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Conserved domains on  [gi|1034659462|ref|XP_016868644|]
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sorting nexin-31 isoform X3 [Homo sapiens]

Protein Classification

PH domain-containing protein; ubiquitin family protein( domain architecture ID 12951907)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner| ubiquitin family protein belongs to a diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes; has an N-terminal domain with similarity to the N-terminus of ubiquitin fusion degradation UFD1 which functions at a post-ubiquitation step in the ubiquitin fusion degradation (UFD) pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM-like_C_SNX31 cd13336
Atypical FERM-like domain C-lobe of Sorting nexin 31; SNX31 functions in regulating recycling ...
 270-384 6.22e-69

Atypical FERM-like domain C-lobe of Sorting nexin 31; SNX31 functions in regulating recycling from endosomes to the cell surface. SNX31 contains a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. It bind Ras GTPase through its FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 275415  Cd Length: 113  Bit Score: 214.37  E-value: 6.22e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 270 GYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTLLDTDGpqRTLNQNLELRFQY 349
Cdd:cd13336     1 GYLQLDPCACDYPECGSEANVWVGNNEISCCIHLPGGQTEHLRFNIRRVICWQVTFLGPKKQEVM--SPLHQHLELRFEY 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034659462 350 SEDSCWQWFVIYTKQAFLLSSCLKKMISEKMVKLA 384
Cdd:cd13336    79 QQGSSWKWIVIRTKQAFLLSSCLKKMISEYPVHRS 113
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 4-106 4.45e-58

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: 186.00  E-value: 4.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462   4 HFCIPVSQQRSDALGGRYVLYSVHLDGFLFCRVRYSQLHGWNEQLRRVFGN-CLPPFPPKYYLAMTTAMADERRDQLEQY 82
Cdd:cd06885     1 HFSIPDTQELSDEGGSTYVAYNIHINGVLHCSVRYSQLHGLNEQLKKEFGNrKLPPFPPKKLLPLTPAQLEERRLQLEKY 80

                          90       100
                  ....*....|....*....|....
gi 1034659462  83 LQNVTMDPNVLRSDVFVEFLKLAQ 106
Cdd:cd06885    81 LQAVVQDPRIANSDIFNSFLLNAQ 104
FERM_F1_SNX31 cd16122
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 112-209 9.00e-56

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 31 (SNX31); SNX31 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. It is a novel sorting nexin associated with the uroplakin-degrading multivesicular bodies in terminally differentiated urothelial cells. SNX31 binds multiple beta integrin cytoplasmic domains and regulates beta1 integrin surface levels and stability. SNX31 contains a PX (Phox homology) domain and a FERM (Band 4.1, ezrin, radixin, moesin) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


:

Pssm-ID: 340539  Cd Length: 98  Bit Score: 179.56  E-value: 9.00e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 112 IATKKAYLDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRFGKEGKLSVVKKLADFELPYVSLGS 191
Cdd:cd16122     1 IHTLKAVLDVYLPDGRSVRIDVKTSDTAERVLEVVLDRIGLSRELRGYFSLFLVKGKGKGDFSVVKKLAPFELPYVTLES 80

                          90
                  ....*....|....*...
gi 1034659462 192 SEVENCKVGLRKWYMAPS 209
Cdd:cd16122    81 GEMERCKLGIRKWYMDPS 98
 
Name Accession Description Interval E-value
FERM-like_C_SNX31 cd13336
Atypical FERM-like domain C-lobe of Sorting nexin 31; SNX31 functions in regulating recycling ...
 270-384 6.22e-69

Atypical FERM-like domain C-lobe of Sorting nexin 31; SNX31 functions in regulating recycling from endosomes to the cell surface. SNX31 contains a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. It bind Ras GTPase through its FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275415  Cd Length: 113  Bit Score: 214.37  E-value: 6.22e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 270 GYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTLLDTDGpqRTLNQNLELRFQY 349
Cdd:cd13336     1 GYLQLDPCACDYPECGSEANVWVGNNEISCCIHLPGGQTEHLRFNIRRVICWQVTFLGPKKQEVM--SPLHQHLELRFEY 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034659462 350 SEDSCWQWFVIYTKQAFLLSSCLKKMISEKMVKLA 384
Cdd:cd13336    79 QQGSSWKWIVIRTKQAFLLSSCLKKMISEYPVHRS 113
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 4-106 4.45e-58

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: 186.00  E-value: 4.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462   4 HFCIPVSQQRSDALGGRYVLYSVHLDGFLFCRVRYSQLHGWNEQLRRVFGN-CLPPFPPKYYLAMTTAMADERRDQLEQY 82
Cdd:cd06885     1 HFSIPDTQELSDEGGSTYVAYNIHINGVLHCSVRYSQLHGLNEQLKKEFGNrKLPPFPPKKLLPLTPAQLEERRLQLEKY 80

                          90       100
                  ....*....|....*....|....
gi 1034659462  83 LQNVTMDPNVLRSDVFVEFLKLAQ 106
Cdd:cd06885    81 LQAVVQDPRIANSDIFNSFLLNAQ 104
FERM_F1_SNX31 cd16122
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 112-209 9.00e-56

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 31 (SNX31); SNX31 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. It is a novel sorting nexin associated with the uroplakin-degrading multivesicular bodies in terminally differentiated urothelial cells. SNX31 binds multiple beta integrin cytoplasmic domains and regulates beta1 integrin surface levels and stability. SNX31 contains a PX (Phox homology) domain and a FERM (Band 4.1, ezrin, radixin, moesin) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340539  Cd Length: 98  Bit Score: 179.56  E-value: 9.00e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 112 IATKKAYLDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRFGKEGKLSVVKKLADFELPYVSLGS 191
Cdd:cd16122     1 IHTLKAVLDVYLPDGRSVRIDVKTSDTAERVLEVVLDRIGLSRELRGYFSLFLVKGKGKGDFSVVKKLAPFELPYVTLES 80

                          90
                  ....*....|....*...
gi 1034659462 192 SEVENCKVGLRKWYMAPS 209
Cdd:cd16122    81 GEMERCKLGIRKWYMDPS 98
SNX17_FERM_C pfam18116
Sorting Nexin 17 FERM C-terminal domain; This is the C-terminal domain of sorting nexin 17 ...
 270-380 1.32e-47

Sorting Nexin 17 FERM C-terminal domain; This is the C-terminal domain of sorting nexin 17 (SNX17) present in Homo sapiens. SNX17 localizes to early endosomes where it directly binds NPX(Y/F) motifs in the target receptors to mediate their rates of endocytic internalization, recycling, or degradation. The domain is known as terminal band 4.1/ezrin/radixin/moesin (FERM) domain. The FERM domain binds directly to the common motif, NPX(Y/F), in the cytoplasmic region of its target proteins.


Pssm-ID: 436285  Cd Length: 109  Bit Score: 158.73  E-value: 1.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 270 GYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTllDTDGPQrTLNQNLELRFQY 349
Cdd:pfam18116   1 GYIQFDPCTCDYPEPDSRVTVSVGNNELNCCITLPEKETEEAAFKVTRMRCWRVTALDN--KSMSPQ-DNEQGLELSFEY 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034659462 350 SED-SCWQWFVIYTKQAFLLSSCLKKMISEKM 380
Cdd:pfam18116  78 LFSkDELKWITIASEQAILLSMCLQSMVDELL 109
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 33-102 3.18e-12

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 61.87  E-value: 3.18e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034659462  33 FCRVRYSQLHGWNEQLRRVFGNC-LPPFPPKYYL-AMTTAMADERRDQLEQYLQNVTMDPNVLRSDVFVEFL 102
Cdd:pfam00787  10 SVRRRYSDFVELHKKLLRKFPSViIPPLPPKRWLgRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFL 81
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 20-102 4.73e-09

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: 53.50  E-value: 4.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462   20 RYVLYSVHLDGFL---FCRVRYSQLHGWNEQLRRVFGNC-LPPFPPKYYL----AMTTAMADERRDQLEQYLQNVTMDPN 91
Cdd:smart00312  13 YYYVIEIETKTGLeewTVSRRYSDFLELHSKLKKHFPRSiLPPLPGKKLFgrlnNFSEEFIEKRRRGLEKYLQSLLNHPE 92

                           90
                   ....*....|..
gi 1034659462   92 -VLRSDVFVEFL 102
Cdd:smart00312  93 lINHSEVVLEFL 104
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 121-251 1.42e-04

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 42.67  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462  121 IFLPNEQSIRIEIITSDTAERVLEVVSHKIGL-CREllgYFGLFLIRFGKEGK--LSVVKKLADFElpyvslgsSEVENC 197
Cdd:smart00295   4 VYLLDGTTLEFEVDSSTTAEELLETVCRKLGIrESE---YFGLQFEDPDEDLRhwLDPAKTLLDQD--------VKSEPL 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034659462  198 KVGLRKWYMaPSLDSVLMDCRVAVDLLYMQAIQDIEKGWAKPTQAQRQKLEAFQ 251
Cdd:smart00295  73 TLYFRVKFY-PPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALA 125
 
Name Accession Description Interval E-value
FERM-like_C_SNX31 cd13336
Atypical FERM-like domain C-lobe of Sorting nexin 31; SNX31 functions in regulating recycling ...
 270-384 6.22e-69

Atypical FERM-like domain C-lobe of Sorting nexin 31; SNX31 functions in regulating recycling from endosomes to the cell surface. SNX31 contains a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. It bind Ras GTPase through its FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275415  Cd Length: 113  Bit Score: 214.37  E-value: 6.22e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 270 GYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTLLDTDGpqRTLNQNLELRFQY 349
Cdd:cd13336     1 GYLQLDPCACDYPECGSEANVWVGNNEISCCIHLPGGQTEHLRFNIRRVICWQVTFLGPKKQEVM--SPLHQHLELRFEY 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034659462 350 SEDSCWQWFVIYTKQAFLLSSCLKKMISEKMVKLA 384
Cdd:cd13336    79 QQGSSWKWIVIRTKQAFLLSSCLKKMISEYPVHRS 113
FERM-like_C_SNX cd13207
Atypical FERM-like domain C-lobe of Sorting nexin family; Sorting nexins function in ...
 270-384 1.15e-60

Atypical FERM-like domain C-lobe of Sorting nexin family; Sorting nexins function in regulating recycling from endosomes to the cell surface. SNX17, SNX27, and SNX31 contain a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. All three proteins are able to bind the Ras GTPase through their FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275395  Cd Length: 116  Bit Score: 192.93  E-value: 1.15e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 270 GYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTLLDTDGPQRTLNQNLELRFQY 349
Cdd:cd13207     1 GYLIFDHCSCDSPEGHVITVISIGNFELSACTELPDSQTQGQLFNQVRAFCWDVTQRWDLLDTDGPQRTDEEGLELCFEY 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034659462 350 SED-SCWQWFVIYTKQAFLLSSCLKKMISEKMVKLA 384
Cdd:cd13207    81 ARGeKKPQWVKIFTPQANYMSECLERMFCELMVKKE 116
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 4-106 4.45e-58

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: 186.00  E-value: 4.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462   4 HFCIPVSQQRSDALGGRYVLYSVHLDGFLFCRVRYSQLHGWNEQLRRVFGN-CLPPFPPKYYLAMTTAMADERRDQLEQY 82
Cdd:cd06885     1 HFSIPDTQELSDEGGSTYVAYNIHINGVLHCSVRYSQLHGLNEQLKKEFGNrKLPPFPPKKLLPLTPAQLEERRLQLEKY 80

                          90       100
                  ....*....|....*....|....
gi 1034659462  83 LQNVTMDPNVLRSDVFVEFLKLAQ 106
Cdd:cd06885    81 LQAVVQDPRIANSDIFNSFLLNAQ 104
FERM_F1_SNX31 cd16122
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 112-209 9.00e-56

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 31 (SNX31); SNX31 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. It is a novel sorting nexin associated with the uroplakin-degrading multivesicular bodies in terminally differentiated urothelial cells. SNX31 binds multiple beta integrin cytoplasmic domains and regulates beta1 integrin surface levels and stability. SNX31 contains a PX (Phox homology) domain and a FERM (Band 4.1, ezrin, radixin, moesin) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340539  Cd Length: 98  Bit Score: 179.56  E-value: 9.00e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 112 IATKKAYLDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRFGKEGKLSVVKKLADFELPYVSLGS 191
Cdd:cd16122     1 IHTLKAVLDVYLPDGRSVRIDVKTSDTAERVLEVVLDRIGLSRELRGYFSLFLVKGKGKGDFSVVKKLAPFELPYVTLES 80

                          90
                  ....*....|....*...
gi 1034659462 192 SEVENCKVGLRKWYMAPS 209
Cdd:cd16122    81 GEMERCKLGIRKWYMDPS 98
FERM_F1_SNX17_like cd17109
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in PX-FERM family ...
 115-207 3.23e-49

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in PX-FERM family sorting nexin proteins; This family includes three endosome-associated PX (Phox homology) and FERM (Band 4.1, ezrin, radixin, moesin) domain-containing proteins called sorting nexin (SNX) 17, SNX27, and SNX31, which are modular peripheral membrane proteins acting as central scaffolds mediating protein-lipid interactions, cargo binding, and regulatory protein recruitment. They are key regulators of endosomal recycling and bind conserved NPX(Y/F) peptide sorting motifs in transmembrane cargos via an atypical FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340629  Cd Length: 93  Bit Score: 162.38  E-value: 3.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 115 KKAYLDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRFGKEGKLSVVKKLADFELPYVSLGSSEV 194
Cdd:cd17109     1 SDVELRVALPNGQTVTVRVKTSDTTEQVLEAVAAKVGLDSTLVGYFALFLVRSHSEGKLSFVRKLAPFELPYVSYISNYT 80

                          90
                  ....*....|...
gi 1034659462 195 ENCKVGLRKWYMA 207
Cdd:cd17109    81 PGTKLTLRKWYFT 93
SNX17_FERM_C pfam18116
Sorting Nexin 17 FERM C-terminal domain; This is the C-terminal domain of sorting nexin 17 ...
 270-380 1.32e-47

Sorting Nexin 17 FERM C-terminal domain; This is the C-terminal domain of sorting nexin 17 (SNX17) present in Homo sapiens. SNX17 localizes to early endosomes where it directly binds NPX(Y/F) motifs in the target receptors to mediate their rates of endocytic internalization, recycling, or degradation. The domain is known as terminal band 4.1/ezrin/radixin/moesin (FERM) domain. The FERM domain binds directly to the common motif, NPX(Y/F), in the cytoplasmic region of its target proteins.


Pssm-ID: 436285  Cd Length: 109  Bit Score: 158.73  E-value: 1.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 270 GYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTllDTDGPQrTLNQNLELRFQY 349
Cdd:pfam18116   1 GYIQFDPCTCDYPEPDSRVTVSVGNNELNCCITLPEKETEEAAFKVTRMRCWRVTALDN--KSMSPQ-DNEQGLELSFEY 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034659462 350 SED-SCWQWFVIYTKQAFLLSSCLKKMISEKM 380
Cdd:pfam18116  78 LFSkDELKWITIASEQAILLSMCLQSMVDELL 109
FERM-like_C_SNX17 cd13337
Atypical FERM-like domain C-lobe of Sorting nexin 17; SNX17 is a beta1-integrin-tail-binding ...
 269-382 4.00e-26

Atypical FERM-like domain C-lobe of Sorting nexin 17; SNX17 is a beta1-integrin-tail-binding protein that interacts with the free kindlin-binding site in endosomes to stabilize beta1 integrins, resulting in their recycling to the cell surface where they can be reused. SNX17 contains a N-terminal PX domain, a FERM-like domain, and a unique C-terminal region. SNX17 binds Ras GTPase through its FERM-like domains. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. These proteins participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades. The typical FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. FERM domains are found in cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270145  Cd Length: 113  Bit Score: 101.65  E-value: 4.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 269 YGYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTLLDTDGPqrtlNQNLELRFQ 348
Cdd:cd13337     1 YGYIQFEPCICDYPKPGTRVLVSIGNRELNFRLKDEEGKVKEGSFRVTRMRCWRITASHIEEDSKKD----EKKLELSFE 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034659462 349 Y--SEDsCWQWFVIYTKQAFLLSSCLKKMISEKMVK 382
Cdd:cd13337    77 YlmSKD-KLQWITIRSDQAILMSLCLQSMVDELLRK 111
FERM_F1_SNX17 cd16121
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 119-205 2.42e-24

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 17 (SNX17); SNX17 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. It localizes to early endosomes, and plays an important role in mediating endocytic internalization, recycling, and/or protection from lysosomal degradation of NPxY-motif containing cell surface proteins including amyloid precursor protein (APP), P-selectin, beta1-integrin, low density lipoprotein receptor (LDLR), LDLR related protein (Lrp1), ApoER2, and FEEL1. SNX17 also affects T cell activation by regulating T cell receptor and integrin recycling. SNX17 contains a PX (Phox homology) domain and a FERM (Band 4.1, ezrin, radixin, moesin) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340538  Cd Length: 93  Bit Score: 96.15  E-value: 2.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 119 LDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRFGKEGKLSVVKKLADFELPYVSLGSSEVENCK 198
Cdd:cd16121     5 LDVFLMNGQKITVNISSTDQTDDVLEAVASKLGLPEELVYYFALFLVKKDDDGNNTIVRKLQDFESPYLSLKSAGKGSHR 84


                  ....*..
gi 1034659462 199 VGLRKWY 205
Cdd:cd16121    85 IVLRKSY 91
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 33-102 3.18e-12

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 61.87  E-value: 3.18e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034659462  33 FCRVRYSQLHGWNEQLRRVFGNC-LPPFPPKYYL-AMTTAMADERRDQLEQYLQNVTMDPNVLRSDVFVEFL 102
Cdd:pfam00787  10 SVRRRYSDFVELHKKLLRKFPSViIPPLPPKRWLgRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFL 81
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 17-104 2.68e-11

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: 60.06  E-value: 2.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462  17 LGGRYVLYSVHL-----DGFLFCRvRYSQLHGWNEQLRRVFGNC-LPPFPPKYYLA-MTTAMADERRDQLEQYLQNVTMD 89
Cdd:cd06093    13 GGKKYVVYIIEVttqggEEWTVYR-RYSDFEELHEKLKKKFPGViLPPLPPKKLFGnLDPEFIEERRKQLEQYLQSLLNH 91

                          90
                  ....*....|....*
gi 1034659462  90 PNVLRSDVFVEFLKL 104
Cdd:cd06093    92 PELRNSEELKEFLEL 106
PX_SNX27 cd06886
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a ...
 18-103 9.53e-11

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: 58.58  E-value: 9.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462  18 GGRYVLYSVHLDGFLFCRVRYSQLHGWNEQLRRVFGN-CLPPFPPKYYLAMTTAMADERRDQLEQYLQNVTMDPNVLRSD 96
Cdd:cd06886    18 GEKFVVYNIYMAGRQLCSRRYREFANLHQNLKKEFPDfQFPKLPGKWPFSLSEQQLDARRRGLEQYLEKVCSIRVIGESD 97


                  ....*..
gi 1034659462  97 VFVEFLK 103
Cdd:cd06886    98 IMQDFLS 104
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 20-102 4.73e-09

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: 53.50  E-value: 4.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462   20 RYVLYSVHLDGFL---FCRVRYSQLHGWNEQLRRVFGNC-LPPFPPKYYL----AMTTAMADERRDQLEQYLQNVTMDPN 91
Cdd:smart00312  13 YYYVIEIETKTGLeewTVSRRYSDFLELHSKLKKHFPRSiLPPLPGKKLFgrlnNFSEEFIEKRRRGLEKYLQSLLNHPE 92

                           90
                   ....*....|..
gi 1034659462   92 -VLRSDVFVEFL 102
Cdd:smart00312  93 lINHSEVVLEFL 104
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
 37-104 1.04e-07

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: 49.96  E-value: 1.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034659462  37 RYS---QLHgwnEQLRRVFGNCLP-PFPPKYYLAMTT---AMADERRDQLEQYLQNVTMDPNV-LR-SDVFVEFLKL 104
Cdd:cd06897    34 RYSefvALH---KQLESEVGIEPPyPLPPKSWFLSTSsnpKLVEERRVGLEAFLRALLNDEDSrWRnSPAVKEFLNL 107
FERM_F1_SNX27 cd01777
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin ...
 119-209 7.45e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in sorting nexin protein 27 (SNX27); SNX27 is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. In addition to a PX (Phox homology) domain that regulates its endosomal localization, SNX27 has a unique PDZ (Psd-95/Dlg/ZO1) domain and an atypical FERM (4.1, ezrin, radixin, moesin) domain that both function to bind short peptide sequence motifs in the cytoplasmic domains of the cargo receptors. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340475  Cd Length: 92  Bit Score: 46.91  E-value: 7.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462 119 LDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRfgkegKLSVVKKLADFELP---YVSLGSSEVE 195
Cdd:cd01777     5 LKVLLPDRTTVTVSVKKNSNTDQVYQALVEKLGMDSETANYFALFEII-----EYNFERKLQPNEFPhnlYIQNYSTASA 79

                          90
                  ....*....|....
gi 1034659462 196 NCkVGLRKWYMAPS 209
Cdd:cd01777    80 TC-ITLRKWLFTLA 92
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
 37-104 3.41e-06

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: 45.73  E-value: 3.41e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034659462  37 RYSQLHGWNEQLRRVFGncLPPFPPKYYLAMTTAMADERRDQLEQYLQNVTMDPNVlrSDVFVEFLKL 104
Cdd:cd06880    38 RYSEFHALHKKLKKSIK--TPDFPPKRVRNWNPKVLEQRRQGLEAYLQGLLKINEL--PKQLLDFLGV 101
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
 14-102 9.82e-06

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: 44.63  E-value: 9.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462  14 SDALGGRYVLYSV------HLDGFLFCRVRYSQLHGWNEQLRRVFGN----CLPPFPPKYYLA-----MTTAMADERRDQ 78
Cdd:cd07280    15 GDTGGGAYVVWKItietkdLIGSSIVAYKRYSEFVQLREALLDEFPRhkrnEIPQLPPKVPWYdsrvnLNKAWLEKRRRG 94

                          90       100
                  ....*....|....*....|....
gi 1034659462  79 LEQYLQNVTMDPNVLRSDVFVEFL 102
Cdd:cd07280    95 LQYFLNCVLLNPVFGGSPVVKEFL 118
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
 10-102 1.96e-05

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: 43.39  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462  10 SQQRSDALGGRYVLYSVHLDGFLFCRvRYSQLHGWNEQLRRVFGNCL-PPFPPK-----YYLAMTTA-----MADERRDQ 78
Cdd:cd06867     7 AGKSSEGGSGSYIVYVIRLGGSEVKR-RYSEFESLRKNLTRLYPTLIiPPIPEKhslkdYAKKPSKAkndakIIERRKRM 85

                          90       100
                  ....*....|....*....|....*
gi 1034659462  79 LEQYLQNVTMDPnVLRSD-VFVEFL 102
Cdd:cd06867    86 LQRFLNRCLQHP-ILRNDiVFQKFL 109
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
 37-102 5.02e-05

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: 43.07  E-value: 5.02e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462  37 RYSQLHGWNEQLRRVFGN-CLPPFPPKY---YLAMTTAMADERRDQLEQYLQNVTMDPNVLRSDVFVEFL 102
Cdd:cd06876    62 RYSEFLELHKYLKKRYPGvLKLDFPQKRkisLKYSKTLLVEERRKALEKYLQELLKIPEVCEDEEFRKFL 131
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 121-251 1.42e-04

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 42.67  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462  121 IFLPNEQSIRIEIITSDTAERVLEVVSHKIGL-CREllgYFGLFLIRFGKEGK--LSVVKKLADFElpyvslgsSEVENC 197
Cdd:smart00295   4 VYLLDGTTLEFEVDSSTTAEELLETVCRKLGIrESE---YFGLQFEDPDEDLRhwLDPAKTLLDQD--------VKSEPL 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034659462  198 KVGLRKWYMaPSLDSVLMDCRVAVDLLYMQAIQDIEKGWAKPTQAQRQKLEAFQ 251
Cdd:smart00295  73 TLYFRVKFY-PPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALA 125
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
 20-104 1.89e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; 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 SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132812  Cd Length: 112  Bit Score: 37.69  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034659462  20 RYVLYSVHL--DGFL-----FCRVRYSQLHGWNEQLRRVFGNCLPP--FPPKYYLA-MTTAMADERRDQLEQYLQNVTMD 89
Cdd:cd07279    17 KYVVYQLAVvqTGDPdtqpaFIERRYSDFLKLYKALRKQHPQLMAKvsFPRKVLMGnFSSELIAERSRAFEQFLGHILSI 96

                          90
                  ....*....|....*
gi 1034659462  90 PNVLRSDVFVEFLKL 104
Cdd:cd07279    97 PNLRDSKAFLDFLQG 111
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 37-102 2.20e-03

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: 37.56  E-value: 2.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034659462  37 RYSQLHGWNEQLRRVF-GNCLPPFPPKYYLAMTTAMAD---ERRDQLEQYLQNVTMDPnVLRSD-VFVEFL 102
Cdd:cd06859    42 RYSDFLWLYERLVEKYpGRIVPPPPEKQAVGRFKVKFEfieKRRAALERFLRRIAAHP-VLRKDpDFRLFL 111
PX_UP1_plant cd06879
The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX ...
 56-104 5.66e-03

The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a 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.


Pssm-ID: 132789  Cd Length: 138  Bit Score: 36.92  E-value: 5.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034659462  56 LPPFPPKYYLAMTT-AMADERRDQLEQYLQNVTMDPNVLRSDVFVEFLKL 104
Cdd:cd06879    88 LPAAPPKGLLRMKNrALLEERRHSLEEWMGKLLSDIDLSRSVPVASFLEL 137
 
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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