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Conserved domains on  [gi|39930455|ref|NP_083150|]
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sorting nexin-19 [Mus musculus]

Protein Classification

PX domain-containing protein( domain architecture ID 10645683)

PX (Phox Homology) domain-containing protein with PXA (PX associated) and nexin C-terminal domains, may bind phosphoinositides; with similarity to sorting nexin-14 but lacking the regulator of G protein signaling (RGS) domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
537-664 8.02e-71

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: 230.89  E-value: 8.02e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 537 NLRITGTITAREHSGTGFHPYTLYTVKYETVLNGENS-----SGLQQLAYHTVNRRYREFLNLQTRLEEKPDLRKFIkNV 611
Cdd:cd06893   1 NIRIPKTITAKEYKGTGTHPYTLYTVQYETILDVQSEqnpnaASEQPLATHTVNRRFREFLTLQTRLEENPKFRKIM-NV 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 39930455 612 KGPKKLFPDLPFGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFLALN 664
Cdd:cd06893  80 KGPPKRLFDLPFGNMDKDKIEARRGLLETFLRQLCSIPEISNSEEVQEFLAYG 132
PXA smart00313
Domain associated with PX domains; unpubl. observations
95-273 5.08e-66

Domain associated with PX domains; unpubl. observations


:

Pssm-ID: 214611  Cd Length: 176  Bit Score: 219.21  E-value: 5.08e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455     95 ERQLEQEINRTIQMIIRDFVLSWYRSVSHEPAFEAEMEAAMKGLVQELRRRMSIVDSHALtqrVLTLCGCHLQSYIQ-AK 173
Cdd:smart00313   1 PAQLEEPLQLLISKIIRDYVQGWYKGVSEDPSFLREIEQTLEYILRQLYRRLSRQDSAHL---ILYEILKNLISTITnAL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455    174 EATAKEQScPVQPSQLWDAYCQVTAPHPAMSCPTTEVTYARGIVNLILKELVPKPHLETRTGRHVVVEVITCNVILPLIS 253
Cdd:smart00313  78 EAVLRFAS-PQIPSTEIDLQYAETAIHKALSSPSNELTYRRQLVEMLLKFLLPEDSLCSRLHRCLLREVLAMQVILPLIT 156
                          170       180
                   ....*....|....*....|
gi 39930455    254 KLSDPDWIHLILVSIFSKYR 273
Cdd:smart00313 157 HLSDPDTINLCIILLFSSSR 176
Nexin_C pfam08628
Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the ...
843-950 1.97e-32

Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the sorting nexin family. It is found on proteins which also contain pfam00787.


:

Pssm-ID: 462541  Cd Length: 111  Bit Score: 121.57  E-value: 1.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455   843 WLCTESM---QKFLHIIFGTLVQRWLEVQVANLTCPQRWAQYLHLLRESIWPGGVLPKfPRPGRTQAQKAATEKQALQSL 919
Cdd:pfam08628   1 WLRRRALnalKQVLQQLLGDTIERKLRESVEWLTSEEQVASYIRLLRDALWPGGLLAE-PPPERTEEEKLRTRKEARKLL 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 39930455   920 MDLLPDFLVEILGVNKCRLSWSLVLESFQQP 950
Cdd:pfam08628  80 LSLIPDALGSVVGRENAREAARRVFDMLQNP 110
 
Name Accession Description Interval E-value
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
537-664 8.02e-71

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: 230.89  E-value: 8.02e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 537 NLRITGTITAREHSGTGFHPYTLYTVKYETVLNGENS-----SGLQQLAYHTVNRRYREFLNLQTRLEEKPDLRKFIkNV 611
Cdd:cd06893   1 NIRIPKTITAKEYKGTGTHPYTLYTVQYETILDVQSEqnpnaASEQPLATHTVNRRFREFLTLQTRLEENPKFRKIM-NV 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 39930455 612 KGPKKLFPDLPFGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFLALN 664
Cdd:cd06893  80 KGPPKRLFDLPFGNMDKDKIEARRGLLETFLRQLCSIPEISNSEEVQEFLAYG 132
PXA smart00313
Domain associated with PX domains; unpubl. observations
95-273 5.08e-66

Domain associated with PX domains; unpubl. observations


Pssm-ID: 214611  Cd Length: 176  Bit Score: 219.21  E-value: 5.08e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455     95 ERQLEQEINRTIQMIIRDFVLSWYRSVSHEPAFEAEMEAAMKGLVQELRRRMSIVDSHALtqrVLTLCGCHLQSYIQ-AK 173
Cdd:smart00313   1 PAQLEEPLQLLISKIIRDYVQGWYKGVSEDPSFLREIEQTLEYILRQLYRRLSRQDSAHL---ILYEILKNLISTITnAL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455    174 EATAKEQScPVQPSQLWDAYCQVTAPHPAMSCPTTEVTYARGIVNLILKELVPKPHLETRTGRHVVVEVITCNVILPLIS 253
Cdd:smart00313  78 EAVLRFAS-PQIPSTEIDLQYAETAIHKALSSPSNELTYRRQLVEMLLKFLLPEDSLCSRLHRCLLREVLAMQVILPLIT 156
                          170       180
                   ....*....|....*....|
gi 39930455    254 KLSDPDWIHLILVSIFSKYR 273
Cdd:smart00313 157 HLSDPDTINLCIILLFSSSR 176
PXA pfam02194
PXA domain; This domain is associated with PX domains pfam00787.
97-268 5.71e-45

PXA domain; This domain is associated with PX domains pfam00787.


Pssm-ID: 460484  Cd Length: 181  Bit Score: 160.09  E-value: 5.71e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455    97 QLEQEINRTIQMIIRDFVLSWYRSVSHEPAFEAEMEAAMKGLVQELRRRMSIVD-SHALTQRVLTLCGCHLQSYIQAKEA 175
Cdd:pfam02194   3 EVDAALDELIDLIIRDFVQSWYSKISSDPEFPNEVRQTLRHALRELSQRLRKVDlASLLLSRLLPLLTSHLEDYRKAEEA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455   176 TAKEQscPVQPSQLWDAYCQVTAPHPAMSC--------PTTEVTYARGIVNLILKELVPKPHLETRTGRHVVVEVITCNV 247
Cdd:pfam02194  83 VRGKK--LNELDLALASKYLALKPHPALSPvllsssqsREAEQKYLRLLVDGLLPLLLPPEDLESRPVRVLVREILACLV 160
                         170       180
                  ....*....|....*....|.
gi 39930455   248 ILPLISKLSDPDWIHLILVSI 268
Cdd:pfam02194 161 LLPVINKLSDPDFINELIVKL 181
Nexin_C pfam08628
Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the ...
843-950 1.97e-32

Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the sorting nexin family. It is found on proteins which also contain pfam00787.


Pssm-ID: 462541  Cd Length: 111  Bit Score: 121.57  E-value: 1.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455   843 WLCTESM---QKFLHIIFGTLVQRWLEVQVANLTCPQRWAQYLHLLRESIWPGGVLPKfPRPGRTQAQKAATEKQALQSL 919
Cdd:pfam08628   1 WLRRRALnalKQVLQQLLGDTIERKLRESVEWLTSEEQVASYIRLLRDALWPGGLLAE-PPPERTEEEKLRTRKEARKLL 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 39930455   920 MDLLPDFLVEILGVNKCRLSWSLVLESFQQP 950
Cdd:pfam08628  80 LSLIPDALGSVVGRENAREAARRVFDMLQNP 110
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
544-661 3.81e-17

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: 77.77  E-value: 3.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455    544 ITAREHSGTGFHPYTLYTVKYETVLngenssglqqlAYHTVNRRYREFLNLQTRLeekpdLRKFiknvkgPKKLFPDLP- 622
Cdd:smart00312   1 VVEPEKIGDGKHYYYVIEIETKTGL-----------EEWTVSRRYSDFLELHSKL-----KKHF------PRSILPPLPg 58
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 39930455    623 ------FGNMDSDRVEARKSLLESFLKQLCAIPEIGN-SEEVQEFL 661
Cdd:smart00312  59 kklfgrLNNFSEEFIEKRRRGLEKYLQSLLNHPELINhSEVVLEFL 104
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
577-661 1.30e-16

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 75.74  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455   577 QQLAYHTVNRRYREFLNLQTRLEEKPDLRKFiknvkgpkklfPDLP----FGNMDSDRVEARKSLLESFLKQLCAIPEIG 652
Cdd:pfam00787   4 FSLEEWSVRRRYSDFVELHKKLLRKFPSVII-----------PPLPpkrwLGRYNEEFIEKRRKGLEQYLQRLLQHPELR 72

                  ....*....
gi 39930455   653 NSEEVQEFL 661
Cdd:pfam00787  73 NSEVLLEFL 81
 
Name Accession Description Interval E-value
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
537-664 8.02e-71

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: 230.89  E-value: 8.02e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 537 NLRITGTITAREHSGTGFHPYTLYTVKYETVLNGENS-----SGLQQLAYHTVNRRYREFLNLQTRLEEKPDLRKFIkNV 611
Cdd:cd06893   1 NIRIPKTITAKEYKGTGTHPYTLYTVQYETILDVQSEqnpnaASEQPLATHTVNRRFREFLTLQTRLEENPKFRKIM-NV 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 39930455 612 KGPKKLFPDLPFGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFLALN 664
Cdd:cd06893  80 KGPPKRLFDLPFGNMDKDKIEARRGLLETFLRQLCSIPEISNSEEVQEFLAYG 132
PXA smart00313
Domain associated with PX domains; unpubl. observations
95-273 5.08e-66

Domain associated with PX domains; unpubl. observations


Pssm-ID: 214611  Cd Length: 176  Bit Score: 219.21  E-value: 5.08e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455     95 ERQLEQEINRTIQMIIRDFVLSWYRSVSHEPAFEAEMEAAMKGLVQELRRRMSIVDSHALtqrVLTLCGCHLQSYIQ-AK 173
Cdd:smart00313   1 PAQLEEPLQLLISKIIRDYVQGWYKGVSEDPSFLREIEQTLEYILRQLYRRLSRQDSAHL---ILYEILKNLISTITnAL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455    174 EATAKEQScPVQPSQLWDAYCQVTAPHPAMSCPTTEVTYARGIVNLILKELVPKPHLETRTGRHVVVEVITCNVILPLIS 253
Cdd:smart00313  78 EAVLRFAS-PQIPSTEIDLQYAETAIHKALSSPSNELTYRRQLVEMLLKFLLPEDSLCSRLHRCLLREVLAMQVILPLIT 156
                          170       180
                   ....*....|....*....|
gi 39930455    254 KLSDPDWIHLILVSIFSKYR 273
Cdd:smart00313 157 HLSDPDTINLCIILLFSSSR 176
PXA pfam02194
PXA domain; This domain is associated with PX domains pfam00787.
97-268 5.71e-45

PXA domain; This domain is associated with PX domains pfam00787.


Pssm-ID: 460484  Cd Length: 181  Bit Score: 160.09  E-value: 5.71e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455    97 QLEQEINRTIQMIIRDFVLSWYRSVSHEPAFEAEMEAAMKGLVQELRRRMSIVD-SHALTQRVLTLCGCHLQSYIQAKEA 175
Cdd:pfam02194   3 EVDAALDELIDLIIRDFVQSWYSKISSDPEFPNEVRQTLRHALRELSQRLRKVDlASLLLSRLLPLLTSHLEDYRKAEEA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455   176 TAKEQscPVQPSQLWDAYCQVTAPHPAMSC--------PTTEVTYARGIVNLILKELVPKPHLETRTGRHVVVEVITCNV 247
Cdd:pfam02194  83 VRGKK--LNELDLALASKYLALKPHPALSPvllsssqsREAEQKYLRLLVDGLLPLLLPPEDLESRPVRVLVREILACLV 160
                         170       180
                  ....*....|....*....|.
gi 39930455   248 ILPLISKLSDPDWIHLILVSI 268
Cdd:pfam02194 161 LLPVINKLSDPDFINELIVKL 181
Nexin_C pfam08628
Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the ...
843-950 1.97e-32

Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the sorting nexin family. It is found on proteins which also contain pfam00787.


Pssm-ID: 462541  Cd Length: 111  Bit Score: 121.57  E-value: 1.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455   843 WLCTESM---QKFLHIIFGTLVQRWLEVQVANLTCPQRWAQYLHLLRESIWPGGVLPKfPRPGRTQAQKAATEKQALQSL 919
Cdd:pfam08628   1 WLRRRALnalKQVLQQLLGDTIERKLRESVEWLTSEEQVASYIRLLRDALWPGGLLAE-PPPERTEEEKLRTRKEARKLL 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 39930455   920 MDLLPDFLVEILGVNKCRLSWSLVLESFQQP 950
Cdd:pfam08628  80 LSLIPDALGSVVGRENAREAARRVFDMLQNP 110
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
537-661 6.74e-18

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: 80.09  E-value: 6.74e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 537 NLRITGTITAREhsgtGFHPYTLYTVKYETvlngenssglQQLAYHTVNRRYREFLNLQTRLEEKpdlrkfiknvkGPKK 616
Cdd:cd06093   1 SVSIPDYEKVKD----GGKKYVVYIIEVTT----------QGGEEWTVYRRYSDFEELHEKLKKK-----------FPGV 55
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 39930455 617 LFPDLP----FGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd06093  56 ILPPLPpkklFGNLDPEFIEERRKQLEQYLQSLLNHPELRNSEELKEFL 104
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
544-661 3.81e-17

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: 77.77  E-value: 3.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455    544 ITAREHSGTGFHPYTLYTVKYETVLngenssglqqlAYHTVNRRYREFLNLQTRLeekpdLRKFiknvkgPKKLFPDLP- 622
Cdd:smart00312   1 VVEPEKIGDGKHYYYVIEIETKTGL-----------EEWTVSRRYSDFLELHSKL-----KKHF------PRSILPPLPg 58
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 39930455    623 ------FGNMDSDRVEARKSLLESFLKQLCAIPEIGN-SEEVQEFL 661
Cdd:smart00312  59 kklfgrLNNFSEEFIEKRRRGLEKYLQSLLNHPELINhSEVVLEFL 104
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
577-661 1.30e-16

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 75.74  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455   577 QQLAYHTVNRRYREFLNLQTRLEEKPDLRKFiknvkgpkklfPDLP----FGNMDSDRVEARKSLLESFLKQLCAIPEIG 652
Cdd:pfam00787   4 FSLEEWSVRRRYSDFVELHKKLLRKFPSVII-----------PPLPpkrwLGRYNEEFIEKRRKGLEQYLQRLLQHPELR 72

                  ....*....
gi 39930455   653 NSEEVQEFL 661
Cdd:pfam00787  73 NSEVLLEFL 81
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
533-661 4.17e-11

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: 61.56  E-value: 4.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 533 VVIQNlritgTITAREHSGTGFhpyTLYTVKYETVLNGENSSGLqqlayhTVNRRYREFLNLQTRLEEK-PDLRkfikNV 611
Cdd:cd06876  22 VSIQS-----YISDVEEEGKEF---VVYLIEVQRLNNDDQSSGW------VVARRYSEFLELHKYLKKRyPGVL----KL 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 39930455 612 KGPKKLFPDLPFGNmdSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd06876  84 DFPQKRKISLKYSK--TLLVEERRKALEKYLQELLKIPEVCEDEEFRKFL 131
PX_SNX27 cd06886
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a ...
586-662 2.04e-09

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: 55.88  E-value: 2.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 586 RRYREFLNLQTRLeekpdlrkfiknvkgpKKLFPDLPFGNMDS--------DRVEARKSLLESFLKQLCAIPEIGNSEEV 657
Cdd:cd06886  36 RRYREFANLHQNL----------------KKEFPDFQFPKLPGkwpfslseQQLDARRRGLEQYLEKVCSIRVIGESDIM 99

                ....*
gi 39930455 658 QEFLA 662
Cdd:cd06886 100 QDFLS 104
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
538-661 2.69e-09

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: 55.72  E-value: 2.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 538 LRITGTITAREHSGTgfhPYTLYTVKYEtvlngenssglqqlaYHTVNRRYREFLNLQTRLE------------EKPDLR 605
Cdd:cd06867   2 IQIVDAGKSSEGGSG---SYIVYVIRLG---------------GSEVKRRYSEFESLRKNLTrlyptliippipEKHSLK 63
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 39930455 606 KFIKNVKGPKKlfpdlpfgnmDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd06867  64 DYAKKPSKAKN----------DAKIIERRKRMLQRFLNRCLQHPILRNDIVFQKFL 109
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
556-663 4.46e-08

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: 51.89  E-value: 4.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 556 PYTLYTVKYETvlngenssglqQLAYHTVNRRYREFLNLQTRLEekPDLRKFIKnVKGPKKLFpdLPFGNMDSDRVEARK 635
Cdd:cd06897  14 PYTVYNIQVRL-----------PLRSYTVSRRYSEFVALHKQLE--SEVGIEPP-YPLPPKSW--FLSTSSNPKLVEERR 77
                        90       100       110
                ....*....|....*....|....*....|
gi 39930455 636 SLLESFLKQLCAIPE--IGNSEEVQEFLAL 663
Cdd:cd06897  78 VGLEAFLRALLNDEDsrWRNSPAVKEFLNL 107
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
556-661 7.80e-08

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: 51.99  E-value: 7.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 556 PYTLYTVkyETVLNGENSSGLQQLAYHTVNRRYREFLNLQTRLeekpdlrkfikNVKGPKKLFPDLP-----FG------ 624
Cdd:cd06864  22 TYTVYLI--ETKIVEHESEEGLSKKLSSLWRRYSEFELLRNYL-----------VVTYPYVIVPPLPekramFMwqklss 88
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 39930455 625 -NMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd06864  89 dTFDPDFVERRRAGLENFLLRVAGHPELCQDKIFLEFL 126
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
540-661 8.57e-08

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: 51.98  E-value: 8.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 540 ITGTITAREHSGTGFHPYTLYTVKYETVLNGENSSglqqlaYHTVNRRYREFLNLQTRLEEKPDLRKFI------KNVKG 613
Cdd:cd07281   1 LKVSITDPEKIGDGMNAYVVYKVTTQTSLLMFRSK------HFTVKRRFSDFLGLYEKLSEKHSQNGFIvppppeKSLIG 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 39930455 614 PKKlfpdLPFGNMDSDR---VEARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd07281  75 MTK----VKVGKEDSSSaefLERRRAALERYLQRIVSHPSLLQDPDVREFL 121
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
584-664 8.57e-08

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: 51.56  E-value: 8.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 584 VNRRYREFLNLQTRLeeKPDLRKFIKNVKGPKKLFpdlpFGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFLAL 663
Cdd:cd07279  38 IERRYSDFLKLYKAL--RKQHPQLMAKVSFPRKVL----MGNFSSELIAERSRAFEQFLGHILSIPNLRDSKAFLDFLQG 111

                .
gi 39930455 664 N 664
Cdd:cd07279 112 P 112
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
551-661 9.68e-08

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: 51.43  E-value: 9.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 551 GTGFHPYTLYTVKYETVLNGENSSGLQqlayhtVNRRYREFLNLQTRLEEK---------PDlrkfiKNVKGpkKLFPDL 621
Cdd:cd06859  12 GDGMSAYVVYRVTTKTNLPDFKKSEFS------VLRRYSDFLWLYERLVEKypgrivpppPE-----KQAVG--RFKVKF 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 39930455 622 PFgnmdsdrVEARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd06859  79 EF-------IEKRRAALERFLRRIAAHPVLRKDPDFRLFL 111
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
584-664 2.65e-07

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: 50.10  E-value: 2.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 584 VNRRYREFLNLQTRLEE-KPDLRKFIKnvkgPKKLFPDlpfgNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFLA 662
Cdd:cd07276  37 VFRRYTDFVRLNDKLKQmFPGFRLSLP----PKRWFKD----NFDPDFLEERQLGLQAFVNNIMAHKDIAKCKLVREFFC 108

                ..
gi 39930455 663 LN 664
Cdd:cd07276 109 LD 110
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
535-661 2.65e-07

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: 50.40  E-value: 2.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 535 IQNLRITG-TITAREHSGTGfhpYTLYTVKYETvlngENSSGLQQLAYhtvnRRYREFLNLQTRLEE--KPDLRKFIknv 611
Cdd:cd07280   2 ATDVNVGDyTIVGGDTGGGA---YVVWKITIET----KDLIGSSIVAY----KRYSEFVQLREALLDefPRHKRNEI--- 67
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 39930455 612 kgpkklfPDLP--------FGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd07280  68 -------PQLPpkvpwydsRVNLNKAWLEKRRRGLQYFLNCVLLNPVFGGSPVVKEFL 118
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
540-662 1.22e-06

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: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 540 ITGTITAREHSGTgfhpYTLY--TVKYETVLNGENSsglqqlaYHTVnRRYREFLNLQTRLEEK-PDLRKfiknVKGPKK 616
Cdd:cd06873   9 IINTGIVKEHGKT----YAVYaiSVTRIYPNGQEES-------WHVY-RRYSDFHDLHMRLKEKfPNLSK----LSFPGK 72
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 39930455 617 LFpdlpFGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFLA 662
Cdd:cd06873  73 KT----FNNLDRAFLEKRRKMLNQYLQSLLNPEVLDANPGLQEIVL 114
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
583-661 2.74e-06

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: 47.27  E-value: 2.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 583 TVNRRYREFLNLQTRL--EEKPDlrkfiKNVKGPKKLfpdlpFGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEF 660
Cdd:cd06875  32 TVKHRYSDFAELHDKLvaEHKVD-----KDLLPPKKL-----IGNKSPSFVEKRRKELEIYLQTLLSFFQKTMPRELAHF 101

                .
gi 39930455 661 L 661
Cdd:cd06875 102 L 102
PX_RPK118_like cd07287
The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a ...
555-661 8.74e-06

The phosphoinositide binding Phox Homology domain of RPK118-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 bear similarity to human RPK118, which contains an N-terminal PX domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. It also binds the antioxidant peroxiredoxin-3 (PRDX3) and may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. Members of this subfamily also show similarity to sorting nexin 15 (SNX15), which contains PX and MIT domains but does not contain a kinase 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.


Pssm-ID: 132820  Cd Length: 118  Bit Score: 45.73  E-value: 8.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 555 HP--YTLYTVKYEtVLNGENSSGLQQLayhTVNRRYREFLNLQTrleekpDLRKFIKNVKGPKKLFPDLP----FGNMDS 628
Cdd:cd07287  13 HPkgYTVYKVTAR-IVSRKNPEDVQEI---VVWKRYSDFKKLHK------DLWQIHKNLCRQSELFPPFAkakvFGRFDE 82
                        90       100       110
                ....*....|....*....|....*....|...
gi 39930455 629 DRVEARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd07287  83 SVIEERRQCAEDLLQFSANIPALYNSSQLEDFF 115
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
533-651 1.09e-05

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: 45.40  E-value: 1.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 533 VVIQNLRItgtitareHSGTGFHPYTLYTVKYETvlngeNSSGLQqLAYHTVNRRYREFLNLQTRLEEKPDLRKfiknvk 612
Cdd:cd06898   2 VEVRDPRT--------HKEDDWGSYTDYEIFLHT-----NSMCFT-LKTSCVRRRYSEFVWLRNRLQKNALLIQ------ 61
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 39930455 613 gPKKLFPDLPFGNMDSDR-VEARKSLLESFLKQLCAIPEI 651
Cdd:cd06898  62 -LPSLPPKNLFGRFNNEGfIEERQQGLQDFLEKVLQTPLL 100
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
556-661 4.33e-05

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: 43.49  E-value: 4.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 556 PYTLYTVKYETvlngenSSGLQQLAYHTVNRRYREFLNLQTRLEEKpdlrkfiknvkGPKKLFPDLP----FGNMDSDRV 631
Cdd:cd06861  17 AHTVYTVRTRT------TSPNFEVSSFSVLRRYRDFRWLYRQLQNN-----------HPGVIVPPPPekqsVGRFDDNFV 79
                        90       100       110
                ....*....|....*....|....*....|
gi 39930455 632 EARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd06861  80 EQRRAALEKMLRKIANHPVLQKDPDFRLFL 109
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
540-661 5.36e-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: 43.09  E-value: 5.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 540 ITGTITAREHSGTGfhpYTLYTVKyetvLNGenssglqqlAYH-TVnrRYREFLNLQtrleEKpdLRKFIKNVKG----P 614
Cdd:cd06885   4 IPDTQELSDEGGST---YVAYNIH----ING---------VLHcSV--RYSQLHGLN----EQ--LKKEFGNRKLppfpP 59
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 39930455 615 KKLFPdlpfgnMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd06885  60 KKLLP------LTPAQLEERRLQLEKYLQAVVQDPRIANSDIFNSFL 100
PX_SNX3 cd07293
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a ...
544-661 6.47e-05

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: 43.44  E-value: 6.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 544 ITAREHSGTGFHPYTLYTVKYETVLNgenssgLQQLAYHTVNRRYREFLNLQTRLEEKPDLrkFIKNVKGpKKLFPDLPF 623
Cdd:cd07293   6 VTNPQTVGVGRGRFTTYEIRLKTNLP------IFKLKESTVRRRYSDFEWLRSELERESKV--VVPPLPG-KALFRQLPF 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 39930455 624 ----GNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd07293  77 rgddGIFDDSFIEERKQGLEQFLNKVAGHPLAQNERCLHMFL 118
PX_p40phox cd06882
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ...
537-661 1.21e-04

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: 42.81  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 537 NLRITGTItAREHSGTGFHPYTLYTVkyETVLNGENSsglqqlayHTVNRRYREFLNLQTRLEEkpdlRKFIKNVKGPK- 615
Cdd:cd06882   1 DVAVSATI-ADIEEKRGFTNYYVFVI--EVKTKGGSK--------YLIYRRYRQFFALQSKLEE----RFGPEAGSSAYd 65
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 39930455 616 KLFPDLP----FGNmDSDRVEARKSLLESFLKQLCAIP-EIGNSEEVQEFL 661
Cdd:cd06882  66 CTLPTLPgkiyVGR-KAEIAERRIPLLNRYMKELLSLPvWVLMDEDVRLFF 115
PX_SNX19_like_plant cd06872
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; ...
544-664 1.54e-04

The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like 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 plant proteins containing an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some sorting nexins (SNXs). This is the same domain architecture found in SNX19. SNX13 and SNX14 also contain these three domains but also contain 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. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132782  Cd Length: 107  Bit Score: 42.12  E-value: 1.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 544 ITAREHSGTGFHPYTLYTVkyeTVLNGENSSglqqlayHTVNRRYREFLNLQTRLEEKPDLrkfikNVKGPKKLFPDLpf 623
Cdd:cd06872   5 VLGAEIVKSGSKSFAVYSV---AVTDNENET-------WVVKRRFRNFETLHRRLKEVPKY-----NLELPPKRFLSS-- 67
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 39930455 624 gNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFLALN 664
Cdd:cd06872  68 -SLDGAFIEERCKLLDKYLKDLLVIEKVAESHEVWSFLSAR 107
PX_UP2_fungi cd06869
The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX ...
577-661 3.38e-04

The phosphoinositide binding Phox Homology domain of uncharacterized fungal 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: 132779  Cd Length: 119  Bit Score: 41.11  E-value: 3.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 577 QQLAYHTVNRRYREFLNLQTRLeekpdLRKFiknvkgPKKLFPDLPFGNMdSDRVEARKSLlESFLKQLCAIPEIGNSEE 656
Cdd:cd06869  45 EEYRTIYVARRYSDFKKLHHDL-----KKEF------PGKKLPKLPHKDK-LPREKLRLSL-RQYLRSLLKDPEVAHSSI 111

                ....*
gi 39930455 657 VQEFL 661
Cdd:cd06869 112 LQEFL 116
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
583-661 5.78e-04

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: 40.81  E-value: 5.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 583 TVNRRYREFLNLQTRLEekpdlrkfiknVKG------PKKLFpdlpfGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEE 656
Cdd:cd06871  39 QVIRRYNDFDLLNASLQ-----------ISGislplpPKKLI-----GNMDREFIAERQQGLQNYLNVILMNPILASCLP 102

                ....*
gi 39930455 657 VQEFL 661
Cdd:cd06871 103 VKKFL 107
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
543-661 7.61e-04

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: 40.35  E-value: 7.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 543 TITAREHSGTGFHPYTLYTVKYETVLNGENSSGLQqlayhtVNRRYREFLNLQTRLEEK-------PDLRKFIknVKGPK 615
Cdd:cd07284   4 TVDEPESHVTAIETFITYRVMTKTSRSEFDSSEFE------VRRRYQDFLWLKGRLEEAhptliipPLPEKFV--MKGMV 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 39930455 616 KLFPDlpfgnmdsDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd07284  76 ERFNE--------DFIETRRKALHKFLNRIADHPTLTFNEDFKIFL 113
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
584-661 1.31e-03

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: 39.63  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 584 VNRRYREFLNLQTRLEEkpdlrkfiknvKGPKKLFPDLP-----FGNMD---SDRVEARKSLLESFLKQLCAIPEIGNSE 655
Cdd:cd06860  39 VRRRYQDFLWLRQKLEE-----------SHPTHIIPPLPekhsvKGLLDrfsPEFVATRMRALHKFLNRIVEHPVLSFNE 107

                ....*.
gi 39930455 656 EVQEFL 661
Cdd:cd06860 108 HLKVFL 113
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
547-665 1.52e-03

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: 39.18  E-value: 1.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 547 REHSGTGfHPYTLYTVKyetVLngenSSGLQqlayHTVNRRYREFLNLQTRleekpdLRKFIKNVKGPKKLFPDLpfgnm 626
Cdd:cd06880  10 LEVDESE-KPYTVFTIE---VL----VNGRR----HTVEKRYSEFHALHKK------LKKSIKTPDFPPKRVRNW----- 66
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 39930455 627 dSDRV-EARKSLLESFLKQLCAIPEIgnSEEVQEFLALNT 665
Cdd:cd06880  67 -NPKVlEQRRQGLEAYLQGLLKINEL--PKQLLDFLGVRH 103
PX_SNX20 cd07300
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a ...
584-661 1.55e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; 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. 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. The PX domain of SNX20 binds PIs and targets the SNX20/PSGL-1 complex to endosomes. SNX20 may function in the sorting and cycling of PSGL-1 into endosomes.


Pssm-ID: 132833  Cd Length: 114  Bit Score: 39.41  E-value: 1.55e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930455 584 VNRRYREFLNLQTRLEEkpDLRKFIKNVKGPKKLFPdlpfGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFL 661
Cdd:cd07300  38 IERRYSDFLKLHQELLS--DFSEELEDVVFPKKKLT----GNFSEEIIAERRVALRDYLTLLYSLRFVRRSQAFQDFL 109
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
583-661 4.38e-03

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: 38.07  E-value: 4.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 583 TVNRRYREFLNLQTRLeekpdLRKFiknvkgPKKLFPDLP----FGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQ 658
Cdd:cd06862  33 TVSRRYKHFDWLYERL-----VEKY------SCIAIPPLPekqvTGRFEEDFIEKRRERLELWMNRLARHPVLSQSEVFR 101

                ...
gi 39930455 659 EFL 661
Cdd:cd06862 102 HFL 104
PX_SNX15_like cd06881
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ...
543-660 5.63e-03

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: 37.68  E-value: 5.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930455 543 TIT-AREHSGTgfhpYTLYTVKYETVLNgensSGLQQLAYHTVNRRYREFlnlqTRLEEkpDLRKFIKNVKGPKKlFPDL 621
Cdd:cd06881   6 TVTdTRRHKKG----YTEYKITSKVFSR----SVPEDVSEVVVWKRYSDF----KKLHR--ELSRLHKQLYLSGS-FPPF 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 39930455 622 P----FGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEF 660
Cdd:cd06881  71 PkgkyFGRFDAAVIEERRQAILELLDFVGNHPALYQSSAFQQF 113
 
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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