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 27-MAR-2024, entry version 153. 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}. 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; 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; 3. 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; 10090-ENSMUSP00000031029; -. DR PeptideAtlas; Q8BVL3; -. DR ProteomicsDB; 261466; -. DR Pumba; Q8BVL3; -. DR Antibodypedia; 28444; 178 antibodies from 27 providers. DR DNASU; 266781; -. DR Ensembl; ENSMUST00000031029.15; ENSMUSP00000031029.9; ENSMUSG00000029146.15. DR GeneID; 266781; -. DR KEGG; mmu:266781; -. DR UCSC; uc008wxm.1; mouse. DR AGR; MGI:2387801; -. 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; 5487301at2759; -. DR PhylomeDB; Q8BVL3; -. DR TreeFam; TF318398; -. DR BioGRID-ORCS; 266781; 7 hits in 79 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 252 other cell types or tissues. DR ExpressionAtlas; Q8BVL3; baseline and differential. 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: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 CDD; cd16121; FERM_F1_SNX17; 1. DR CDD; cd06885; PX_SNX17_31; 1. DR Gene3D; 1.20.80.60; -; 1. DR Gene3D; 3.30.1520.10; Phox-like domain; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR048763; SNX17-31_FERM_F1. DR InterPro; IPR048767; SNX17-31_FERM_F2. DR InterPro; IPR037831; SNX17/27/31-like. DR InterPro; IPR040842; SNX17/31_FERM. DR InterPro; IPR037836; SNX17_FERM-like_dom. DR InterPro; IPR028666; SNX17_FERM_N. DR PANTHER; PTHR12431; SORTING NEXIN 17 AND 27; 1. DR PANTHER; PTHR12431:SF16; SORTING NEXIN-17; 1. DR Pfam; PF00787; PX; 1. DR Pfam; PF21273; SNX17-27-31_F1_FERM; 1. DR Pfam; PF21271; SNX17-31_F2_FERM; 1. DR Pfam; PF18116; SNX17_FERM_C; 1. DR SMART; SM00312; PX; 1. DR SUPFAM; SSF64268; PX domain; 1. DR PROSITE; PS50195; PX; 1. DR PROSITE; PS50200; RA; 1. DR Genevisible; Q8BVL3; MM. 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 //