SNX17_MOUSE
ID SNX17_MOUSE Reviewed; 470 AA.
AC Q8BVL3; Q8R0N8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Sorting nexin-17;
GN Name=Snx17;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
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 [3]
RP INTERACTION WITH LDLR; VLDLR; LRP1 AND LRP8, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND FUNCTION.
RX PubMed=12169628; DOI=10.1093/emboj/cdf435;
RA Stockinger W., Sailler B., Strasser V., Recheis B., Fasching D., Kahr L.,
RA Schneider W.J., Nimpf J.;
RT "The PX-domain protein SNX17 interacts with members of the LDL receptor
RT family and modulates endocytosis of the LDL receptor.";
RL EMBO J. 21:4259-4267(2002).
RN [4]
RP INTERACTION WITH LRP1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16052210; DOI=10.1038/sj.emboj.7600756;
RA van Kerkhof P., Lee J., McCormick L., Tetrault E., Lu W., Schoenfish M.,
RA Oorschot V., Strous G.J., Klumperman J., Bu G.;
RT "Sorting nexin 17 facilitates LRP recycling in the early endosome.";
RL EMBO J. 24:2851-2861(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APP, AND TISSUE
RP SPECIFICITY.
RX PubMed=18276590; DOI=10.1074/jbc.m800642200;
RA Lee J., Retamal C., Cuitino L., Caruano-Yzermans A., Shin J.E.,
RA van Kerkhof P., Marzolo M.P., Bu G.;
RT "Adaptor protein sorting nexin 17 regulates amyloid precursor protein
RT trafficking and processing in the early endosomes.";
RL J. Biol. Chem. 283:11501-11508(2008).
RN [6]
RP INTERACTION WITH KIF1B.
RX PubMed=19967056; DOI=10.4196/kjpp.2008.12.4.199;
RA Seog D.H., Han J.;
RT "Sorting nexin 17 interacts directly with kinesin superfamily KIF1Bbeta
RT protein.";
RL Korean J. Physiol. Pharmacol. 12:199-204(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND SER-421, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409; SER-415 AND SER-421, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Critical regulator of endosomal recycling of numerous surface
CC proteins, including integrins, signaling receptor and channels
CC (PubMed:12169628, PubMed:16052210). Binds to NPxY sequences in the
CC cytoplasmic tails of target cargos (By similarity). Associates with
CC 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 (By similarity). Also
CC required for maintenance of normal cell surface levels of APP and LRP1
CC (PubMed:16052210, PubMed:18276590). Interacts with membranes containing
CC phosphatidylinositol 3-phosphate (PtdIns(3P)) (By similarity).
CC {ECO:0000250|UniProtKB:Q15036, ECO:0000269|PubMed:12169628,
CC ECO:0000269|PubMed:16052210, ECO:0000269|PubMed:18276590}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with APP (via cytoplasmic
CC YXNPXY motif) (PubMed:18276590). Interacts with KIF1B
CC (PubMed:19967056). Interacts with the C-termini of P-selectin, PTC,
CC LDLR, VLDLR, LRP1 and LRP8. Interacts with KRIT1 (via N-terminus)
CC (PubMed:12169628, PubMed:16052210). Interacts with HRAS. Interacts with
CC ITGB1 and ITGB5 (via NPxY motif). Interacts with CCDC22, CCDC93, VPS26C
CC and VPS35L; the interaction with VPS26C is direct and associates SNX17
CC with the retriever and CCC complexes (By similarity).
CC {ECO:0000250|UniProtKB:Q15036, ECO:0000269|PubMed:12169628,
CC ECO:0000269|PubMed:16052210, ECO:0000269|PubMed:18276590,
CC ECO:0000269|PubMed:19967056}.
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 -!- TISSUE SPECIFICITY: Detected in brain neurons (at protein level).
CC Broadly expressed, with highest levels in brain and placenta, and
CC lowest levels in colon, intestine and liver.
CC {ECO:0000269|PubMed:12169628, ECO:0000269|PubMed:18276590}.
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; AK077650; BAC36927.1; -; mRNA.
DR EMBL; AK077780; BAC37004.1; -; mRNA.
DR EMBL; AK156299; BAE33663.1; -; mRNA.
DR EMBL; BC026571; AAH26571.1; -; mRNA.
DR EMBL; BC023732; AAH23732.1; -; mRNA.
DR CCDS; CCDS19177.1; -.
DR RefSeq; NP_710147.1; NM_153680.2.
DR AlphaFoldDB; Q8BVL3; -.
DR BMRB; Q8BVL3; -.
DR SMR; Q8BVL3; -.
DR BioGRID; 234470; 2.
DR IntAct; Q8BVL3; 1.
DR STRING; 10090.ENSMUSP00000031029; -.
DR iPTMnet; Q8BVL3; -.
DR PhosphoSitePlus; Q8BVL3; -.
DR SwissPalm; Q8BVL3; -.
DR EPD; Q8BVL3; -.
DR jPOST; Q8BVL3; -.
DR MaxQB; Q8BVL3; -.
DR PaxDb; Q8BVL3; -.
DR PeptideAtlas; Q8BVL3; -.
DR PRIDE; Q8BVL3; -.
DR ProteomicsDB; 261466; -.
DR Antibodypedia; 28444; 166 antibodies from 27 providers.
DR DNASU; 266781; -.
DR Ensembl; ENSMUST00000031029; ENSMUSP00000031029; ENSMUSG00000029146.
DR GeneID; 266781; -.
DR KEGG; mmu:266781; -.
DR UCSC; uc008wxm.1; mouse.
DR CTD; 9784; -.
DR MGI; MGI:2387801; Snx17.
DR VEuPathDB; HostDB:ENSMUSG00000029146; -.
DR eggNOG; KOG3784; Eukaryota.
DR GeneTree; ENSGT00950000183212; -.
DR HOGENOM; CLU_041342_1_0_1; -.
DR InParanoid; Q8BVL3; -.
DR OMA; RRHCVGV; -.
DR OrthoDB; 577861at2759; -.
DR PhylomeDB; Q8BVL3; -.
DR TreeFam; TF318398; -.
DR BioGRID-ORCS; 266781; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Snx17; mouse.
DR PRO; PR:Q8BVL3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BVL3; protein.
DR Bgee; ENSMUSG00000029146; Expressed in medial ganglionic eminence and 248 other tissues.
DR ExpressionAtlas; Q8BVL3; baseline and differential.
DR Genevisible; Q8BVL3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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:MGI.
DR GO; GO:0005768; C:endosome; IPI:MGI.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0003279; P:cardiac septum development; IMP:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
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; IMP:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:MGI.
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_0000236205"
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..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:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
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"
FT CONFLICT 198
FT /note="K -> E (in Ref. 1; BAC37004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 52797 MW; 3023B5FAEF38BB42 CRC64;
MHFSIPETES RSGDSGGSAY VAYNIHVNGV LHCRVRYSQL LGLHEQLRKE YGANVVPAFP
PKKLFSLTPA EVEQRREQLE KYMQAVRQDP LLGSSETFNS FLRRAQQETQ QVPTEEVSLE
VLLSNGQKVL VTVLTSDQTE DVLEAVAAKL DLPDDLIGYF SLFLVREKED GAFSFVRKLQ
EFELPYVSVT SLRSQEYKIV LRKSYWDSAY DDDVMENRVG LNLLYAQTVS DIEHGWILVT
KEQHRQLKSL QEKVSKKEFL RLAQTLRHYG YLRFDACVAD FPEKDCPVVV SAGNSELSLQ
LRLPGQQLRE GSFRVTRMRC WRVTSSVPLP SGGTSSPSRG RGEVRLELAF EYLMSKDRLQ
WVTITSPQAI MMSICLQSMV DELMVKKSGG SIRKMLRRRV GGTLRRSDSQ QAVKSPPLLE
SPDASRESMV KLSSKLSAVS LRGIGSPSTD ASASAVHGNF AFEGIGDEDL
