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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  91 LFVIVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKFVVKGVVDRFSE 170
Cdd:cd06860    1 LFITVDNPEKHVTTLETYITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSVKGLLDRFSP 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 153791707 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNIFLTAK 206
Cdd:cd06860   81 EFVATRMRALHKFLNRIVEHPVLSFNEHLKVFLTAK 116

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  91 LFVIVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKFVVKGVVDRFSE 170
Cdd:cd06860    1 LFITVDNPEKHVTTLETYITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSVKGLLDRFSP 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 153791707 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNIFLTAK 206
Cdd:cd06860   81 EFVATRMRALHKFLNRIVEHPVLSFNEHLKVFLTAK 116

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707    94 IVDDPKKHVcTMETYITYRITTKStrvefDLPEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKfVVKGVVDRFSEEFV 173
Cdd:smart00312   1 VVEPEKIGD-GKHYYYVIEIETKT-----GLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGK-KLFGRLNNFSEEFI 73

                           90       100       110
                   ....*....|....*....|....*....|..
gi 153791707   174 ETRRKALDKFLKRITDHPVLS-FNEHFNIFLT 204
Cdd:smart00312  74 EKRRRGLEKYLQSLLNHPELInHSEVVLEFLE 105

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 227 KHVTGGYKLRTRPLEFAAIGDYLDTFALKLGTIDRIAQRIIKEEIEYLVELREYGPVYSTWSALEGELAEPLEGVSACIG 306
Cdd:cd07624    1 RNTSTMYLLKNRSPEFDKMNEYLTLFGEKLGTIERISQRIHKERIEYFDELKEYSPIFQLWSASETELAPLLEGVSSAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 307 NCSTALEELTDDMTEDFLPVLREYILYSDSMKSVLKKRDQVQAEYEAKLEAVALRKEDrpkVPADVEKCQDRMECFNADL 386
Cdd:cd07624   81 RCTAALEVLLSDHEFVFLPPLREYLLYSDAVKDVLKRRDQFQIEYELSVEELNKKRLE---LLKEVEKLQDKLECANADL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153791707 387 KADMERWQNNKRQDFRQLLMGMADKNIQYYEKCLMAWESIIPL 429
Cdd:cd07624  158 KADLERWKQNKRQDLKKILLDMAEKQIQYYEQCLAAWEEVLPA 200

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  91 LFVIVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKFVVKGVVDRFSE 170
Cdd:cd06860    1 LFITVDNPEKHVTTLETYITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSVKGLLDRFSP 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 153791707 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNIFLTAK 206
Cdd:cd06860   81 EFVATRMRALHKFLNRIVEHPVLSFNEHLKVFLTAK 116

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  91 LFVIVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKFVVKGVVDRFSE 170
Cdd:cd07284    1 IFITVDEPESHVTAIETFITYRVMTKTSRSEFDSSEFEVRRRYQDFLWLKGRLEEAHPTLIIPPLPEKFVMKGMVERFNE 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 153791707 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNIFLTAK 206
Cdd:cd07284   81 DFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 116

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  91 LFVIVDDPKKHVC-TMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKFVVKGVV-DRF 168
Cdd:cd06863    1 LECLVSDPQKELDgSSDTYISYLITTKTNLPSFSRKEFKVRRRYSDFVFLHECLSNDFPACVVPPLPDKHRLEYITgDRF 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 153791707 169 SEEFVETRRKALDKFLKRITDHPVLSFNEHFNIFLT 204
Cdd:cd06863   81 SPEFITRRAQSLQRFLRRISLHPVLSQSKILHQFLE 116

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  93 VIVDDPKKHVCTMETYITYRITTKSTrvefDLPEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKFVVKgvvdRFSEEF 172
Cdd:cd06093    2 VSIPDYEKVKDGGKKYVVYIIEVTTQ----GGEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFG----NLDPEF 73

                         90       100       110
                 ....*....|....*....|....*....|..
gi 153791707 173 VETRRKALDKFLKRITDHPVLSFNEHFNIFLT 204
Cdd:cd06093   74 IEERRKQLEQYLQSLLNHPELRNSEELKEFLE 105

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  93 VIVDDPKKHVCTME------TYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKFVVKGVVd 166
Cdd:cd06865    2 ITVSDPKKEQEPSRvplggpPYISYKVTTRTNIPSYTHGEFTVRRRFRDVVALADRLAEAYRGAFVPPRPDKSVVESQV- 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 153791707 167 RFSEEFVETRRKALDKFLKRITDHPVLSFNEHFNIFLTA 205
Cdd:cd06865   81 MQSAEFIEQRRVALEKYLNRLAAHPVIGLSDELRVFLTL 119

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 106 ETYITYRITTKSTR--VEFDLPE--YSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKFVV----KGVVDRFSEEFVETRR 177
Cdd:cd06864   21 ETYTVYLIETKIVEheSEEGLSKklSSLWRRYSEFELLRNYLVVTYPYVIVPPLPEKRAMfmwqKLSSDTFDPDFVERRR 100

                         90       100
                 ....*....|....*....|....*..
gi 153791707 178 KALDKFLKRITDHPVLSFNEHFNIFLT 204
Cdd:cd06864  101 AGLENFLLRVAGHPELCQDKIFLEFLT 127

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  95 VDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRSKLeESQPTH---LIPPLPEKFVVK------GVV 165
Cdd:cd07282    5 VSDPEKVGDGMNAYMAYRVTTKTSLSMFSRSEFSVRRRFSDFLGLHSKL-ASKYLHvgyIVPPAPEKSIVGmtkvkvGKE 83

                         90       100
                 ....*....|....*....|....*...
gi 153791707 166 DRFSEEFVETRRKALDKFLKRITDHPVL 193
Cdd:cd07282   84 DSSSTEFVEKRRAALERYLQRTVKHPTL 111

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  88 TRDLFVIVDDPKKHVCTME---TYITYRITTKSTRVEFDL---PEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEK-FV 160
Cdd:COG5391  128 DYFISSTVSNPQSLTLLVDsrdKHTSYEIITVTNLPSFQLresRPLVVRRRYSDFESLHSILIKLLPLCAIPPLPSKkSN 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 161 VKGVVDRFSEEFVETRRKALDKFLKRITDHPVLS-------FNEHFNIFLTAKDLNAYKKQGIAL-LTRMGESVKHVtgg 232
Cdd:COG5391  208 SEYYGDRFSDEFIEERRQSLQNFLRRVSTHPLLSnyknsksWESHSTLLSSFIENRKSVPTPLSLdLTSTTQELDME--- 284

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 233 yklRTRPLEFaaigdyLDTFALKLGTIDRIAQRIIKE------------EIEYLVELREygpvystwSALEGELAEPLE- 299
Cdd:COG5391  285 ---RKELNES------TSKAIHNILSIFSLFEKILIQleseeesltrllESLNNLLLLV--------LNFSGVFAKRLEq 347

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 300 ----GVSACIGNCSTALEELTDDMTEdFLPVLREYILYSDSMKSVLKKRDQVQAEYEAKLEAVAL--------------- 360
Cdd:COG5391  348 nqnsILNEGVVQAETLRSSLKELLTQ-LQDEIKSRESLILTDSNLEKLTDQNLEDVEELSRSLRKnssqravvsqqpegl 426

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 361 ------------------RKEDRPKVPADVEKCQDR-------MECFNADLKADMERWQNNKRQDFRQLLMGMADKNIQY 415
Cdd:COG5391  427 tsfsklsyklrdfvqeksRSKSIESLQQDKEKLEEQlaiaekdAQEINEELKNELKFFFSVRNSDLEKILKSVADSHIEW 506

                        410
                 ....*....|
gi 153791707 416 YEKCLMAWES 425
Cdd:COG5391  507 AEENLEIWKS 516

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  95 VDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRSKLEEsQPTHLIPPLPEK-----FVVKGVVDRFS 169
Cdd:cd06894    6 VVNPQTHGVGKKRFTDYEVRMRTNLPVFKKKESSVRRRYSDFEWLRSELER-DSKIVVPPLPGKalkrqLPFRGDDGIFE 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 153791707 170 EEFVETRRKALDKFLKRITDHPVLSFNEHFNIFLTAKDL 208
Cdd:cd06894   85 EEFIEERRKGLETFINKVAGHPLAQNEKCLHMFLQEETI 123

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Atg24p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Atg24p is involved in membrane fusion events at the vacuolar surface during pexophagy. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 241 EFAAIGDYLDTFALKLGTIDRIAQRIIKEEIEYLVELREYGPVYSTWSALE-GELAEPLEGVSACIGNCSTALEELTDDM 319
Cdd:cd07628    5 EFLEIREKSDKLDENLTKIDKIFAKVVKRQSDLSVDYADLATQFQKLGSLEsGEITEPFKIFSESLSQFSTSLRVLNKYT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 320 TEDFLPVLREYILYSDSMKSVLKKRDQVQAEYEAkLEAVALRKEdrpkvpadVEKCQDRMECFNADLKADMERWQNNKRQ 399
Cdd:cd07628   85 DENYLTSLKDLLHYILSLKNLIKLRDQKQLDYEE-LSDYLLTDE--------VENAKETSDAFNKEVLKEYPNFERIKKQ 155

                        170       180
                 ....*....|....*....|....*....
gi 153791707 400 DFRQLLMGMADKNIQYYEKCLMAWESIIP 428
Cdd:cd07628  156 EIKDSLGALADGHIDFYQGLVEDWEKVEP 184

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  93 VIVDDPKKHVCTMET-YITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEkfvvKGVVDRF-SE 170
Cdd:cd06898    2 VEVRDPRTHKEDDWGsYTDYEIFLHTNSMCFTLKTSCVRRRYSEFVWLRNRLQKNALLIQLPSLPP----KNLFGRFnNE 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 153791707 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNIFL 203
Cdd:cd06898   78 GFIEERQQGLQDFLEKVLQTPLLLSDSRLHLFL 110

The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  82 DDIDGETRDLFvivddpKKHVctmetyiTYRITTKSTrvefdlpEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKFVV 161
Cdd:cd06866    5 VELVPEKKGLF------LKHV-------EYEVSSKRF-------KSTVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIG 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 153791707 162 KGVvdrfSEEFVETRRKALDKFLKRITDHPVLSFNEHFNIFLTA 205
Cdd:cd06866   65 GSA----DREFLEARRRGLSRFLNLVARHPVLSEDELVRTFLTE 104

The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX9, also known as SH3PX1, is a cytosolic protein that interacts with proteins associated with clathrin-coated pits such as Cdc-42-associated tyrosine kinase 2 (ACK2). It contains an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature. The PX-BAR structural unit helps determine specific membrane localization. Through its SH3 domain, SNX9 binds class I polyproline sequences found in dynamin 1/2 and the WASP/N-WASP actin regulators. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis. Its array of interacting partners suggests that SNX9 functions at the interface between endocytosis and actin cytoskeletal organization.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707  94 IVDDPKK--HVCTMETYITYRITTKSTrvefdlpEYSVRRRYQDFDWLRSKLEESQPTHL-IPPLPEKfvvkGVVDRFSE 170
Cdd:cd07285    4 VVADPRKgsKMYGLKSYIEYQLTPTNT-------NRSVNHRYKHFDWLYERLLVKFGLAIpIPSLPDK----QVTGRFEE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 153791707 171 EFVETRRKALDKFLKRITDHPVLSFNEHFNIFLTAKDLNAYK 212
Cdd:cd07285   73 EFIKMRMERLQAWMTRMCRHPVISESEVFQQFLNFRDEKEWK 114

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 4; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It is also implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and leptin. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 227 KHVTGGYKLRTRPLEFAAIGDYLDTFALKLGTIDRIAQRIIKEEIEYLVELREYGPVYSTWSALEGELAEPLEGvsacIG 306
Cdd:cd07622    1 KALNASFRLRNPDKRFEDLKNYSDELQTNLNNLLKVRARLAERLYGVYKIHANYGRVFSEWSAIEKEMGDGLQK----AG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 307 NCSTALEELTDDMTED---FLPVLREYILYSDSMKSVLKKRDQVQAEYEAKLEAVALRKEdrpKVPADVEKCQDRMECFN 383
Cdd:cd07622   77 HYMDSYAASIDNGLEDeelIADQLKEYLFFADSLRAVCKKHELLQYDLEKAEDALANKKQ---QGEEAVKEAKDELNEFV 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 153791707 384 ADLKADMERWQNNKRQDFRQLLMGMADKNIQYYEKCLMAWESIIPLLQ 431
Cdd:cd07622  154 KKALEDVERFKKQKVRDLKEILISYAKLQIKLAKKGLQTWTNIKECLQ 201

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 107 TYITYRITtkstrVEFDLPEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKFVVKGVVDrfSEEFVETRRKALDKFLKR 186
Cdd:cd06897   14 PYTVYNIQ-----VRLPLRSYTVSRRYSEFVALHKQLESEVGIEPPYPLPPKSWFLSTSS--NPKLVEERRVGLEAFLRA 86

                 ....*
gi 153791707 187 ITDHP 191
Cdd:cd06897   87 LLNDE 91

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 257 GTIDRIAQRIIKEEIEYLVELREYGPVYSTWSALE--GELAEPLEGVSACIGNCSTALEELTDDMTEDFLPVLREYILYS 334
Cdd:cd07629   22 GGMEKVNRRITKRLGDLAEDMADLGGRFNAFSLEEqkSELAEALEKVGQAVDSTYLATEALVGSLYYNINEPLSESAQFA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 335 DSMKSVLKKRDQVQAEYEAKLEAValrKEDRPKVPADVEKCQdrmecfNADLKADMERWQNNKRQDFRQLLMGMADKNIQ 414
Cdd:cd07629  102 GVVRELLKYRKLKHVQYEMTKDSL---LESALVAASDDLVIS------STIKQKDLPRFQREREADLREILKNYSKYHKD 172

                        170
                 ....*....|..
gi 153791707 415 YYEKCLMAWESI 426
Cdd:cd07629  173 WAKQNLEAWKEA 184

The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 119 RVEFDLPE-YSVRRRYQDFDWLRSKLEESQPTHLIPPLPEK--FVVKgvvdrfSEEFVETRRKALDKFLKRITDHPVLSF 195
Cdd:cd06877   35 RAKGHEPQhWSVLRRYNEFYVLESKLTEFHGEFPDAPLPSRriFGPK------SYEFLESKREIFEEFLQKLLQKPELRG 108

                         90
                 ....*....|
gi 153791707 196 NEHFNIFLTA 205
Cdd:cd06877  109 SELLYDFLSP 118

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 104 TMETYITYRITTKSTRVEF--------DLPEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKFVVKGVVDrfseefVET 175
Cdd:cd06868   16 TSSGHVLYQIVVVTRLAAFksakhkeeDVVQFMVSKKYSEFEELYKKLSEKYPGTILPPLPRKALFVSESD------IRE 89

                         90       100       110
                 ....*....|....*....|....*....|.
gi 153791707 176 RRKALDKFLKRITDHPVLSFNEHFNIFLTAK 206
Cdd:cd06868   90 RRAAFNDFMRFISKDEKLANCPELLEFLGVK 120

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791707 126 EYSVRRRYQDFDWLRSKLEESQP-THLipPLPEKfvvKGVVDRFSEEFVETRRKALDKFLKRITDHPVLSFNEHFNIFLT 204
Cdd:cd06870   33 SWFVFRRYAEFDKLYESLKKQFPaSNL--KIPGK---RLFGNNFDPDFIKQRRAGLDEFIQRLVSDPKLLNHPDVRAFLQ 107

                 .
gi 153791707 205 A 205
Cdd:cd06870  108 M 108

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791707 124 LPEYS--VRRRYQDFDWLRSKLEESQpthLIPPLPEKFVVkGVVDRfseEFVETRRKALDKFLKRITDHPVLS 194
Cdd:cd06871   33 SPENSwqVIRRYNDFDLLNASLQISG---ISLPLPPKKLI-GNMDR---EFIAERQQGLQNYLNVILMNPILA 98