ID SNX17_HUMAN Reviewed; 470 AA. AC Q15036; B4DQM7; Q53HN7; Q6IAS3; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 213. DE RecName: Full=Sorting nexin-17; GN Name=SNX17; Synonyms=KIAA0064; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584044; DOI=10.1093/dnares/1.5.223; RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., RA Kawarabayasi Y., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. II. The RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 1:223-229(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Wightman P.J., Bonthron D.T.; RT "Genomic structure of the KIAA064 gene."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Adipose tissue; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph, Muscle, Placenta, and Testis; 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 [9] RP PROTEIN SEQUENCE OF 1-11. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [10] RP SUBCELLULAR LOCATION, AND INTERACTION WITH P-SELECTIN. RX PubMed=11237770; DOI=10.1006/bbrc.2001.4467; RA Florian V., Schlueter T., Bohnensack R.; RT "A new member of the sorting nexin family interacts with the C-terminus of RT P-selectin."; RL Biochem. Biophys. Res. Commun. 281:1045-1050(2001). RN [11] RP INTERACTION WITH LDLR, MUTAGENESIS OF LYS-62, AND SUBCELLULAR LOCATION. RX PubMed=14739284; DOI=10.1074/jbc.m313689200; RA Burden J.J., Sun X.-M., Garcia Garcia A.B., Soutar A.K.; RT "Sorting motifs in the intracellular domain of the low density lipoprotein RT receptor interact with a novel domain of sorting nexin-17."; RL J. Biol. Chem. 279:16237-16245(2004). RN [12] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=15121882; DOI=10.1091/mbc.e04-02-0143; RA Williams R., Schlueter T., Roberts M.S., Knauth P., Bohnensack R., RA Cutler D.F.; RT "Sorting nexin 17 accelerates internalization yet retards degradation of P- RT selectin."; RL Mol. Biol. Cell 15:3095-3105(2004). RN [13] RP SUBCELLULAR LOCATION, INTERACTION WITH P-SELECTIN; LRP1 AND PTC, AND RP FUNCTION. RX PubMed=15769472; DOI=10.1016/j.jmb.2005.02.004; RA Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V., RA Schreckenberger S., Hahn H., Bohnensack R.; RT "Functions of sorting nexin 17 domains and recognition motif for P-selectin RT trafficking."; RL J. Mol. Biol. 347:813-825(2005). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KRIT1. RX PubMed=16712798; DOI=10.1016/j.bbrc.2006.04.129; RA Czubayko M., Knauth P., Schluter T., Florian V., Bohnensack R.; RT "Sorting nexin 17, a non-self-assembling and a PtdIns(3)P high class RT affinity protein, interacts with the cerebral cavernous malformation RT related protein KRIT1."; RL Biochem. Biophys. Res. Commun. 345:1264-1272(2006). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415; SER-421; SER-437 AND RP SER-440, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP FUNCTION, AND INTERACTION WITH LRP1. RX PubMed=19005208; DOI=10.1091/mbc.e08-08-0805; RA Donoso M., Cancino J., Lee J., van Kerkhof P., Retamal C., Bu G., RA Gonzalez A., Caceres A., Marzolo M.P.; RT "Polarized traffic of LRP1 involves AP1B and SNX17 operating on Y-dependent RT sorting motifs in different pathways."; RL Mol. Biol. Cell 20:481-497(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; SER-415 AND SER-421, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-440, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [21] RP FUNCTION, AND INTERACTION WITH ITGB1 AND ITGB5. RX PubMed=22492727; DOI=10.1083/jcb.201111121; RA Steinberg F., Heesom K.J., Bass M.D., Cullen P.J.; RT "SNX17 protects integrins from degradation by sorting between lysosomal and RT recycling pathways."; RL J. Cell Biol. 197:219-230(2012). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-409; SER-415; RP SER-437 AND SER-440, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP FUNCTION, INTERACTION WITH CCDC22; CCDC93; VPS26C AND VPS35L, MUTAGENESIS RP OF LEU-432; SER-433; SER-440; GLY-464; 467-ASP--LEU-470; ASP-469 AND RP LEU-470, AND SUBCELLULAR LOCATION. RX PubMed=28892079; DOI=10.1038/ncb3610; RA McNally K.E., Faulkner R., Steinberg F., Gallon M., Ghai R., Pim D., RA Langton P., Pearson N., Danson C.M., Naegele H., Morris L.L., Singla A., RA Overlee B.L., Heesom K.J., Sessions R., Banks L., Collins B.M., Berger I., RA Billadeau D.D., Burstein E., Cullen P.J.; RT "Retriever is a multiprotein complex for retromer-independent endosomal RT cargo recycling."; RL Nat. Cell Biol. 19:1214-1225(2017). RN [25] RP DOMAIN. RX PubMed=33436498; DOI=10.1126/scisignal.abf1117; RA Kliche J., Kuss H., Ali M., Ivarsson Y.; RT "Cytoplasmic short linear motifs in ACE2 and integrin beta3 link SARS-CoV-2 RT host cell receptors to mediators of endocytosis and autophagy."; RL Sci. Signal. 14:0-0(2021). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-108. RG Structural genomics consortium (SGC); RT "Crystal structure of the PX domain of sorting nexin-17 (SNX17)."; RL Submitted (JAN-2009) to the PDB data bank. RN [27] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-112, FUNCTION, SUBCELLULAR RP LOCATION, DOMAIN FERM-LIKE REGION, SUBUNIT, AND INTERACTION WITH HRAS. RX PubMed=21512128; DOI=10.1073/pnas.1017110108; RA Ghai R., Mobli M., Norwood S.J., Bugarcic A., Teasdale R.D., King G.F., RA Collins B.M.; RT "Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as RT molecular scaffolds that interact with cargo receptors and Ras GTPases."; RL Proc. Natl. Acad. Sci. U.S.A. 108:7763-7768(2011). CC -!- FUNCTION: Critical regulator of endosomal recycling of numerous surface CC proteins, including integrins, signaling receptor and channels CC (PubMed:15121882, PubMed:15769472). Binds to NPxY sequences in the CC cytoplasmic tails of target cargos (PubMed:21512128). 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 (PubMed:28892079, CC PubMed:22492727). Also required for maintenance of normal cell surface CC levels of APP and LRP1 (PubMed:16712798, PubMed:19005208). Interacts CC with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) CC (PubMed:16712798). {ECO:0000269|PubMed:15121882, CC ECO:0000269|PubMed:15769472, ECO:0000269|PubMed:16712798, CC ECO:0000269|PubMed:19005208, ECO:0000269|PubMed:21512128, CC ECO:0000269|PubMed:22492727, ECO:0000269|PubMed:28892079}. CC -!- SUBUNIT: Monomer (PubMed:21512128). Interacts with APP (via cytoplasmic CC YXNPXY motif) (By similarity). Interacts with KIF1B (By similarity). CC Interacts with the C-termini of P-selectin, PTC, LDLR, VLDLR, LRP1 and CC LRP8 (PubMed:11237770, PubMed:14739284, PubMed:15769472, CC PubMed:19005208). Interacts with KRIT1 (via N-terminus) CC (PubMed:16712798). Interacts with HRAS (PubMed:21512128). Interacts CC with ITGB1 and ITGB5 (via NPxY motif) (PubMed:22492727). Interacts with CC CCDC22, CCDC93, VPS26C and VPS35L; the interaction with VPS26C is CC direct and associates SNX17 with the retriever and CCC complexes CC (PubMed:28892079). {ECO:0000250|UniProtKB:Q8BVL3, CC ECO:0000269|PubMed:11237770, ECO:0000269|PubMed:14739284, CC ECO:0000269|PubMed:15769472, ECO:0000269|PubMed:16712798, CC ECO:0000269|PubMed:19005208, ECO:0000269|PubMed:21512128, CC ECO:0000269|PubMed:22492727, ECO:0000269|PubMed:28892079}. CC -!- INTERACTION: CC Q15036; P05067: APP; NbExp=3; IntAct=EBI-1752620, EBI-77613; CC Q15036; P31273: HOXC8; NbExp=8; IntAct=EBI-1752620, EBI-1752118; CC Q15036; P16333: NCK1; NbExp=3; IntAct=EBI-1752620, EBI-389883; CC Q15036; P19174: PLCG1; NbExp=2; IntAct=EBI-1752620, EBI-79387; CC Q15036; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-1752620, EBI-712367; CC Q15036; Q13671: RIN1; NbExp=3; IntAct=EBI-1752620, EBI-366017; CC Q15036; Q8TEB7: RNF128; NbExp=3; IntAct=EBI-1752620, EBI-2341619; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11237770, CC ECO:0000269|PubMed:21512128}. Early endosome CC {ECO:0000269|PubMed:14739284, ECO:0000269|PubMed:15121882, CC ECO:0000269|PubMed:15769472, ECO:0000269|PubMed:21512128, CC ECO:0000269|PubMed:28892079}. Cytoplasmic vesicle membrane CC {ECO:0000269|PubMed:11237770, ECO:0000269|PubMed:16712798}; Peripheral CC membrane protein {ECO:0000269|PubMed:11237770}; Cytoplasmic side CC {ECO:0000269|PubMed:11237770}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q15036-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15036-2; Sequence=VSP_044935; CC -!- DOMAIN: The PX domain mediates specific binding to phosphatidylinositol CC 3-phosphate (PtdIns(P3)). Required for association with endosomes. CC {ECO:0000269|PubMed:21512128}. 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:0000269|PubMed:21512128, ECO:0000269|PubMed:33436498}. CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA06542.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; D31764; BAA06542.2; ALT_INIT; mRNA. DR EMBL; AJ404855; CAC12897.1; -; Genomic_DNA. DR EMBL; AJ404856; CAC12897.1; JOINED; Genomic_DNA. DR EMBL; BT007167; AAP35831.1; -; mRNA. DR EMBL; AK298869; BAG60989.1; -; mRNA. DR EMBL; CR457081; CAG33362.1; -; mRNA. DR EMBL; AK222543; BAD96263.1; -; mRNA. DR EMBL; AC074117; AAY14844.1; -; Genomic_DNA. DR EMBL; BC002524; AAH02524.1; -; mRNA. DR EMBL; BC002610; AAH02610.1; -; mRNA. DR EMBL; BC014620; AAH14620.1; -; mRNA. DR EMBL; BC050590; AAH50590.1; -; mRNA. DR CCDS; CCDS1750.1; -. [Q15036-1] DR CCDS; CCDS58704.1; -. [Q15036-2] DR RefSeq; NP_001253989.1; NM_001267060.1. [Q15036-2] DR RefSeq; NP_055563.1; NM_014748.3. [Q15036-1] DR PDB; 3FOG; X-ray; 2.80 A; A=1-108. DR PDB; 3LUI; X-ray; 1.80 A; A/B/C=1-112. DR PDB; 4GXB; X-ray; 1.80 A; A=111-388. DR PDB; 4TKN; X-ray; 3.00 A; A/B/C=108-391. DR PDB; 7RM8; NMR; -; A=457-470. DR PDBsum; 3FOG; -. DR PDBsum; 3LUI; -. DR PDBsum; 4GXB; -. DR PDBsum; 4TKN; -. DR PDBsum; 7RM8; -. DR AlphaFoldDB; Q15036; -. DR BMRB; Q15036; -. DR SMR; Q15036; -. DR BioGRID; 115128; 84. DR DIP; DIP-52265N; -. DR IntAct; Q15036; 42. DR MINT; Q15036; -. DR STRING; 9606.ENSP00000233575; -. DR TCDB; 3.A.34.1.1; the sorting nexins of the escrt complexes (sn-escrt). DR TCDB; 9.A.3.1.2; the sorting nexin27 (snx27)-retromer assembly apparatus (retromeraa) family. DR GlyGen; Q15036; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q15036; -. DR PhosphoSitePlus; Q15036; -. DR BioMuta; SNX17; -. DR DMDM; 3123050; -. DR EPD; Q15036; -. DR jPOST; Q15036; -. DR MassIVE; Q15036; -. DR MaxQB; Q15036; -. DR PaxDb; 9606-ENSP00000233575; -. DR PeptideAtlas; Q15036; -. DR ProteomicsDB; 4890; -. DR ProteomicsDB; 60385; -. [Q15036-1] DR Pumba; Q15036; -. DR Antibodypedia; 28444; 178 antibodies from 27 providers. DR DNASU; 9784; -. DR Ensembl; ENST00000233575.7; ENSP00000233575.2; ENSG00000115234.11. [Q15036-1] DR Ensembl; ENST00000537606.5; ENSP00000439208.1; ENSG00000115234.11. [Q15036-2] DR GeneID; 9784; -. DR KEGG; hsa:9784; -. DR MANE-Select; ENST00000233575.7; ENSP00000233575.2; NM_014748.4; NP_055563.1. DR UCSC; uc002rkg.3; human. [Q15036-1] DR AGR; HGNC:14979; -. DR CTD; 9784; -. DR DisGeNET; 9784; -. DR GeneCards; SNX17; -. DR HGNC; HGNC:14979; SNX17. DR HPA; ENSG00000115234; Low tissue specificity. DR MIM; 605963; gene. DR neXtProt; NX_Q15036; -. DR OpenTargets; ENSG00000115234; -. DR PharmGKB; PA37954; -. DR VEuPathDB; HostDB:ENSG00000115234; -. DR eggNOG; KOG3784; Eukaryota. DR GeneTree; ENSGT00950000183212; -. DR HOGENOM; CLU_041342_1_0_1; -. DR InParanoid; Q15036; -. DR OMA; RRHCVGV; -. DR OrthoDB; 5487301at2759; -. DR PhylomeDB; Q15036; -. DR TreeFam; TF318398; -. DR PathwayCommons; Q15036; -. DR SignaLink; Q15036; -. DR BioGRID-ORCS; 9784; 34 hits in 1152 CRISPR screens. DR ChiTaRS; SNX17; human. DR EvolutionaryTrace; Q15036; -. DR GeneWiki; SNX17; -. DR GenomeRNAi; 9784; -. DR Pharos; Q15036; Tbio. DR PRO; PR:Q15036; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q15036; Protein. DR Bgee; ENSG00000115234; Expressed in granulocyte and 200 other cell types or tissues. DR ExpressionAtlas; Q15036; baseline and differential. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0010008; C:endosome membrane; IDA:MGI. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:UniProtKB. DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; NAS:UniProtKB. DR GO; GO:0035904; P:aorta development; IEA:Ensembl. DR GO; GO:0003279; P:cardiac septum development; IEA:Ensembl. DR GO; GO:0006707; P:cholesterol catabolic process; IC:UniProtKB. DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl. DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB. DR GO; GO:0016197; P:endosomal transport; NAS: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; IEA:Ensembl. DR GO; GO:0030100; P:regulation of endocytosis; NAS:UniProtKB. 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; Q15036; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle; KW Direct protein sequencing; Endosome; Lipid-binding; Membrane; KW Phosphoprotein; Protein transport; Reference proteome; Transport. FT CHAIN 1..470 FT /note="Sorting nexin-17" FT /id="PRO_0000213865" 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 REGION 270..432 FT /note="PTB-like F3 module" 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:0007744|PubMed:23186163" FT MOD_RES 407 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 409 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 415 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 421 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 437 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 440 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VAR_SEQ 22..46 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044935" FT MUTAGEN 62 FT /note="K->A: No association with endosomes." FT /evidence="ECO:0000269|PubMed:14739284" FT MUTAGEN 432 FT /note="L->A: No effect on interaction with CCDC22, CCDC93, FT VPS26C and VPS35L." FT /evidence="ECO:0000269|PubMed:28892079" FT MUTAGEN 433 FT /note="S->D: No effect on interaction with CCDC22, CCDC93, FT VPS26C and VPS35L." FT /evidence="ECO:0000269|PubMed:28892079" FT MUTAGEN 440 FT /note="S->D: No effect on interaction with CCDC22, CCDC93, FT VPS26C and VPS35L." FT /evidence="ECO:0000269|PubMed:28892079" FT MUTAGEN 464 FT /note="G->V: Slightly decreases interaction with CCDC22, FT CCDC93, VPS26C and VPS35L." FT /evidence="ECO:0000269|PubMed:28892079" FT MUTAGEN 467..470 FT /note="Missing: Strongly decreases interaction with CCDC22, FT CCDC93, VPS26C and VPS35L. No effect on endosomal FT location." FT /evidence="ECO:0000269|PubMed:28892079" FT MUTAGEN 469 FT /note="D->K: Slightly decreases interaction with CCDC22, FT CCDC93, VPS26C and VPS35L." FT /evidence="ECO:0000269|PubMed:28892079" FT MUTAGEN 470 FT /note="L->G: Strongly decreases interaction with CCDC22, FT CCDC93, VPS26C and VPS35L. No effect on endosomal FT location." FT /evidence="ECO:0000269|PubMed:28892079" FT CONFLICT 429 FT /note="M -> V (in Ref. 6; BAD96263)" FT /evidence="ECO:0000305" FT STRAND 3..11 FT /evidence="ECO:0007829|PDB:3LUI" FT STRAND 20..27 FT /evidence="ECO:0007829|PDB:3LUI" FT STRAND 30..36 FT /evidence="ECO:0007829|PDB:3LUI" FT HELIX 37..51 FT /evidence="ECO:0007829|PDB:3LUI" FT TURN 53..55 FT /evidence="ECO:0007829|PDB:3FOG" FT HELIX 69..88 FT /evidence="ECO:0007829|PDB:3LUI" FT HELIX 90..94 FT /evidence="ECO:0007829|PDB:3LUI" FT HELIX 96..109 FT /evidence="ECO:0007829|PDB:3LUI" FT STRAND 116..123 FT /evidence="ECO:0007829|PDB:4GXB" FT STRAND 128..134 FT /evidence="ECO:0007829|PDB:4GXB" FT HELIX 139..150 FT /evidence="ECO:0007829|PDB:4GXB" FT HELIX 154..159 FT /evidence="ECO:0007829|PDB:4GXB" FT STRAND 160..167 FT /evidence="ECO:0007829|PDB:4GXB" FT STRAND 173..178 FT /evidence="ECO:0007829|PDB:4GXB" FT HELIX 185..190 FT /evidence="ECO:0007829|PDB:4GXB" FT TURN 191..193 FT /evidence="ECO:0007829|PDB:4TKN" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:4GXB" FT HELIX 208..210 FT /evidence="ECO:0007829|PDB:4GXB" FT HELIX 211..214 FT /evidence="ECO:0007829|PDB:4GXB" FT HELIX 218..233 FT /evidence="ECO:0007829|PDB:4GXB" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:4GXB" FT HELIX 241..253 FT /evidence="ECO:0007829|PDB:4GXB" FT HELIX 256..263 FT /evidence="ECO:0007829|PDB:4GXB" FT TURN 268..270 FT /evidence="ECO:0007829|PDB:4GXB" FT STRAND 277..283 FT /evidence="ECO:0007829|PDB:4GXB" FT STRAND 286..293 FT /evidence="ECO:0007829|PDB:4GXB" FT STRAND 296..300 FT /evidence="ECO:0007829|PDB:4GXB" FT STRAND 310..314 FT /evidence="ECO:0007829|PDB:4GXB" FT HELIX 315..317 FT /evidence="ECO:0007829|PDB:4GXB" FT STRAND 318..325 FT /evidence="ECO:0007829|PDB:4GXB" FT STRAND 346..355 FT /evidence="ECO:0007829|PDB:4GXB" FT STRAND 358..365 FT /evidence="ECO:0007829|PDB:4GXB" FT HELIX 369..387 FT /evidence="ECO:0007829|PDB:4GXB" SQ SEQUENCE 470 AA; 52901 MW; B1C8650CB8AFB5EE CRC64; MHFSIPETES RSGDSGGSAY VAYNIHVNGV LHCRVRYSQL LGLHEQLRKE YGANVLPAFP PKKLFSLTPA EVEQRREQLE KYMQAVRQDP LLGSSETFNS FLRRAQQETQ QVPTEEVSLE VLLSNGQKVL VNVLTSDQTE DVLEAVAAKL DLPDDLIGYF SLFLVREKED GAFSFVRKLQ EFELPYVSVT SLRSQEYKIV LRKSYWDSAY DDDVMENRVG LNLLYAQTVS DIERGWILVT KEQHRQLKSL QEKVSKKEFL RLAQTLRHYG YLRFDACVAD FPEKDCPVVV SAGNSELSLQ LRLPGQQLRE GSFRVTRMRC WRVTSSVPLP SGSTSSPGRG RGEVRLELAF EYLMSKDRLQ WVTITSPQAI MMSICLQSMV DELMVKKSGG SIRKMLRRRV GGTLRRSDSQ QAVKSPPLLE SPDATRESMV KLSSKLSAVS LRGIGSPSTD ASASDVHGNF AFEGIGDEDL //