GenomeNet

Database: UniProt
Entry: Q19532
LinkDB: Q19532
Original site: Q19532 
ID   SNX17_CAEEL             Reviewed;         540 AA.
AC   Q19532;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   17-JAN-2003, sequence version 2.
DT   10-APR-2019, entry version 110.
DE   RecName: Full=Sorting nexin-17 homolog {ECO:0000250|UniProtKB:Q15036};
GN   Name=snx-17 {ECO:0000312|WormBase:F17H10.3a};
GN   ORFNames=F17H10.3 {ECO:0000312|WormBase:F17H10.3a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Critical regulator of endosomal recycling of numerous
CC       receptors, channels, and other transmembrane proteins. Interacts
CC       with membranes containing phosphatidylinositol 3-phosphate
CC       (PtdIns(3P)). {ECO:0000250|UniProtKB:Q15036}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15036}.
CC       Early endosome {ECO:0000250|UniProtKB:Q15036}. Cytoplasmic vesicle
CC       membrane {ECO:0000250|UniProtKB:Q15036}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:Q15036}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q15036}.
CC   -!- DOMAIN: The PX domain mediates specific binding to
CC       phosphatidylinositol 3-phosphate (PtdIns(P3)).
CC       {ECO:0000250|UniProtKB:Q15036}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
DR   EMBL; Z69789; CAA93650.2; -; Genomic_DNA.
DR   PIR; T21077; T21077.
DR   RefSeq; NP_001076762.1; NM_001083293.2.
DR   UniGene; Cel.17803; -.
DR   ProteinModelPortal; Q19532; -.
DR   SMR; Q19532; -.
DR   STRING; 6239.F17H10.3a; -.
DR   PaxDb; Q19532; -.
DR   PeptideAtlas; Q19532; -.
DR   PRIDE; Q19532; -.
DR   EnsemblMetazoa; F17H10.3a; F17H10.3a; WBGene00008927.
DR   GeneID; 184624; -.
DR   KEGG; cel:CELE_F17H10.3; -.
DR   UCSC; F17H10.3a; c. elegans.
DR   CTD; 184624; -.
DR   WormBase; F17H10.3a; CE31483; WBGene00008927; snx-17.
DR   eggNOG; KOG3784; Eukaryota.
DR   eggNOG; ENOG410XT9I; LUCA.
DR   GeneTree; ENSGT00950000183212; -.
DR   HOGENOM; HOG000017719; -.
DR   InParanoid; Q19532; -.
DR   KO; K17929; -.
DR   OMA; SVCLQAM; -.
DR   OrthoDB; 577861at2759; -.
DR   PhylomeDB; Q19532; -.
DR   PRO; PR:Q19532; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00008927; Expressed in 4 organ(s), highest expression level in pharyngeal muscle cell (C elegans).
DR   ExpressionAtlas; Q19532; baseline and differential.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:1990126; P:retrograde transport, endosome to plasma membrane; IBA:GO_Central.
DR   CDD; cd13337; FERM-like_C_SNX17; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.30.1520.10; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR037831; SNX17/27/31.
DR   InterPro; IPR037836; SNX17_FERM-like_dom.
DR   PANTHER; PTHR12431; PTHR12431; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; SSF64268; 1.
DR   PROSITE; PS50195; PX; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Cytoplasmic vesicle; Endosome;
KW   Lipid-binding; Membrane; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN         1    540       Sorting nexin-17 homolog. {ECO:0000305}.
FT                                /FTId=PRO_0000213877.
FT   DOMAIN       67    176       PX. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00147}.
FT   BINDING     102    102       Phosphatidylinositol 3-phosphate.
FT                                {ECO:0000250|UniProtKB:Q08826}.
FT   BINDING     104    104       Phosphatidylinositol 3-phosphate; via
FT                                amide nitrogen and carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q08826}.
FT   BINDING     129    129       Phosphatidylinositol 3-phosphate.
FT                                {ECO:0000250|UniProtKB:Q08826}.
FT   BINDING     142    142       Phosphatidylinositol 3-phosphate.
FT                                {ECO:0000250|UniProtKB:Q08826}.
SQ   SEQUENCE   540 AA;  62901 MW;  0061DDEC6F45162F CRC64;
     MVSSAAMARS NGDKPSTSSM EEDLEIEQSM RNASIIDHQY EKEENKNHRV LNAFDPADKT
     TFSDMIHVDV PDTKTLVERS DGITKYTAYN IHINGWYHGS VRFSHLYEFA ELIKQKFSQR
     YKGPEFPAKK LFKLDPKAID ERRQKITKYF QALVQHPEVA RHYLVEKKLL GFQIDSFRAT
     SQYVTLDVFL GNGEKTTIKC LVSDSTLEIM KIICEKLGFK NKDQFIYHFG LFMAKGRDPT
     NACYSVTTEN FNPLLTRFLR NFEAPFVSLS TANQKYNENG HYHFLCLRKL IWDSRVEEPL
     LDDGNFVELL YKQAMQDYKN GHMDPVKEDL DSKLKSCMAR NDSKMFLRTC HQLSTYSYEI
     MSPCSCDYPK PGTPCEIKFG RRQIIMTTRD ETGKPKPSIF RATRIRVWRI TQVMDKISFQ
     FEYLMAKDTF EWITLDTDQS ILMSLLLQSI GSEILYEHNN MTIEQQVMKE KHSKGNYVEK
     SEKLPRDPKK PIIVLKNEVE DTDPLGVMEH YHNYNRMLTT ISDGIPQRNQ AFTDITNDDL
//
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