SNX17_RAT
ID SNX17_RAT Reviewed; 470 AA.
AC Q6AYS6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Sorting nexin-17;
GN Name=Snx17;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415; SER-421; SER-437 AND
RP SER-440, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
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DR EMBL; BC078931; AAH78931.1; -; mRNA.
DR RefSeq; NP_001011981.1; NM_001011981.1.
DR AlphaFoldDB; Q6AYS6; -.
DR BMRB; Q6AYS6; -.
DR SMR; Q6AYS6; -.
DR IntAct; Q6AYS6; 2.
DR STRING; 10116.ENSRNOP00000029617; -.
DR iPTMnet; Q6AYS6; -.
DR PhosphoSitePlus; Q6AYS6; -.
DR jPOST; Q6AYS6; -.
DR PaxDb; Q6AYS6; -.
DR PRIDE; Q6AYS6; -.
DR GeneID; 298836; -.
DR KEGG; rno:298836; -.
DR CTD; 9784; -.
DR RGD; 1306424; Snx17.
DR eggNOG; KOG3784; Eukaryota.
DR InParanoid; Q6AYS6; -.
DR OrthoDB; 577861at2759; -.
DR PhylomeDB; Q6AYS6; -.
DR PRO; PR:Q6AYS6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:RGD.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0035904; P:aorta development; ISO:RGD.
DR GO; GO:0003279; P:cardiac septum development; ISO:RGD.
DR GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
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 1: Evidence at protein 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_0000236206"
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 401..425
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 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:0007744|PubMed:22673903"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 470 AA; 52882 MW; CB8CB7D8F89469D7 CRC64;
MHFSIPETES RSGDSGGSTY VAYNIHVNGV LHCRVRYSQL LGLHEQLRKE YGANVLPAFP
PKKLFSLTPA EVEQRREQLE KYMQAVRQDP LLGSSETFNS FLRRAQQETQ QVPTEEVSLE
VLLSDGQKVL VNVLTSDQTE DVLEAVAAKL DLPDDLIGYF SLFLVREKED GAFSFVRKLQ
EFELPYVSVT SLRSQEYKIV LRKSYWDSAY DDDVMENRVG LNLLYAQTVS DIEHGWILVT
KEQHRQLKSL QEKVSKKEFL RLAQTLRHYG YLRFDACVAD FPEKDCPVVV SAGNSELSLQ
LRLPGQQLRE GSFRVTRMRC WRVTSSVPLP SGGTSTPSRG RGEVRLELAF EYLMSKDRLQ
WVTITSPQAI MMSICLQSMV DELMVKKSGG SIRKMLRRRV GGNLRRSDSQ QAVKSPPLLE
SPDASRESMV KLSSKLSAVS LRGIGSPSTD ASASAVHGNF AFEGIGDEDL
