRRRFSDFLGLHSKLASkylHVGYI-VPPAPEKSIVGMTkv 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 23111026  92 --------SDEFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQS 128
Cdd:cd07282  79 kvgkedssSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLES 123
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
 26-111 4.16e-14

The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of YPT35 proteins from the fungal subkingdom Dikarya. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of YPT35 binds to phosphatidylinositol 3-phosphate (PI3P). It also serves as a protein interaction domain, binding to members of the Yip1p protein family, which localize to the ER and Golgi. YPT35 is mainly associated with endosomes and together with Yip1p proteins, may be involved in a specific function in the endocytic pathway.


Pssm-ID: 132813  Cd Length: 120  Bit Score: 66.97  E-value: 4.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  26 VQNEGSWNSYVDYKIFLHTNSKAFTAKTScvRRRYREFVWLRKQLQR---NAGLVPVPELPGKSTFFGT----SDEFIEK 98
Cdd:cd07280  13 VGGDTGGGAYVVWKITIETKDLIGSSIVA--YKRYSEFVQLREALLDefpRHKRNEIPQLPPKVPWYDSrvnlNKAWLEK 90

                        90
                ....*....|...
gi 23111026  99 RRQGLQHFLEKVL 111
Cdd:cd07280  91 RRRGLQYFLNCVL 103
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
 34-129 1.03e-13

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: 66.15  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  34 SYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGT----SDEFIEKRRQGLQHFLEK 109
Cdd:cd07284  17 TFITYRVMTKTSRSEFDSSEFEVRRRYQDFLWLKGRLEEAHPTLIIPPLPEKFVMKGMverfNEDFIETRRKALHKFLNR 96

                        90       100
                ....*....|....*....|
gi 23111026 110 VLQSVVLLSDSQLHLFLQSQ 129
Cdd:cd07284  97 IADHPTLTFNEDFKIFLTAQ 116
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
 17-127 2.97e-13

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: 65.08  E-value: 2.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  17 ITVRVQDPRVQNEGSW--NSYVDY----KIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFG 90
Cdd:cd06864   3 ITVTEAEKRTGGSAMNlkETYTVYlietKIVEHESEEGLSKKLSSLWRRYSEFELLRNYLVVTYPYVIVPPLPEKRAMFM 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 23111026  91 ----TSD----EFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQ 127
Cdd:cd06864  83 wqklSSDtfdpDFVERRRAGLENFLLRVAGHPELCQDKIFLEFLT 127
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
 31-107 4.26e-13

The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132807  Cd Length: 108  Bit Score: 63.83  E-value: 4.26e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23111026  31 SWNSYVDYKIFLHTNSKAFTaktscVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSD--EFIEKRRQGLQHFL 107
Cdd:cd06897  11 SPKPYTVYNIQVRLPLRSYT-----VSRRYSEFVALHKQLESEVGIEPPYPLPPKSWFLSTSSnpKLVEERRVGLEAFL 84
PX_SNX30 cd07283
The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; The PX domain is a ...
 19-129 1.38e-12

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: 62.80  E-value: 1.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  19 VRVQDPRvQNEGSWNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGT----SDE 94
Cdd:cd07283   3 VTVDDPK-KHVCTMETYITYRVTTKTTRTEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVvdrfSEE 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 23111026  95 FIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQSQ 129
Cdd:cd07283  82 FVETRRKALDKFLKRIADHPVLSFNEHFNVFLTAK 116
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 17-174 1.67e-12

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 66.74  E-value: 1.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  17 ITVRVQDPRVQNEGSWNSYVDYKIFLHTNSKAFTAKTSC---VRRRYREFVWLRKQLQRNAGLVPVPELPGK---STFFG 90
Cdd:COG5391 133 STVSNPQSLTLLVDSRDKHTSYEIITVTNLPSFQLRESRplvVRRRYSDFESLHSILIKLLPLCAIPPLPSKksnSEYYG 212

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  91 T--SDEFIEKRRQGLQHFLEKV-----LQSVVLLSDSQLHL-----FLQSQLSVPEieacvqgrstmTVSDAILRYAMSN 158
Cdd:COG5391 213 DrfSDEFIEERRQSLQNFLRRVsthplLSNYKNSKSWESHStllssFIENRKSVPT-----------PLSLDLTSTTQEL 281

                       170
                ....*....|....*.
gi 23111026 159 CGWAQEERQSSSHLAK 174
Cdd:COG5391 282 DMERKELNESTSKAIH 297
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
 29-126 2.47e-12

The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; 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. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.


Pssm-ID: 132776  Cd Length: 105  Bit Score: 61.86  E-value: 2.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  29 EGSWNSYVDYKIFlhtnSKAFTaktSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFIEKRRQGLQHFLE 108
Cdd:cd06866  12 KGLFLKHVEYEVS----SKRFK---STVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGSADREFLEARRRGLSRFLN 84

                        90
                ....*....|....*...
gi 23111026 109 KVLQSVVLLSDSQLHLFL 126
Cdd:cd06866  85 LVARHPVLSEDELVRTFL 102
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
 28-126 4.28e-11

The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; 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. SNX41 and SNX42 (also called Atg20p) form dimers with SNX4, and are required in protein recycling from the sorting endosome (post-Golgi endosome) back to the late Golgi in yeast.


Pssm-ID: 132777  Cd Length: 112  Bit Score: 58.80  E-value: 4.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  28 NEGSWNSYVDYKIFLhtnskaftaKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFF------GTSDE---FIEK 98
Cdd:cd06867  11 SEGGSGSYIVYVIRL---------GGSEVKRRYSEFESLRKNLTRLYPTLIIPPIPEKHSLKdyakkpSKAKNdakIIER 81

                        90       100
                ....*....|....*....|....*...
gi 23111026  99 RRQGLQHFLEKVLQSVVLLSDSQLHLFL 126
Cdd:cd06867  82 RKRMLQRFLNRCLQHPILRNDIVFQKFL 109
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
 34-129 3.75e-10

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: 56.56  E-value: 3.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  34 SYVDYKIflhTNSkaFTAKTscVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFIEKRRQGLQHFLEKVLQS 113
Cdd:cd06862  19 SFIAYQI---TPT--HTNVT--VSRRYKHFDWLYERLVEKYSCIAIPPLPEKQVTGRFEEDFIEKRRERLELWMNRLARH 91

                        90
                ....*....|....*..
gi 23111026 114 VVlLSDSQ-LHLFLQSQ 129
Cdd:cd06862  92 PV-LSQSEvFRHFLTCT 107
PX_SNX27 cd06886
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a ...
 26-110 2.06e-08

The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; 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. SNX27 contains an N-terminal PDZ domain followed by a PX domain and a Ras-Associated (RA) domain. It binds G protein-gated potassium (Kir3) channels, which play a role in neuronal excitability control, through its PDZ domain. SNX27 downregulates Kir3 channels by promoting their movement in the endosome, reducing surface expression and increasing degradation. SNX27 also associates with 5-hydroxytryptamine type 4 receptor (5-HT4R), cytohesin associated scaffolding protein (CASP), and diacylglycerol kinase zeta, and may play a role in their intracellular trafficking and endocytic recycling. The SNX27 PX domain preferentially binds to phosphatidylinositol-3-phosphate (PI3P) and is important for targeting to the early endosome.


Pssm-ID: 132796  Cd Length: 106  Bit Score: 50.87  E-value: 2.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  26 VQNEGSwnSYVDYKIFLhtnskafTAKTSCvRRRYREFVWLRKQLQRNAGLVPVPELPGKSTfFGTSDEFIEKRRQGLQH 105
Cdd:cd06886  14 VEQNGE--KFVVYNIYM-------AGRQLC-SRRYREFANLHQNLKKEFPDFQFPKLPGKWP-FSLSEQQLDARRRGLEQ 82


                ....*
gi 23111026 106 FLEKV 110
Cdd:cd06886  83 YLEKV 87
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
 55-128 4.15e-08

The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; 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. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.


Pssm-ID: 132787  Cd Length: 119  Bit Score: 50.45  E-value: 4.15e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23111026  55 CVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQS 128
Cdd:cd06877  45 SVLRRYNEFYVLESKLTEFHGEFPDAPLPSRRIFGPKSYEFLESKREIFEEFLQKLLQKPELRGSELLYDFLSP 118
PX_SNX18 cd07286
The phosphoinositide binding Phox Homology domain of Sorting Nexin 18; The PX domain is a ...
 21-126 1.66e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 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. SNX18, like SNX9, contains an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature. The PX-BAR structural unit helps determine specific membrane localization. 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: 132819  Cd Length: 127  Bit Score: 49.28  E-value: 1.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  21 VQDPRVQNE-GSWNSYVDYKIF-LHTNSKaftaktscVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFIEK 98
Cdd:cd07286   5 IDDPTKQTKfKGMKSYISYKLVpSHTGLQ--------VHRRYKHFDWLYARLAEKFPVISVPHIPEKQATGRFEEDFISK 76

                        90       100
                ....*....|....*....|....*...
gi 23111026  99 RRQGLQHFLEKVLQSVVLLSDSQLHLFL 126
Cdd:cd07286  77 RRKGLIWWMDHMCSHPVLARCDAFQHFL 104
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
 17-116 2.08e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; 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. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome.


Pssm-ID: 132783  Cd Length: 120  Bit Score: 48.42  E-value: 2.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  17 ITVRVQDPRVQNEgSWNSYvdykiflhtnskaftaktscvrRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFI 96
Cdd:cd06873  27 ISVTRIYPNGQEE-SWHVY----------------------RRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNNLDRAFL 83

                        90       100
                ....*....|....*....|
gi 23111026  97 EKRRQGLQHFLEKVLQSVVL 116
Cdd:cd06873  84 EKRRKMLNQYLQSLLNPEVL 103
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
 56-126 3.88e-07

The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132781  Cd Length: 120  Bit Score: 47.74  E-value: 3.88e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23111026  56 VRRRYREFVWLRKQLQRNAGLVPVPelPGKstFFGTSD-EFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFL 126
Cdd:cd06871  40 VIRRYNDFDLLNASLQISGISLPLP--PKK--LIGNMDrEFIAERQQGLQNYLNVILMNPILASCLPVKKFL 107
PX_SNX15_like cd06881
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ...
 21-127 4.48e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily have similarity to sorting nexin 15 (SNX15), which contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) 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. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein. Other members of this subfamily contain an additional C-terminal kinase domain, similar to human RPK118, which binds sphingosine kinase and the antioxidant peroxiredoxin-3 (PRDX3). RPK118 may be involved in the transport of proteins such as PRDX3 from the cytoplasm to its site of function in the mitochondria.


Pssm-ID: 132791  Cd Length: 117  Bit Score: 47.70  E-value: 4.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  21 VQDPRVQNEGswnsYVDYKIFLHTNSKAFTAKTSC--VRRRYREFVWLRKQLQR------NAGLVPVPElpgKSTFFGTS 92
Cdd:cd06881   7 VTDTRRHKKG----YTEYKITSKVFSRSVPEDVSEvvVWKRYSDFKKLHRELSRlhkqlyLSGSFPPFP---KGKYFGRF 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 23111026  93 DE-FIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQ 127
Cdd:cd06881  80 DAaVIEERRQAILELLDFVGNHPALYQSSAFQQFFE 115
PX_SNX9 cd07285
The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; The PX domain is a ...
 21-126 5.04e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; 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. SNX9, also known as SH3PX1, is a cytosolic protein that interacts with proteins associated with clathrin-coated pits such as Cdc-42-associated tyrosine kinase 2 (ACK2). It contains an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature. The PX-BAR structural unit helps determine specific membrane localization. Through its SH3 domain, SNX9 binds class I polyproline sequences found in dynamin 1/2 and the WASP/N-WASP actin regulators. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis. Its array of interacting partners suggests that SNX9 functions at the interface between endocytosis and actin cytoskeletal organization.


Pssm-ID: 132818  Cd Length: 126  Bit Score: 47.71  E-value: 5.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  21 VQDPRvqnEGS----WNSYVDYKIFLHTNSKAftaktscVRRRYREFVWLRKQLQRNAGL-VPVPELPGKSTFFGTSDEF 95
Cdd:cd07285   5 VADPR---KGSkmygLKSYIEYQLTPTNTNRS-------VNHRYKHFDWLYERLLVKFGLaIPIPSLPDKQVTGRFEEEF 74

                        90       100       110
                ....*....|....*....|....*....|.
gi 23111026  96 IEKRRQGLQHFLEKVLQSVVLLSDSQLHLFL 126
Cdd:cd07285  75 IKMRMERLQAWMTRMCRHPVISESEVFQQFL 105
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
 18-128 5.41e-07

The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. 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: 132786  Cd Length: 133  Bit Score: 47.69  E-value: 5.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  18 TVRVQDPRVQNEGSWNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKS--TFFGTSDEF 95
Cdd:cd06876  21 RVSIQSYISDVEEEGKEFVVYLIEVQRLNNDDQSSGWVVARRYSEFLELHKYLKKRYPGVLKLDFPQKRkiSLKYSKTLL 100

                        90       100       110
                ....*....|....*....|....*....|...
gi 23111026  96 IEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQS 128
Cdd:cd06876 101 VEERRKALEKYLQELLKIPEVCEDEEFRKFLSQ 133
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
 35-127 2.87e-06

The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.


Pssm-ID: 132780  Cd Length: 109  Bit Score: 45.09  E-value: 2.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  35 YVDYKIFLHT-NSKAFtaktscVRRRYREFVWLRKQLQRNaglvpVP----ELPGKStFFGT--SDEFIEKRRQGLQHFL 107
Cdd:cd06870  20 FTVYKVVVSVgRSSWF------VFRRYAEFDKLYESLKKQ-----FPasnlKIPGKR-LFGNnfDPDFIKQRRAGLDEFI 87

                        90       100
                ....*....|....*....|
gi 23111026 108 EKVLQSVVLLSDSQLHLFLQ 127
Cdd:cd06870  88 QRLVSDPKLLNHPDVRAFLQ 107
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
 56-115 7.02e-06

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins 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. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.


Pssm-ID: 132810  Cd Length: 118  Bit Score: 44.26  E-value: 7.02e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  56 VRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFIEKRRQGLQHFLEKVLQSVV 115
Cdd:cd07277  34 VYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKDAKFVEERRKRLQVYLRRVVNTLI 93
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
 45-126 1.57e-05

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: 43.68  E-value: 1.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  45 NSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTF-----FGTSD-EFIEKRRQGLQHFLEKvLQSVVLLS 118
Cdd:cd06893  42 AASEQPLATHTVNRRFREFLTLQTRLEENPKFRKIMNVKGPPKRlfdlpFGNMDkDKIEARRGLLETFLRQ-LCSIPEIS 120


                ....*....
gi 23111026 119 DS-QLHLFL 126
Cdd:cd06893 121 NSeEVQEFL 129
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
 56-111 1.92e-05

The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. 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. 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: 132785  Cd Length: 116  Bit Score: 43.04  E-value: 1.92e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23111026  56 VRRRYREFVWLRKQLqRNAGLVPVPELPGKSTFFGTSDEFIEKRRQGLQHFLEKVL 111
Cdd:cd06875  33 VKHRYSDFAELHDKL-VAEHKVDKDLLPPKKLIGNKSPSFVEKRRKELEIYLQTLL 87
PX_Vps17p cd06891
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps17p; The PX domain ...
 38-128 4.10e-05

The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps17p; 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. Vsp17p forms a dimer with Vps5p, the yeast counterpart of human SNX1, and is part of the retromer complex that mediates the transport of the carboxypeptidase Y receptor Vps10p from endosomes to Golgi. Similar to Vps5p and SNX1, Vps17p harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit helps determine specific membrane localization.


Pssm-ID: 132801  Cd Length: 140  Bit Score: 42.34  E-value: 4.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  38 YKIFLHTNSKAFTAKT-SCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEfiEKRRQ---GLQHFLEKVLQS 113
Cdd:cd06891  47 IRFDVTTNLPTFRSSTyKDVRRTYEEFQKLFKYLNGANPETFVPALPLPSTSYGSNNE--EDARKlkaNLQRWFNRVCSD 124

                        90
                ....*....|....*
gi 23111026 114 VVLLSDSQLHLFLQS 128
Cdd:cd06891 125 PILIRDEELRFFIES 139
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
 55-111 4.41e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; 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. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.


Pssm-ID: 132790  Cd Length: 110  Bit Score: 41.88  E-value: 4.41e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23111026  55 CVRRRYREFVWLRKQLQRnagLVPVPELPGKsTFFGTSDEFIEKRRQGLQHFLEKVL 111
Cdd:cd06880  34 TVEKRYSEFHALHKKLKK---SIKTPDFPPK-RVRNWNPKVLEQRRQGLEAYLQGLL 86
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 33-128 4.77e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17), SNX31, and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region. 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. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR, VLDLR, ApoER2, and others, regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide, which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown.


Pssm-ID: 132795  Cd Length: 104  Bit Score: 41.55  E-value: 4.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  33 NSYVDYKIflHTNSKAFtaktsCvRRRYREFVWLRKQLQRNAGLVPVPELPGKStFFGTSDEFIEKRRQGLQHFLEKVLQ 112
Cdd:cd06885  16 STYVAYNI--HINGVLH-----C-SVRYSQLHGLNEQLKKEFGNRKLPPFPPKK-LLPLTPAQLEERRLQLEKYLQAVVQ 86

                        90
                ....*....|....*.
gi 23111026 113 SVVLLSDSQLHLFLQS 128
Cdd:cd06885  87 DPRIANSDIFNSFLLN 102
PX_p40phox cd06882
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ...
 25-131 7.99e-05

The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p40phox contains an N-terminal PX domain, a central SH3 domain that binds p47phox, and a C-terminal PB1 domain that interacts with p67phox. It is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. The PX domain is a phospholipid-binding module involved in the membrane targeting of proteins. The p40phox PX domain binds to PI3P, an abundant lipid in phagosomal membranes, playing an important role in the localization of NADPH oxidase. The PX domain of p40phox is also involved in protein-protein interaction.


Pssm-ID: 132792  Cd Length: 123  Bit Score: 41.27  E-value: 7.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  25 RVQNEGSWNSYVdYKIFLHTNSKAFtaktscVRRRYREFVWLRKQLQRNAGL--------VPVPELPGKsTFFGTSDEFI 96
Cdd:cd06882  13 EKRGFTNYYVFV-IEVKTKGGSKYL------IYRRYRQFFALQSKLEERFGPeagssaydCTLPTLPGK-IYVGRKAEIA 84

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 23111026  97 EKRRQGLQHFLEKVLQS-VVLLSDSQLHLFLQSQLS 131
Cdd:cd06882  85 ERRIPLLNRYMKELLSLpVWVLMDEDVRLFFYQTES 120
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
 56-126 2.66e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; 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. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.


Pssm-ID: 132809  Cd Length: 110  Bit Score: 39.70  E-value: 2.66e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23111026  56 VRRRYREFVWLRKQLqRNAGLVPVPELPGKSTFFGTSD-EFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFL 126
Cdd:cd07276  37 VFRRYTDFVRLNDKL-KQMFPGFRLSLPPKRWFKDNFDpDFLEERQLGLQAFVNNIMAHKDIAKCKLVREFF 107
PX_HS1BP3 cd06868
The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a ...
 33-126 3.27e-03

The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Hematopoietic lineage cell-specific protein-1 (HS1) binding protein 3 (HS1BP3) associates with HS1 proteins through their SH3 domains, suggesting a role in mediating signaling. It has been reported that HS1BP3 might affect the IL-2 signaling pathway in hematopoietic lineage cells. Mutations in HS1BP3 may also be associated with familial Parkinson disease and essential tremor. HS1BP3 contains a PX domain, a leucine zipper, motifs similar to immunoreceptor tyrosine-based inhibitory motif and proline-rich regions. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132778  Cd Length: 120  Bit Score: 36.62  E-value: 3.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  33 NSYVDYKIFLHTNSKAFTAKTS--------CVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDefIEKRRQGLQ 104
Cdd:cd06868  18 SGHVLYQIVVVTRLAAFKSAKHkeedvvqfMVSKKYSEFEELYKKLSEKYPGTILPPLPRKALFVSESD--IRERRAAFN 95

                        90       100
                ....*....|....*....|..
gi 23111026 105 HFLEKVLQSVVLLSDSQLHLFL 126
Cdd:cd06868  96 DFMRFISKDEKLANCPELLEFL 117
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
 19-131 3.54e-03

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. 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: 132784  Cd Length: 127  Bit Score: 36.59  E-value: 3.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23111026  19 VRVQDPR-VQNEGSWNSYVDYKIFLHTNSKAFTaktscVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFIE 97
Cdd:cd06874   1 IKITIPRyVLRGQGKDEHFEFEVKITVLDETWT-----VFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAK 75

                        90       100       110
                ....*....|....*....|....*....|....
gi 23111026  98 KRRQGLQHFLEKVLQSVVLLSDSQLHLFLQSQLS 131
Cdd:cd06874  76 ERRRQLETYLRNFFSVCLKLPACPLYPKVGRTLS 109
 
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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