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   03-AUG-2022, entry version 123.
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 investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Critical regulator of endosomal recycling of numerous
CC       receptors, channels, and other transmembrane proteins. Interacts with
CC       membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)).
CC       {ECO:0000250|UniProtKB:Q15036}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15036}. Early
CC       endosome {ECO:0000250|UniProtKB:Q15036}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:Q15036}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q15036}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q15036}.
CC   -!- DOMAIN: The PX domain mediates specific binding to phosphatidylinositol
CC       3-phosphate (PtdIns(P3)). {ECO:0000250|UniProtKB:Q15036}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR   EMBL; Z69789; CAA93650.2; -; Genomic_DNA.
DR   PIR; T21077; T21077.
DR   RefSeq; NP_001076762.1; NM_001083293.2.
DR   AlphaFoldDB; Q19532; -.
DR   SMR; Q19532; -.
DR   STRING; 6239.F17H10.3a; -.
DR   PaxDb; Q19532; -.
DR   PeptideAtlas; Q19532; -.
DR   PRIDE; Q19532; -.
DR   EnsemblMetazoa; F17H10.3a.1; F17H10.3a.1; 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   GeneTree; ENSGT00950000183212; -.
DR   InParanoid; Q19532; -.
DR   OMA; RRHCVGV; -.
DR   OrthoDB; 577861at2759; -.
DR   PhylomeDB; Q19532; -.
DR   PRO; PR:Q19532; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00008927; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
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   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; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR037831; SNX17/27/31.
DR   InterPro; IPR040842; SNX17/31_FERM.
DR   InterPro; IPR037836; SNX17_FERM-like_dom.
DR   PANTHER; PTHR12431; PTHR12431; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF18116; SNX17_FERM_C; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; SSF64268; 1.
DR   PROSITE; PS50195; PX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoplasmic vesicle; Endosome; Lipid-binding; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..540
FT                   /note="Sorting nexin-17 homolog"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000213877"
FT   DOMAIN          67..176
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         102
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250|UniProtKB:Q08826"
FT   BINDING         104
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250|UniProtKB:Q08826"
FT   BINDING         129
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250|UniProtKB:Q08826"
FT   BINDING         142
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="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