NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|225543217|ref|NP_001038839|]
View 

sorting nexin-22 [Danio rerio]

Protein Classification

PX domain-containing protein( domain architecture ID 10160756)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
 11-121 5.10e-52

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: 163.60  E-value: 5.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217  11 IEVFIPSLMREVDETGKLRKLFRVEILFNGRKHFVLRRHGEFQTLHRKVKKILRVPDFPSKRNQHLRTKPLEQRRQELED 90
Cdd:cd06880    1 IEVSIPSYRLEVDESEKPYTVFTIEVLVNGRRHTVEKRYSEFHALHKKLKKSIKTPDFPPKRVRNWNPKVLEQRRQGLEA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 225543217  91 YIQVILYQNDvVPQELLDFLQVKHFHPTSKN 121
Cdd:cd06880   81 YLQGLLKINE-LPKQLLDFLGVRHFPSLPKS 110
 
Name Accession Description Interval E-value
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
 11-121 5.10e-52

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: 163.60  E-value: 5.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217  11 IEVFIPSLMREVDETGKLRKLFRVEILFNGRKHFVLRRHGEFQTLHRKVKKILRVPDFPSKRNQHLRTKPLEQRRQELED 90
Cdd:cd06880    1 IEVSIPSYRLEVDESEKPYTVFTIEVLVNGRRHTVEKRYSEFHALHKKLKKSIKTPDFPPKRVRNWNPKVLEQRRQGLEA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 225543217  91 YIQVILYQNDvVPQELLDFLQVKHFHPTSKN 121
Cdd:cd06880   81 YLQGLLKINE-LPKQLLDFLGVRHFPSLPKS 110
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 38-112 4.74e-07

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 46.08  E-value: 4.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217   38 FNGRKHFVLRRHGEFQTLHRKVKK---ILRVPDFPSKRnQHLRTKP--LEQRRQELEDYIQVILyQNDVVPQ--ELLDFL 110
Cdd:pfam00787   4 FSLEEWSVRRRYSDFVELHKKLLRkfpSVIIPPLPPKR-WLGRYNEefIEKRRKGLEQYLQRLL-QHPELRNseVLLEFL 81


                  ..
gi 225543217  111 QV 112
Cdd:pfam00787  82 ES 83
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 31-96 5.32e-05

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: 41.18  E-value: 5.32e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225543217    31 LFRVEILFNGRKHFVLRRHGEFQTLHRKVKKI---LRVPDFPSK----RNQHLRTKPLEQRRQELEDYIQVIL 96
Cdd:smart00312  16 VIEIETKTGLEEWTVSRRYSDFLELHSKLKKHfprSILPPLPGKklfgRLNNFSEEFIEKRRRGLEKYLQSLL 88
 
Name Accession Description Interval E-value
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
 11-121 5.10e-52

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: 163.60  E-value: 5.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217  11 IEVFIPSLMREVDETGKLRKLFRVEILFNGRKHFVLRRHGEFQTLHRKVKKILRVPDFPSKRNQHLRTKPLEQRRQELED 90
Cdd:cd06880    1 IEVSIPSYRLEVDESEKPYTVFTIEVLVNGRRHTVEKRYSEFHALHKKLKKSIKTPDFPPKRVRNWNPKVLEQRRQGLEA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 225543217  91 YIQVILYQNDvVPQELLDFLQVKHFHPTSKN 121
Cdd:cd06880   81 YLQGLLKINE-LPKQLLDFLGVRHFPSLPKS 110
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
 12-96 4.55e-08

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: 50.00  E-value: 4.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217  12 EVFIPSLMREVDETGKLRKLFRVEILFNGRKHF-----VLRRHGEFQTLHRKVKK---ILRVPDFPSKRNQHLR---TKP 80
Cdd:cd06876   21 RVSIQSYISDVEEEGKEFVVYLIEVQRLNNDDQssgwvVARRYSEFLELHKYLKKrypGVLKLDFPQKRKISLKyskTLL 100

                         90
                 ....*....|....*.
gi 225543217  81 LEQRRQELEDYIQVIL 96
Cdd:cd06876  101 VEERRKALEKYLQELL 116
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 31-111 3.63e-07

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 46.97  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217  31 LFRVEI-LFNGRKHFVLRRHGEFQTLHRKVKK---ILRVPDFPSKRNQH-LRTKPLEQRRQELEDYIQVILYQNDVV-PQ 104
Cdd:cd06093   19 VYIIEVtTQGGEEWTVYRRYSDFEELHEKLKKkfpGVILPPLPPKKLFGnLDPEFIEERRKQLEQYLQSLLNHPELRnSE 98


                 ....*..
gi 225543217 105 ELLDFLQ 111
Cdd:cd06093   99 ELKEFLE 105
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 38-112 4.74e-07

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 46.08  E-value: 4.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217   38 FNGRKHFVLRRHGEFQTLHRKVKK---ILRVPDFPSKRnQHLRTKP--LEQRRQELEDYIQVILyQNDVVPQ--ELLDFL 110
Cdd:pfam00787   4 FSLEEWSVRRRYSDFVELHKKLLRkfpSVIIPPLPPKR-WLGRYNEefIEKRRKGLEQYLQRLL-QHPELRNseVLLEFL 81


                  ..
gi 225543217  111 QV 112
Cdd:pfam00787  82 ES 83
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 15-111 3.39e-06

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: 44.24  E-value: 3.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217  15 IPSLMREVDETGKLRKLFRVEIlfNGRKHFVLRrHGEFQTLHRKVKKIL---RVPDFPSKRNQHLRTKPLEQRRQELEDY 91
Cdd:cd06885    4 IPDTQELSDEGGSTYVAYNIHI--NGVLHCSVR-YSQLHGLNEQLKKEFgnrKLPPFPPKKLLPLTPAQLEERRLQLEKY 80

                         90       100
                 ....*....|....*....|.
gi 225543217  92 IQVILYQNDVVPQELL-DFLQ 111
Cdd:cd06885   81 LQAVVQDPRIANSDIFnSFLL 101
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
 19-112 3.15e-05

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


Pssm-ID: 132780  Cd Length: 109  Bit Score: 41.62  E-value: 3.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217  19 MREVDETGKLRKLFRVEILFNGRKHFVLRRHGEFQTLHRKVKKilRVPD----FPSKR--NQHLRTKPLEQRRQELEDYI 92
Cdd:cd06870   10 SDEDREKKKRFTVYKVVVSVGRSSWFVFRRYAEFDKLYESLKK--QFPAsnlkIPGKRlfGNNFDPDFIKQRRAGLDEFI 87

                         90       100
                 ....*....|....*....|.
gi 225543217  93 QVILYQNDVVPQ-ELLDFLQV 112
Cdd:cd06870   88 QRLVSDPKLLNHpDVRAFLQM 108
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
 31-113 3.36e-05

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: 41.49  E-value: 3.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217  31 LFRVEILFNGRKHFVLRRHGEFQTLHRKVKK---ILRVPDFPSKR---NQHLRTKPLEQRRQELEDYIQVILYQNDV--- 101
Cdd:cd06897   17 VYNIQVRLPLRSYTVSRRYSEFVALHKQLESevgIEPPYPLPPKSwflSTSSNPKLVEERRVGLEAFLRALLNDEDSrwr 96

                         90
                 ....*....|..
gi 225543217 102 VPQELLDFLQVK 113
Cdd:cd06897   97 NSPAVKEFLNLP 108
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 31-96 5.32e-05

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: 41.18  E-value: 5.32e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225543217    31 LFRVEILFNGRKHFVLRRHGEFQTLHRKVKKI---LRVPDFPSK----RNQHLRTKPLEQRRQELEDYIQVIL 96
Cdd:smart00312  16 VIEIETKTGLEEWTVSRRYSDFLELHSKLKKHfprSILPPLPGKklfgRLNNFSEEFIEKRRRGLEKYLQSLL 88
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
 13-110 2.75e-04

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


Pssm-ID: 132787  Cd Length: 119  Bit Score: 39.28  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217  13 VFIPSL-MREVDETGKLRKLF-----RVEILFNG--RKHF-VLRRHGEFQTLHRKVKKI---LRVPDFPSKRNQHLRTKP 80
Cdd:cd06877    5 VSIPYVeMRRDPSNGERIYVFcieveRNDRRAKGhePQHWsVLRRYNEFYVLESKLTEFhgeFPDAPLPSRRIFGPKSYE 84

                         90       100       110
                 ....*....|....*....|....*....|..
gi 225543217  81 -LEQRRQELEDYIQVILYQNDVVPQELL-DFL 110
Cdd:cd06877   85 fLESKREIFEEFLQKLLQKPELRGSELLyDFL 116
PX_SNX27 cd06886
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a ...
 42-93 3.98e-04

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: 38.55  E-value: 3.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 225543217  42 KHFVLRRHGEFQTLHRKVKKILR---VPDFPSKRNQHLRTKPLEQRRQELEDYIQ 93
Cdd:cd06886   31 RQLCSRRYREFANLHQNLKKEFPdfqFPKLPGKWPFSLSEQQLDARRRGLEQYLE 85
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
 45-96 4.50e-04

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.


Pssm-ID: 132810  Cd Length: 118  Bit Score: 38.87  E-value: 4.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 225543217  45 VLRRHGEFQTLHRKVKK---ILRVPDFPSKR---NQHlrTKPLEQRRQELEDYIQVIL 96
Cdd:cd07277   34 VYRRYSEFYELHKKLKKkfpVVRSFDFPPKKaigNKD--AKFVEERRKRLQVYLRRVV 89
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
 45-113 6.09e-04

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: 38.40  E-value: 6.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217  45 VLRRHGEFQTLHRKVKKilRVPD-----FPSKRNQH-LRTKPLEQRRQELEDYIQVILyQNDVVP-----QELL-DFLQV 112
Cdd:cd06873   43 VYRRYSDFHDLHMRLKE--KFPNlsklsFPGKKTFNnLDRAFLEKRRKMLNQYLQSLL-NPEVLDanpglQEIVlDFLEP 119


                 .
gi 225543217 113 K 113
Cdd:cd06873  120 G 120
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
 34-116 1.81e-03

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: 36.87  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217  34 VEILFNGRKHFVLRRHGEFQTLHRKV-------KKILrvPdfPSKRNQHLRTKPLEQRRQELEDYIQVIL-YQNDVVPQE 105
Cdd:cd06875   22 IEVKVGSVEWTVKHRYSDFAELHDKLvaehkvdKDLL--P--PKKLIGNKSPSFVEKRRKELEIYLQTLLsFFQKTMPRE 97

                         90
                 ....*....|.
gi 225543217 106 LLDFLqvkHFH 116
Cdd:cd06875   98 LAHFL---DFH 105
PX_PLD cd06895
The phosphoinositide binding Phox Homology domain of Phospholipase D; The PX domain is a ...
 30-112 2.37e-03

The phosphoinositide binding Phox Homology domain of Phospholipase D; 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. Phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond of phosphatidylcholine to generate membrane-bound phosphatidic acid and choline. Members of this subfamily contain PX and Pleckstrin Homology (PH) domains in addition to the catalytic domain. PLD activity has been detected in viruses, bacteria, yeast, plants, and mammals, but the PX domain is not present in PLDs from viruses and bacteria. PLDs are implicated in many cellular functions like signaling, cytoskeletal reorganization, vesicular transport, stress responses, and the control of differentiation, proliferation, and survival. Vertebrates contain two PLD isozymes, PLD1 and PLD2. PLD1 is located mainly in intracellular membranes while PLD2 is associated with plasma membranes. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132805  Cd Length: 140  Bit Score: 36.98  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543217  30 KLFRV--EILFNGRKHFVLRRHGEFQTLHRKVKKILRVPDFPSKRNQHLRTKPLEQRRQELEDYIQVILYQNDVVP-QEL 106
Cdd:cd06895   54 KLYRAllRIPLPTRRHKEERLSLKRSRKPEREKKNRRLPSLPALPDILVSEEQLDSRKKQLENYLQNLLKIPDYRNhPET 133


                 ....*.
gi 225543217 107 LDFLQV 112
Cdd:cd06895  134 LEFLEV 139
PX_SNX25 cd06878
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ...
 45-96 3.13e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; 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. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.


Pssm-ID: 132788  Cd Length: 127  Bit Score: 36.58  E-value: 3.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 225543217  45 VLRRHGEFQTLHRKVKKI---LRVPDFPS---KRNQHLRTKPLEQRRQELEDYIQVIL 96
Cdd:cd06878   52 VTRKLSEFHDLHRKLKECsswLKKVELPSlskKWFKSIDKKFLDKSKNQLQKYLQFIL 109
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH