SNX17_DANRE
ID SNX17_DANRE Reviewed; 473 AA.
AC Q5RID7; B3DI45;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Sorting nexin-17;
GN Name=snx17; ORFNames=si:ch211-101l18.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Critical regulator of endosomal recycling of numerous surface
CC proteins, including integrins, signaling receptor and channels. Binds
CC to NPxY sequences in the cytoplasmic tails of target cargos. Associates
CC with retriever and CCC complexes to prevent lysosomal degradation and
CC promote cell surface recycling of numerous cargos such as integrins
CC ITGB1, ITGB5 and their associated alpha subunits. Also required for
CC maintenance of normal cell surface levels of APP and LRP1. Interacts
CC with membranes containing phosphatidylinositol 3-phosphate
CC (PtdIns(3P)). {ECO:0000250|UniProtKB:Q15036,
CC ECO:0000250|UniProtKB:Q8BVL3}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with CCDC22, CCDC93, DSCR3
CC and VPS35L; the interaction with DSCR3 is direct and associates SNX17
CC with the retriever and CCC complexes (By similarity).
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)). Required for association with endosomes.
CC {ECO:0000250|UniProtKB:Q15036}.
CC -!- DOMAIN: The PTB-like F3 module within the FERM-like domain mediates
CC cargo recognition via their NPxY sequences, while the F1 module (Ras-
CC associating) is responsible for interaction with membrane-bound HRAS.
CC {ECO:0000250|UniProtKB:Q15036}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; BX276101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC162993; AAI62993.1; -; mRNA.
DR RefSeq; NP_001038622.2; NM_001045157.3.
DR RefSeq; XP_009292899.1; XM_009294624.1.
DR AlphaFoldDB; Q5RID7; -.
DR SMR; Q5RID7; -.
DR STRING; 7955.ENSDARP00000040190; -.
DR PaxDb; Q5RID7; -.
DR PRIDE; Q5RID7; -.
DR Ensembl; ENSDART00000040191; ENSDARP00000040190; ENSDARG00000091418.
DR GeneID; 568263; -.
DR KEGG; dre:568263; -.
DR CTD; 9784; -.
DR ZFIN; ZDB-GENE-030131-9475; snx17.
DR eggNOG; KOG3784; Eukaryota.
DR GeneTree; ENSGT00950000183212; -.
DR InParanoid; Q5RID7; -.
DR OrthoDB; 577861at2759; -.
DR PhylomeDB; Q5RID7; -.
DR TreeFam; TF318398; -.
DR PRO; PR:Q5RID7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000091418; Expressed in cleaving embryo and 26 other tissues.
DR ExpressionAtlas; Q5RID7; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProt.
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; IPR000159; RA_dom.
DR InterPro; IPR028666; SNX17.
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 PANTHER; PTHR12431:SF16; PTHR12431:SF16; 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.
DR PROSITE; PS50200; RA; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; Endosome; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..473
FT /note="Sorting nexin-17"
FT /id="PRO_0000238953"
FT DOMAIN 1..108
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 114..205
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 114..433
FT /note="FERM-like"
FT /evidence="ECO:0000250"
FT REGION 269..433
FT /note="PTB-like F3 module"
FT /evidence="ECO:0000250"
FT REGION 391..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35
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"
FT BINDING 37
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"
FT BINDING 61
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"
FT BINDING 74
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"
FT CONFLICT 395
FT /note="Missing (in Ref. 2; AAI62993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 53618 MW; CE328362A354A43B CRC64;
MHFSIPETEV RSDENGSSYV AYNIHVNGVL HCRVRYSQLL GLHEQIKKEY GNNVVPAFPP
KKIFTLTPAE VDQRREQLEK YMQAVRQDPI LGSSEMFNSF LRKAQQETQQ IPTEEVQLEI
YLSNGQKVKV NILTSDQTED VLEAVASKLD LPDELVGYFS LFLVQERADG SCTYVRKLQE
FELPYVSITS LHSSDYRIIL RKSYWDTAYD SDVMDDRVGL NLLYAQTVSD IDRGWILVNK
EQHRQLKSLQ EKGSKKEFIR LAQTLKYYGY IKFDPCITDF PEKGCHVIVG AGNNELNFHV
KLPNEQMKEG SFKVTRMRCW RVTSSQVPVA NGTANPSSSS KCDVKLELAF EYLMSKDRLQ
WVTITSQQAI MMSICLQSMV DELMVKKSGG SIKKQMQKKR LNGSLQRSDS QQAVKSPPIL
DSPDPNREQV VKLSTKLSSV SLRGLSSSNS AGDISGNDFH GNYAFEGIGD DDL
