SNX17_BOVIN
ID SNX17_BOVIN Reviewed; 470 AA.
AC Q5EA77; Q17QP3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Sorting nexin-17;
GN Name=SNX17;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) 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 APP (via cytoplasmic
CC YXNPXY motif). Interacts with KIF1B (By similarity). Interacts with the
CC C-termini of P-selectin, PTC, LDLR, VLDLR, LRP1 and LRP8. Interacts
CC with KRIT1 (via N-terminus). Interacts with HRAS. Interacts with ITGB1
CC and ITGB5 (via NPxY motif). Interacts with CCDC22, CCDC93, VPS26C and
CC VPS35L; the interaction with VPS26C is direct and associates SNX17 with
CC the retriever and CCC complexes (By similarity).
CC {ECO:0000250|UniProtKB:Q15036, ECO:0000250|UniProtKB:Q8BVL3}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT020692; AAX08709.1; -; mRNA.
DR EMBL; BC118249; AAI18250.1; -; mRNA.
DR RefSeq; NP_001015638.1; NM_001015638.1.
DR AlphaFoldDB; Q5EA77; -.
DR BMRB; Q5EA77; -.
DR SMR; Q5EA77; -.
DR STRING; 9913.ENSBTAP00000025998; -.
DR PaxDb; Q5EA77; -.
DR PRIDE; Q5EA77; -.
DR Ensembl; ENSBTAT00000025998; ENSBTAP00000025998; ENSBTAG00000019515.
DR GeneID; 529972; -.
DR KEGG; bta:529972; -.
DR CTD; 9784; -.
DR VEuPathDB; HostDB:ENSBTAG00000019515; -.
DR VGNC; VGNC:35097; SNX17.
DR eggNOG; KOG3784; Eukaryota.
DR GeneTree; ENSGT00950000183212; -.
DR HOGENOM; CLU_041342_1_0_1; -.
DR InParanoid; Q5EA77; -.
DR OMA; RRHCVGV; -.
DR OrthoDB; 577861at2759; -.
DR TreeFam; TF318398; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000019515; Expressed in granulosa cell and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:AgBase.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; ISS:AgBase.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IEA:Ensembl.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:AgBase.
DR GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR GO; GO:0003279; P:cardiac septum development; IEA:Ensembl.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:AgBase.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..470
FT /note="Sorting nexin-17"
FT /id="PRO_0000238952"
FT DOMAIN 1..109
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 115..206
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 115..432
FT /note="FERM-like"
FT /evidence="ECO:0000250"
FT REGION 270..432
FT /note="PTB-like F3 module"
FT /evidence="ECO:0000250"
FT REGION 400..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36
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 38
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 62
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 75
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 MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15036"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15036"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15036"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15036"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15036"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15036"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15036"
SQ SEQUENCE 470 AA; 52825 MW; 3ABC73220EA919FE CRC64;
MHFSIPETES RSGDSGGSAY VAYNIHVNGV LHCRVRYSQL LGLHEQLRKE YGANVLPAFP
PKKLFSLTPA EVEQRREQLE KYMQAVRQDP LLGSSETFNS FLRRAQQETQ QVPTEEVSLE
VLLSNGQKVL VNVLTSDQTE DVLEAVAAKL DLPDDLIGYF SLFLVREKED GAFSFVRKLQ
EFELPYVSVT SLRSQEYKIV LRKSYWDSAY DDDVMENRVG LNLLYAQTVA DIERGWILVT
KEQHRQLKSL QEKVSKKEFL RLAQTLRHYG YLRFDACVAD FPEKDCPVVV SAGNSELSLQ
LRLPGQQLRE GSFRVTRMRC WRVTSSVPLP SGGTSSPGRG RGEVRLELAF EYLMSKDRLQ
WVTITSPQAI MMSICLQSMV DELMVKKSGG SIRKMLRRRV GGTLRRSDSQ QAVKSPPLLE
SPDASRESMV KLSSKLSAVS LRGIGTPGTD ASASDVHGNF AFEGIGDEDL
