SNX17_HUMAN
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 03-AUG-2022, entry version 204.
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};
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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 PDBsum; 3FOG; -.
DR PDBsum; 3LUI; -.
DR PDBsum; 4GXB; -.
DR PDBsum; 4TKN; -.
DR AlphaFoldDB; Q15036; -.
DR BMRB; Q15036; -.
DR SMR; Q15036; -.
DR BioGRID; 115128; 73.
DR DIP; DIP-52265N; -.
DR IntAct; Q15036; 42.
DR MINT; Q15036; -.
DR STRING; 9606.ENSP00000233575; -.
DR TCDB; 9.A.3.1.2; the sorting nexin27 (snx27)-retromer assembly apparatus (retromeraa) family.
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; Q15036; -.
DR PeptideAtlas; Q15036; -.
DR PRIDE; Q15036; -.
DR ProteomicsDB; 4890; -.
DR ProteomicsDB; 60385; -. [Q15036-1]
DR Antibodypedia; 28444; 166 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 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; 577861at2759; -.
DR PhylomeDB; Q15036; -.
DR TreeFam; TF318398; -.
DR PathwayCommons; Q15036; -.
DR SignaLink; Q15036; -.
DR BioGRID-ORCS; 9784; 23 hits in 1075 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 198 other tissues.
DR ExpressionAtlas; Q15036; baseline and differential.
DR Genevisible; Q15036; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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:0008022; F:protein C-terminus binding; IPI: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 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 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
