ID SNX1_HUMAN Reviewed; 522 AA.
AC Q13596; A6NM19; A8K6T7; H0Y2M5; O60750; O60751; Q6ZRJ8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 3.
DT 27-MAR-2024, entry version 210.
DE RecName: Full=Sorting nexin-1;
GN Name=SNX1;
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 [MRNA].
RX PubMed=8638121; DOI=10.1126/science.272.5264.1008;
RA Kurten R.C., Cadena D.L., Gill G.N.;
RT "Enhanced degradation of EGF receptors by a sorting nexin, SNX1.";
RL Science 272:1008-1010(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND INTERACTION WITH
RP VPS26A; VPS29; VPS35 AND SNX2.
RX PubMed=9819414; DOI=10.1128/mcb.18.12.7278;
RA Haft C.R., de la Luz Sierra M., Barr V.A., Haft D.H., Taylor S.I.;
RT "Identification of a family of sorting nexin molecules and characterization
RT of their association with receptors.";
RL Mol. Cell. Biol. 18:7278-7287(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta, and Testis;
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 GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [8]
RP INTERACTION WITH VPS26A, AND SUBUNIT.
RX PubMed=11102511; DOI=10.1091/mbc.11.12.4105;
RA Renfrew Haft C., de la Luz Sierra M., Bafford R., Lesniak M.A., Barr V.A.,
RA Taylor S.I.;
RT "Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and
RT 35: assembly into multimeric complexes.";
RL Mol. Biol. Cell 11:4105-4116(2000).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-214, AND INTERACTION
RP WITH PHOSPHATIDYLINOSITIDES.
RX PubMed=12198132; DOI=10.1074/jbc.m206986200;
RA Cozier G.E., Carlton J., McGregor A.H., Gleeson P.A., Teasdale R.D.,
RA Mellor H., Cullen P.J.;
RT "The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated
RT association of sorting nexin-1 with an early sorting endosomal compartment
RT is required for its ability to regulate epidermal growth factor receptor
RT degradation.";
RL J. Biol. Chem. 277:48730-48736(2002).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SNX2.
RX PubMed=11997453; DOI=10.1073/pnas.092142699;
RA Zhong Q., Lazar C.S., Tronchere H., Sato T., Meerloo T., Yeo M.,
RA Songyang Z., Emr S.D., Gill G.N.;
RT "Endosomal localization and function of sorting nexin 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6767-6772(2002).
RN [11]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-214 AND
RP 429-LYS--ARG-431.
RX PubMed=15498486; DOI=10.1016/j.cub.2004.09.077;
RA Carlton J., Bujny M., Peter B.J., Oorschot V.M., Rutherford A., Mellor H.,
RA Klumperman J., McMahon H.T., Cullen P.J.;
RT "Sorting nexin-1 mediates tubular endosome-to-TGN transport through
RT coincidence sensing of high- curvature membranes and 3-phosphoinositides.";
RL Curr. Biol. 14:1791-1800(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP FUNCTION.
RX PubMed=16407403; DOI=10.1091/mbc.e05-09-0899;
RA Gullapalli A., Wolfe B.L., Griffin C.T., Magnuson T., Trejo J.;
RT "An essential role for SNX1 in lysosomal sorting of protease-activated
RT receptor-1: evidence for retromer-, Hrs-, and Tsg101-independent functions
RT of sorting nexins.";
RL Mol. Biol. Cell 17:1228-1238(2006).
RN [14]
RP FUNCTION.
RX PubMed=17550970; DOI=10.1242/jcs.003111;
RA Bujny M.V., Popoff V., Johannes L., Cullen P.J.;
RT "The retromer component sorting nexin-1 is required for efficient
RT retrograde transport of Shiga toxin from early endosome to the trans Golgi
RT network.";
RL J. Cell Sci. 120:2010-2021(2007).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17101778; DOI=10.1128/mcb.00156-06;
RA Rojas R., Kametaka S., Haft C.R., Bonifacino J.S.;
RT "Interchangeable but essential functions of SNX1 and SNX2 in the
RT association of retromer with endosomes and the trafficking of mannose 6-
RT phosphate receptors.";
RL Mol. Cell. Biol. 27:1112-1124(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-39 AND SER-188, AND
RP 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 [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18088323; DOI=10.1111/j.1600-0854.2007.00686.x;
RA Mari M., Bujny M.V., Zeuschner D., Geerts W.J., Griffith J., Petersen C.M.,
RA Cullen P.J., Klumperman J., Geuze H.J.;
RT "SNX1 defines an early endosomal recycling exit for sortilin and mannose 6-
RT phosphate receptors.";
RL Traffic 9:380-393(2008).
RN [18]
RP INTERACTION WITH SNX6.
RX PubMed=19935774; DOI=10.1038/cr.2009.130;
RA Hong Z., Yang Y., Zhang C., Niu Y., Li K., Zhao X., Liu J.J.;
RT "The retromer component SNX6 interacts with dynactin p150(Glued) and
RT mediates endosome-to-TGN transport.";
RL Cell Res. 19:1334-1349(2009).
RN [19]
RP SUBUNIT, AND INTERACTION WITH SNX5; SNX6; VPS26A; VPS29; VPS35 AND DENND5A.
RX PubMed=19619496; DOI=10.1016/j.devcel.2009.04.016;
RA Wassmer T., Attar N., Harterink M., van Weering J.R., Traer C.J.,
RA Oakley J., Goud B., Stephens D.J., Verkade P., Korswagen H.C., Cullen P.J.;
RT "The retromer coat complex coordinates endosomal sorting and dynein-
RT mediated transport, with carrier recognition by the trans-Golgi network.";
RL Dev. Cell 17:110-122(2009).
RN [20]
RP FUNCTION, AND DOMAIN.
RX PubMed=19816406; DOI=10.1038/emboj.2009.261;
RA Bhatia V.K., Madsen K.L., Bolinger P.Y., Kunding A., Hedegaard P.,
RA Gether U., Stamou D.;
RT "Amphipathic motifs in BAR domains are essential for membrane curvature
RT sensing.";
RL EMBO J. 28:3303-3314(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP 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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-237, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [23]
RP INTERACTION WITH DNAJC13, AND SUBCELLULAR LOCATION.
RX PubMed=19874558; DOI=10.1111/j.1600-0854.2009.00993.x;
RA Popoff V., Mardones G.A., Bai S.K., Chambon V., Tenza D., Burgos P.V.,
RA Shi A., Benaroch P., Urbe S., Lamaze C., Grant B.D., Raposo G.,
RA Johannes L.;
RT "Analysis of articulation between clathrin and retromer in retrograde
RT sorting on early endosomes.";
RL Traffic 10:1868-1880(2009).
RN [24]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21040701; DOI=10.1016/j.bbrc.2010.10.121;
RA Kim E., Lee Y., Lee H.J., Kim J.S., Song B.S., Huh J.W., Lee S.R.,
RA Kim S.U., Kim S.H., Hong Y., Shim I., Chang K.T.;
RT "Implication of mouse Vps26b-Vps29-Vps35 retromer complex in sortilin
RT trafficking.";
RL Biochem. Biophys. Res. Commun. 403:167-171(2010).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP 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 [26]
RP FUNCTION, INTERACTION WITH KALRN AND RHOG, AND SUBCELLULAR LOCATION.
RX PubMed=20604901; DOI=10.1111/j.1600-0854.2010.01100.x;
RA Prosser D.C., Tran D., Schooley A., Wendland B., Ngsee J.K.;
RT "A novel, retromer-independent role for sorting nexins 1 and 2 in RhoG-
RT dependent membrane remodeling.";
RL Traffic 11:1347-1362(2010).
RN [27]
RP FUNCTION.
RX PubMed=20070609; DOI=10.1111/j.1600-0854.2010.01035.x;
RA Nisar S., Kelly E., Cullen P.J., Mundell S.J.;
RT "Regulation of P2Y1 receptor traffic by sorting Nexin 1 is retromer
RT independent.";
RL Traffic 11:508-519(2010).
RN [28]
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 [29]
RP SUBCELLULAR LOCATION.
RX PubMed=22431521; DOI=10.1128/mcb.06726-11;
RA Mamo A., Jules F., Dumaresq-Doiron K., Costantino S., Lefrancois S.;
RT "The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal
RT sorting.";
RL Mol. Cell. Biol. 32:1855-1866(2012).
RN [30]
RP FUNCTION, AND INTERACTION WITH DRD5.
RX PubMed=23152498; DOI=10.1074/jbc.m112.428458;
RA Villar V.A., Jones J.E., Armando I., Asico L.D., Escano C.S. Jr., Lee H.,
RA Wang X., Yang Y., Pascua-Crusan A.M., Palmes-Saloma C.P., Felder R.A.,
RA Jose P.A.;
RT "Sorting nexin 1 loss results in D5 dopamine receptor dysfunction in human
RT renal proximal tubule cells and hypertension in mice.";
RL J. Biol. Chem. 288:152-163(2013).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-188 AND SER-280, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-39; THR-48; SER-188
RP AND SER-280, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [33]
RP STRUCTURE BY NMR OF 142-269, AND SUBCELLULAR LOCATION.
RX PubMed=15673616; DOI=10.1091/mbc.e04-06-0504;
RA Zhong Q., Watson M.J., Lazar C.S., Hounslow A.M., Waltho J.P., Gill G.N.;
RT "Determinants of the endosomal localization of sorting nexin 1.";
RL Mol. Biol. Cell 16:2049-2057(2005).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 301-522, FUNCTION, INTERACTION
RP WITH SNX5; SNX6 AND SNX32, SELF-ASSOCIATION, SUBUNIT, DOMAIN, AND
RP MUTAGENESIS OF 287-MET-PHE-288; LYS-442 AND LYS-445.
RX PubMed=23085988; DOI=10.1038/emboj.2012.283;
RA van Weering J.R., Sessions R.B., Traer C.J., Kloer D.P., Bhatia V.K.,
RA Stamou D., Carlsson S.R., Hurley J.H., Cullen P.J.;
RT "Molecular basis for SNX-BAR-mediated assembly of distinct endosomal
RT sorting tubules.";
RL EMBO J. 31:4466-4480(2012).
CC -!- FUNCTION: Involved in several stages of intracellular trafficking.
CC Interacts with membranes containing phosphatidylinositol 3-phosphate
CC (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2)
CC (PubMed:12198132). Acts in part as component of the retromer membrane-
CC deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde
CC transport of cargo proteins from endosomes to the trans-Golgi network
CC (TGN) and is involved in endosome-to-plasma membrane transport for
CC cargo protein recycling. The SNX-BAR subcomplex functions to deform the
CC donor membrane into a tubular profile called endosome-to-TGN transport
CC carrier (ETC) (Probable). Can sense membrane curvature and has in vitro
CC vesicle-to-membrane remodeling activity (PubMed:19816406,
CC PubMed:23085988). Involved in retrograde endosome-to-TGN transport of
CC lysosomal enzyme receptors (IGF2R, M6PR and SORT1) and Shiginella
CC dysenteria toxin stxB. Plays a role in targeting ligand-activated EGFR
CC to the lysosomes for degradation after endocytosis from the cell
CC surface and release from the Golgi (PubMed:12198132, PubMed:15498486,
CC PubMed:17550970, PubMed:17101778, PubMed:18088323, PubMed:21040701).
CC Involvement in retromer-independent endocytic trafficking of P2RY1 and
CC lysosomal degradation of protease-activated receptor-1/F2R
CC (PubMed:16407403, PubMed:20070609). Promotes KALRN- and RHOG-dependent
CC but retromer-independent membrane remodeling such as lamellipodium
CC formation; the function is dependent on GEF activity of KALRN
CC (PubMed:20604901). Required for endocytosis of DRD5 upon agonist
CC stimulation but not for basal receptor trafficking (PubMed:23152498).
CC {ECO:0000269|PubMed:12198132, ECO:0000269|PubMed:15498486,
CC ECO:0000269|PubMed:16407403, ECO:0000269|PubMed:17101778,
CC ECO:0000269|PubMed:17550970, ECO:0000269|PubMed:18088323,
CC ECO:0000269|PubMed:19816406, ECO:0000269|PubMed:20070609,
CC ECO:0000269|PubMed:20604901, ECO:0000269|PubMed:21040701,
CC ECO:0000269|PubMed:23085988, ECO:0000269|PubMed:23152498,
CC ECO:0000303|PubMed:15498486}.
CC -!- SUBUNIT: Predominantly forms heterodimers with BAR domain-containing
CC sorting nexins SNX5, SNX6 and SNX32; can self-associate to form
CC homodimers (PubMed:23085988). The heterodimers are proposed to self-
CC assemble into helical arrays on the membrane to stabilize and expand
CC local membrane curvature underlying endosomal tubule formation. Thought
CC to be a component of the originally described retromer complex (also
CC called SNX-BAR retromer) which is a pentamer containing the
CC heterotrimeric retromer cargo-selective complex (CSC), also described
CC as vacuolar protein sorting subcomplex (VPS) and a heterodimeric
CC membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or
CC SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR
CC subcomplexes associate with low affinity (Probable). Interacts with
CC SNX5, SNX6, SNX32, VPS26A, VPS29, VPS35, DRD5, DENND5A, KALRN, RHOG
CC (GDP-bound form) (PubMed:9819414, PubMed:11102511, PubMed:19619496,
CC PubMed:19935774, PubMed:19619496, PubMed:20604901, PubMed:23085988,
CC PubMed:23152498). The interaction with SNX2 is reported controversially
CC (PubMed:9819414, PubMed:11997453, PubMed:19619496, PubMed:23085988).
CC Interacts with DNAJC13; prevented by presence of HGS (PubMed:19874558).
CC Interacts with HGS (By similarity). {ECO:0000250|UniProtKB:Q99N27,
CC ECO:0000250|UniProtKB:Q9WV80, ECO:0000269|PubMed:11102511,
CC ECO:0000269|PubMed:11997453, ECO:0000269|PubMed:12198132,
CC ECO:0000269|PubMed:15498486, ECO:0000269|PubMed:17101778,
CC ECO:0000269|PubMed:19619496, ECO:0000269|PubMed:19874558,
CC ECO:0000269|PubMed:19935774, ECO:0000269|PubMed:20604901,
CC ECO:0000269|PubMed:23085988, ECO:0000269|PubMed:23152498,
CC ECO:0000269|PubMed:9819414, ECO:0000303|PubMed:19619496,
CC ECO:0000303|PubMed:23085988}.
CC -!- INTERACTION:
CC Q13596; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-2822329, EBI-741181;
CC Q13596; Q15041: ARL6IP1; NbExp=4; IntAct=EBI-2822329, EBI-714543;
CC Q13596; Q5T9G4-2: ARMC12; NbExp=3; IntAct=EBI-2822329, EBI-36513937;
CC Q13596; P07510-2: CHRNG; NbExp=3; IntAct=EBI-2822329, EBI-11979451;
CC Q13596; Q8IZR5-2: CMTM4; NbExp=3; IntAct=EBI-2822329, EBI-17278014;
CC Q13596; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-2822329, EBI-2548702;
CC Q13596; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-2822329, EBI-11522780;
CC Q13596; Q9NZJ6: COQ3; NbExp=3; IntAct=EBI-2822329, EBI-10897372;
CC Q13596; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-2822329, EBI-14240149;
CC Q13596; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-2822329, EBI-3918971;
CC Q13596; Q8IVP5: FUNDC1; NbExp=3; IntAct=EBI-2822329, EBI-3059266;
CC Q13596; P53701: HCCS; NbExp=3; IntAct=EBI-2822329, EBI-10763431;
CC Q13596; Q9H400: LIME1; NbExp=3; IntAct=EBI-2822329, EBI-2830566;
CC Q13596; O95563: MPC2; NbExp=3; IntAct=EBI-2822329, EBI-719403;
CC Q13596; O60664: PLIN3; NbExp=4; IntAct=EBI-2822329, EBI-725795;
CC Q13596; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-2822329, EBI-712367;
CC Q13596; Q00765: REEP5; NbExp=3; IntAct=EBI-2822329, EBI-1549827;
CC Q13596; Q96HR9: REEP6; NbExp=4; IntAct=EBI-2822329, EBI-750345;
CC Q13596; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-2822329, EBI-14065960;
CC Q13596; Q6ZWK4: RHEX; NbExp=3; IntAct=EBI-2822329, EBI-18304046;
CC Q13596; O95197: RTN3; NbExp=3; IntAct=EBI-2822329, EBI-740467;
CC Q13596; Q9NQC3: RTN4; NbExp=3; IntAct=EBI-2822329, EBI-715945;
CC Q13596; O00560: SDCBP; NbExp=3; IntAct=EBI-2822329, EBI-727004;
CC Q13596; Q8N3Y7: SDR16C5; NbExp=3; IntAct=EBI-2822329, EBI-3923480;
CC Q13596; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-2822329, EBI-2854842;
CC Q13596; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-2822329, EBI-2623095;
CC Q13596; Q13596: SNX1; NbExp=2; IntAct=EBI-2822329, EBI-2822329;
CC Q13596; O60749: SNX2; NbExp=3; IntAct=EBI-2822329, EBI-1046690;
CC Q13596; Q86XE0: SNX32; NbExp=11; IntAct=EBI-2822329, EBI-8099743;
CC Q13596; Q9Y5X3: SNX5; NbExp=2; IntAct=EBI-2822329, EBI-715760;
CC Q13596; Q9UNH7: SNX6; NbExp=6; IntAct=EBI-2822329, EBI-949294;
CC Q13596; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-2822329, EBI-12187159;
CC Q13596; P08247: SYP; NbExp=3; IntAct=EBI-2822329, EBI-9071725;
CC Q13596; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-2822329, EBI-11528917;
CC Q13596; Q96QK1: VPS35; NbExp=2; IntAct=EBI-2822329, EBI-1054634;
CC Q13596; Q12768: WASHC5; NbExp=2; IntAct=EBI-2822329, EBI-2563794;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:15498486,
CC ECO:0000269|PubMed:18088323, ECO:0000269|PubMed:22431521}; Peripheral
CC membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane;
CC Peripheral membrane protein; Cytoplasmic side. Cell projection,
CC lamellipodium {ECO:0000269|PubMed:20604901}. Note=Enriched on tubular
CC elements of the early endosome membrane. Binds preferentially to highly
CC curved membranes enriched in phosphatidylinositol 3-phosphate
CC (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2)
CC (PubMed:15498486). Colocalized with SORT1 to tubular endosomal membrane
CC structures called endosome-to-TGN transport carriers (ETCs) which are
CC budding from early endosome vacuoles just before maturing into late
CC endosome vacuoles (PubMed:18088323). Colocalizes with DNAJC13 and
CC Shiginella dysenteria toxin stxB on early endosomes (PubMed:19874558).
CC Colocalized with F-actin at the leading edge of lamellipodia in a
CC KALRN-dependent manner (PubMed:20604901). {ECO:0000269|PubMed:15498486,
CC ECO:0000269|PubMed:18088323, ECO:0000269|PubMed:20604901}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13596-1; Sequence=Displayed;
CC Name=1A;
CC IsoId=Q13596-2; Sequence=VSP_006189;
CC Name=3;
CC IsoId=Q13596-3; Sequence=VSP_044823;
CC -!- DOMAIN: The BAR domain is able to sense membrane curvature upon
CC dimerization (PubMed:19816406). Membrane remodeling seems to implicate
CC insertion of a N-terminal amphipathic helix (AH) in the membrane
CC (Probable). {ECO:0000269|PubMed:19816406, ECO:0000303|PubMed:23085988}.
CC -!- MISCELLANEOUS: Binds phosphatidylinositol 3-phosphate (PtdIns-(3)P) and
CC phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2) in liposome-
CC based assays. Can bind PtdIns(3,4,5)P3 in protein:lipid overlay assays,
CC but not in liposome-based assays.
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; U53225; AAA98672.1; -; mRNA.
DR EMBL; AF065483; AAC17182.1; -; mRNA.
DR EMBL; AF065484; AAC17183.1; -; mRNA.
DR EMBL; BT006983; AAP35629.1; -; mRNA.
DR EMBL; AK128179; BAC87312.1; -; mRNA.
DR EMBL; AK291752; BAF84441.1; -; mRNA.
DR EMBL; AC021541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77663.1; -; Genomic_DNA.
DR EMBL; CH471082; EAW77665.1; -; Genomic_DNA.
DR EMBL; BC000357; AAH00357.1; -; mRNA.
DR CCDS; CCDS32266.1; -. [Q13596-1]
DR CCDS; CCDS32268.1; -. [Q13596-2]
DR CCDS; CCDS58371.1; -. [Q13596-3]
DR PIR; G02522; G02522.
DR RefSeq; NP_001229862.1; NM_001242933.1. [Q13596-3]
DR RefSeq; NP_003090.2; NM_003099.4. [Q13596-1]
DR RefSeq; NP_683758.1; NM_148955.3. [Q13596-2]
DR PDB; 2I4K; NMR; -; A=142-269.
DR PDB; 4FZS; X-ray; 2.80 A; A/B=301-522.
DR PDB; 8A1G; X-ray; 2.50 A; A/B=301-522.
DR PDB; 8ABQ; X-ray; 2.81 A; A/B=301-522.
DR PDB; 8AFZ; EM; 10.00 A; A=1-522.
DR PDBsum; 2I4K; -.
DR PDBsum; 4FZS; -.
DR PDBsum; 8A1G; -.
DR PDBsum; 8ABQ; -.
DR PDBsum; 8AFZ; -.
DR AlphaFoldDB; Q13596; -.
DR BMRB; Q13596; -.
DR EMDB; EMD-15413; -.
DR SMR; Q13596; -.
DR BioGRID; 112525; 223.
DR CORUM; Q13596; -.
DR DIP; DIP-398N; -.
DR IntAct; Q13596; 78.
DR MINT; Q13596; -.
DR STRING; 9606.ENSP00000261889; -.
DR MoonDB; Q13596; Predicted.
DR TCDB; 3.A.34.1.1; the sorting nexins of the escrt complexes (sn-escrt).
DR TCDB; 8.A.194.1.1; the sorting nexin (snx) family.
DR GlyGen; Q13596; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13596; -.
DR MetOSite; Q13596; -.
DR PhosphoSitePlus; Q13596; -.
DR BioMuta; SNX1; -.
DR DMDM; 17380569; -.
DR EPD; Q13596; -.
DR jPOST; Q13596; -.
DR MassIVE; Q13596; -.
DR MaxQB; Q13596; -.
DR PaxDb; 9606-ENSP00000261889; -.
DR PeptideAtlas; Q13596; -.
DR ProteomicsDB; 34313; -.
DR ProteomicsDB; 59589; -. [Q13596-1]
DR ProteomicsDB; 59590; -. [Q13596-2]
DR Pumba; Q13596; -.
DR Antibodypedia; 13352; 411 antibodies from 39 providers.
DR DNASU; 6642; -.
DR Ensembl; ENST00000261889.9; ENSP00000261889.5; ENSG00000028528.15. [Q13596-3]
DR Ensembl; ENST00000559844.6; ENSP00000453785.1; ENSG00000028528.15. [Q13596-1]
DR Ensembl; ENST00000561026.5; ENSP00000453567.1; ENSG00000028528.15. [Q13596-2]
DR GeneID; 6642; -.
DR KEGG; hsa:6642; -.
DR MANE-Select; ENST00000559844.6; ENSP00000453785.1; NM_003099.5; NP_003090.2.
DR UCSC; uc002amv.4; human. [Q13596-1]
DR AGR; HGNC:11172; -.
DR CTD; 6642; -.
DR DisGeNET; 6642; -.
DR GeneCards; SNX1; -.
DR HGNC; HGNC:11172; SNX1.
DR HPA; ENSG00000028528; Low tissue specificity.
DR MIM; 601272; gene.
DR neXtProt; NX_Q13596; -.
DR OpenTargets; ENSG00000028528; -.
DR PharmGKB; PA36011; -.
DR VEuPathDB; HostDB:ENSG00000028528; -.
DR eggNOG; KOG2273; Eukaryota.
DR GeneTree; ENSGT00940000155889; -.
DR HOGENOM; CLU_022783_2_0_1; -.
DR InParanoid; Q13596; -.
DR OMA; EKMAAVW; -.
DR OrthoDB; 1891044at2759; -.
DR PhylomeDB; Q13596; -.
DR TreeFam; TF313698; -.
DR PathwayCommons; Q13596; -.
DR SignaLink; Q13596; -.
DR BioGRID-ORCS; 6642; 18 hits in 1158 CRISPR screens.
DR ChiTaRS; SNX1; human.
DR EvolutionaryTrace; Q13596; -.
DR GeneWiki; SNX1; -.
DR GenomeRNAi; 6642; -.
DR Pharos; Q13596; Tbio.
DR PRO; PR:Q13596; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q13596; Protein.
DR Bgee; ENSG00000028528; Expressed in right lobe of thyroid gland and 209 other cell types or tissues.
DR ExpressionAtlas; Q13596; baseline and differential.
DR Genevisible; Q13596; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:HPA.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:HPA.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0030904; C:retromer complex; IDA:UniProtKB.
DR GO; GO:0030905; C:retromer, tubulation complex; IPI:ParkinsonsUK-UCL.
DR GO; GO:0031982; C:vesicle; IDA:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005158; F:insulin receptor binding; IDA:UniProtKB.
DR GO; GO:1990460; F:leptin receptor binding; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:ParkinsonsUK-UCL.
DR GO; GO:1990459; F:transferrin receptor binding; IDA:UniProtKB.
DR GO; GO:0034498; P:early endosome to Golgi transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0072673; P:lamellipodium morphogenesis; IDA:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR CDD; cd07665; BAR_SNX1; 1.
DR CDD; cd07281; PX_SNX1; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR034901; PX_SNX1.
DR InterPro; IPR028660; SNX1_BAR.
DR InterPro; IPR005329; Sorting_nexin_N.
DR InterPro; IPR015404; Vps5_C.
DR PANTHER; PTHR10555; SORTING NEXIN; 1.
DR PANTHER; PTHR10555:SF129; SORTING NEXIN-1; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF03700; Sorting_nexin; 1.
DR Pfam; PF09325; Vps5; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection; Endosome;
KW Golgi apparatus; Lipid-binding; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..522
FT /note="Sorting nexin-1"
FT /id="PRO_0000213835"
FT DOMAIN 143..272
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 302..522
FT /note="BAR"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..298
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000303|PubMed:19816406"
FT COMPBIAS 55..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186
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|UniProtKB:Q96L94"
FT BINDING 188
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|UniProtKB:Q96L94"
FT BINDING 214
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|UniProtKB:Q96L94"
FT BINDING 238
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|UniProtKB:Q96L94"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV80"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV80"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 237
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 91..155
FT /note="Missing (in isoform 1A)"
FT /evidence="ECO:0000305"
FT /id="VSP_006189"
FT VAR_SEQ 507..522
FT /note="LAKYWEAFLPEAKAIS -> AGEQLGIRSGILLTKKLPRYSKFFSTVHKFCA
FT AASLWKWGFFLSAYLSYLF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044823"
FT VARIANT 115
FT /note="S -> Y (in dbSNP:rs1049501)"
FT /id="VAR_052477"
FT VARIANT 466
FT /note="D -> N (in dbSNP:rs1802376)"
FT /id="VAR_034507"
FT MUTAGEN 214
FT /note="K->A: Abolishes phosphatidylinositol phosphate
FT binding. Abolishes endosomal location."
FT /evidence="ECO:0000269|PubMed:12198132,
FT ECO:0000269|PubMed:15498486"
FT MUTAGEN 287..288
FT /note="MF->EE: Abolishes membrane remodeling capacity; no
FT effect on dimerization."
FT /evidence="ECO:0000269|PubMed:23085988"
FT MUTAGEN 429..431
FT /note="KKR->EEE: Loss of endosomal location."
FT /evidence="ECO:0000269|PubMed:15498486"
FT MUTAGEN 442
FT /note="K->A: No effect on membrane remodeling and membrane
FT binding; when associated with A-445."
FT /evidence="ECO:0000269|PubMed:23085988"
FT MUTAGEN 445
FT /note="K->A: No effect on membrane remodeling and membrane
FT binding; when associated with A-442."
FT /evidence="ECO:0000269|PubMed:23085988"
FT CONFLICT 117
FT /note="P -> S (in Ref. 2; AAC17182)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="P -> S (in Ref. 2; AAC17182/AAC17183)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="Y -> C (in Ref. 4; BAC87312)"
FT /evidence="ECO:0000305"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:2I4K"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:2I4K"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:2I4K"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:2I4K"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:2I4K"
FT HELIX 234..251
FT /evidence="ECO:0007829|PDB:2I4K"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:2I4K"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:2I4K"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:2I4K"
FT HELIX 307..357
FT /evidence="ECO:0007829|PDB:8A1G"
FT HELIX 361..438
FT /evidence="ECO:0007829|PDB:8A1G"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:8A1G"
FT HELIX 443..519
FT /evidence="ECO:0007829|PDB:8A1G"
SQ SEQUENCE 522 AA; 59070 MW; 6AC8AA0A589513E3 CRC64;
MASGGGGCSA SERLPPPFPG LEPESEGAAG GSEPEAGDSD TEGEDIFTGA AVVSKHQSPK
ITTSLLPINN GSKENGIHEE QDQEPQDLFA DATVELSLDS TQNNQKKVLA KTLISLPPQE
ATNSSKPQPT YEELEEEEQE DQFDLTVGIT DPEKIGDGMN AYVAYKVTTQ TSLPLFRSKQ
FAVKRRFSDF LGLYEKLSEK HSQNGFIVPP PPEKSLIGMT KVKVGKEDSS SAEFLEKRRA
ALERYLQRIV NHPTMLQDPD VREFLEKEEL PRAVGTQTLS GAGLLKMFNK ATDAVSKMTI
KMNESDIWFE EKLQEVECEE QRLRKLHAVV ETLVNHRKEL ALNTAQFAKS LAMLGSSEDN
TALSRALSQL AEVEEKIEQL HQEQANNDFF LLAELLSDYI RLLAIVRAAF DQRMKTWQRW
QDAQATLQKK REAEARLLWA NKPDKLQQAK DEILEWESRV TQYERDFERI STVVRKEVIR
FEKEKSKDFK NHVIKYLETL LYSQQQLAKY WEAFLPEAKA IS
//
