STIM1_HUMAN
ID STIM1_HUMAN Reviewed; 685 AA.
AC Q13586; E9PQJ4; Q8N382;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Stromal interaction molecule 1;
DE Flags: Precursor;
GN Name=STIM1; Synonyms=GOK {ECO:0000303|PubMed:9377559};
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] (ISOFORM 1).
RC TISSUE=Fetal liver, and Placenta;
RX PubMed=8921403; DOI=10.1006/geno.1996.0553;
RA Parker N.J., Begley C.G., Smith P.J., Fox R.M.;
RT "Molecular cloning of a novel human gene (D11S4896E) at chromosomal region
RT 11p15.5.";
RL Genomics 37:253-256(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [6]
RP POSSIBLE ROLE IN CANCER DEVELOPMENT.
RX PubMed=9377559;
RA Sabbioni S., Barbanti-Brodano G., Croce C.M., Negrini M.;
RT "GOK: a gene at 11p15 involved in rhabdomyosarcoma and rhabdoid tumor
RT development.";
RL Cancer Res. 57:4493-4497(1997).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND
RP PHOSPHORYLATION.
RX PubMed=11004585; DOI=10.1016/s0167-4838(00)00105-9;
RA Manji S.S., Parker N.J., Williams R.T., van Stekelenburg L., Pearson R.B.,
RA Dziadek M., Smith P.J.;
RT "STIM1: a novel phosphoprotein located at the cell surface.";
RL Biochim. Biophys. Acta 1481:147-155(2000).
RN [8]
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=11463338; DOI=10.1042/0264-6021:3570673;
RA Williams R.T., Manji S.S.M., Parker N.J., Hancock M.S.,
RA van Stekelenburg L., Eid J.-P., Senior P.V., Kazenwadel J.S., Shandala T.,
RA Saint R., Smith P.J., Dziadek M.A.;
RT "Identification and characterization of the STIM (stromal interaction
RT molecule) gene family: coding for a novel class of transmembrane
RT proteins.";
RL Biochem. J. 357:673-685(2001).
RN [9]
RP SUBUNIT, AND GLYCOSYLATION AT ASN-131 AND ASN-171.
RX PubMed=11983428; DOI=10.1016/s0167-4838(02)00211-x;
RA Williams R.T., Senior P.V., van Stekelenburg L., Layton J.E., Smith P.J.,
RA Dziadek M.A.;
RT "Stromal interaction molecule 1 (STIM1), a transmembrane protein with
RT growth suppressor activity, contains an extracellular SAM domain modified
RT by N-linked glycosylation.";
RL Biochim. Biophys. Acta 1596:131-137(2002).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-660 AND SER-668, 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 [14]
RP FUNCTION, INTERACTION WITH ORAI1, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=19249086; DOI=10.1016/j.cell.2009.02.014;
RA Park C.Y., Hoover P.J., Mullins F.M., Bachhawat P., Covington E.D.,
RA Raunser S., Walz T., Garcia K.C., Dolmetsch R.E., Lewis R.S.;
RT "STIM1 clusters and activates CRAC channels via direct binding of a
RT cytosolic domain to Orai1.";
RL Cell 136:876-890(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575; SER-660; THR-665 AND
RP SER-668, AND 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, 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 [17]
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 [18]
RP INTERACTION WITH ASPH.
RX PubMed=22586105; DOI=10.1073/pnas.1200667109;
RA Srikanth S., Jew M., Kim K.D., Yee M.K., Abramson J., Gwack Y.;
RT "Junctate is a Ca2+-sensing structural component of Orai1 and stromal
RT interaction molecule 1 (STIM1).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:8682-8687(2012).
RN [19]
RP INTERACTION WITH ADCY8.
RX PubMed=22494970; DOI=10.1126/scisignal.2002299;
RA Willoughby D., Everett K.L., Halls M.L., Pacheco J., Skroblin P., Vaca L.,
RA Klussmann E., Cooper D.M.;
RT "Direct binding between Orai1 and AC8 mediates dynamic interplay between
RT Ca2+ and cAMP signaling.";
RL Sci. Signal. 5:RA29-RA29(2012).
RN [20]
RP GLYCOSYLATION AT ASN-171.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-76.
RX PubMed=16005298; DOI=10.1016/j.cub.2005.05.055;
RA Liou J., Kim M.L., Heo W.D., Jones J.T., Myers J.W., Ferrell J.E. Jr.,
RA Meyer T.;
RT "STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+
RT influx.";
RL Curr. Biol. 15:1235-1241(2005).
RN [22]
RP FUNCTION.
RX PubMed=15866891; DOI=10.1083/jcb.200502019;
RA Roos J., DiGregorio P.J., Yeromin A.V., Ohlsen K., Lioudyno M., Zhang S.,
RA Safrina O., Kozak J.A., Wagner S.L., Cahalan M.D., Velicelebi G.,
RA Stauderman K.A.;
RT "STIM1, an essential and conserved component of store-operated Ca2+ channel
RT function.";
RL J. Cell Biol. 169:435-445(2005).
RN [23]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16208375; DOI=10.1038/nature04147;
RA Zhang S.L., Yu Y., Roos J., Kozak J.A., Deerinck T.J., Ellisman M.H.,
RA Stauderman K.A., Cahalan M.D.;
RT "STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the
RT Ca2+ store to the plasma membrane.";
RL Nature 437:902-905(2005).
RN [24]
RP FUNCTION, AND MUTAGENESIS OF ASP-76; ASP-78 AND GLU-87.
RX PubMed=16807233; DOI=10.1074/jbc.m604589200;
RA Mercer J.C., Dehaven W.I., Smyth J.T., Wedel B., Boyles R.R., Bird G.S.,
RA Putney J.W. Jr.;
RT "Large store-operated calcium selective currents due to co-expression of
RT Orai1 or Orai2 with the intracellular calcium sensor, Stim1.";
RL J. Biol. Chem. 281:24979-24990(2006).
RN [25]
RP FUNCTION.
RX PubMed=16766533; DOI=10.1074/jbc.c600126200;
RA Soboloff J., Spassova M.A., Tang X.D., Hewavitharana T., Xu W., Gill D.L.;
RT "Orai1 and STIM reconstitute store-operated calcium channel function.";
RL J. Biol. Chem. 281:20661-20665(2006).
RN [26]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-171.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [27]
RP FUNCTION.
RX PubMed=16733527; DOI=10.1038/ncb1435;
RA Peinelt C., Vig M., Koomoa D.L., Beck A., Nadler M.J.S.,
RA Koblan-Huberson M., Lis A., Fleig A., Penner R., Kinet J.-P.;
RT "Amplification of CRAC current by STIM1 and CRACM1 (Orai1).";
RL Nat. Cell Biol. 8:771-773(2006).
RN [28]
RP FUNCTION, AND MUTAGENESIS OF GLU-87.
RX PubMed=16537481; DOI=10.1073/pnas.0510050103;
RA Spassova M.A., Soboloff J., He L.-P., Xu W., Dziadek M.A., Gill D.L.;
RT "STIM1 has a plasma membrane role in the activation of store-operated
RT Ca(2+) channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:4040-4045(2006).
RN [29]
RP INTERACTION WITH ORAI1.
RX PubMed=17905723; DOI=10.1096/fj.07-9449com;
RA Parvez S., Beck A., Peinelt C., Soboloff J., Lis A., Monteilh-Zoller M.,
RA Gill D.L., Fleig A., Penner R.;
RT "STIM2 protein mediates distinct store-dependent and store-independent
RT modes of CRAC channel activation.";
RL FASEB J. 22:752-761(2008).
RN [30]
RP INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, DOMAIN MICROTUBULE TIP
RP LOCALIZATION SIGNAL, AND MUTAGENESIS OF 644-ILE-PRO-645.
RX PubMed=19632184; DOI=10.1016/j.cell.2009.04.065;
RA Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S.,
RA Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A.,
RA Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.;
RT "An EB1-binding motif acts as a microtubule tip localization signal.";
RL Cell 138:366-376(2009).
RN [31]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-171.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [32]
RP INVOLVEMENT IN IMD10.
RX PubMed=19420366; DOI=10.1056/nejmoa0900082;
RA Picard C., McCarl C.A., Papolos A., Khalil S., Luthy K., Hivroz C.,
RA LeDeist F., Rieux-Laucat F., Rechavi G., Rao A., Fischer A., Feske S.;
RT "STIM1 mutation associated with a syndrome of immunodeficiency and
RT autoimmunity.";
RL N. Engl. J. Med. 360:1971-1980(2009).
RN [33]
RP INTERACTION WITH CRACR2A.
RX PubMed=20418871; DOI=10.1038/ncb2045;
RA Srikanth S., Jung H.J., Kim K.D., Souda P., Whitelegge J., Gwack Y.;
RT "A novel EF-hand protein, CRACR2A, is a cytosolic Ca2+ sensor that
RT stabilizes CRAC channels in T cells.";
RL Nat. Cell Biol. 12:436-446(2010).
RN [34]
RP INTERACTION WITH ATP1A1; ATP2A2; ATP2B1; ATP2B4; KPNB1; SLC35G1 AND XPO1.
RX PubMed=22084111; DOI=10.1073/pnas.1117231108;
RA Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.;
RT "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to
RT multiple transporters.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011).
RN [35]
RP FUNCTION, AND INTERACTION WITH SARAF.
RX PubMed=22464749; DOI=10.1016/j.cell.2012.01.055;
RA Palty R., Raveh A., Kaminsky I., Meller R., Reuveny E.;
RT "SARAF inactivates the store operated calcium entry machinery to prevent
RT excess calcium refilling.";
RL Cell 149:425-438(2012).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-512; SER-519;
RP SER-521; SER-567; SER-575; SER-608; SER-618; SER-621; SER-628; SER-660 AND
RP SER-668, AND 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 [37]
RP INVOLVEMENT IN STRMK, AND VARIANT STRMK TRP-304.
RX PubMed=24619930; DOI=10.1002/humu.22544;
RA Misceo D., Holmgren A., Louch W.E., Holme P.A., Mizobuchi M., Morales R.J.,
RA De Paula A.M., Stray-Pedersen A., Lyle R., Dalhus B., Christensen G.,
RA Stormorken H., Tjoennfjord G.E., Frengen E.;
RT "A dominant STIM1 mutation causes Stormorken syndrome.";
RL Hum. Mutat. 35:556-564(2014).
RN [38]
RP FUNCTION, AND VARIANT CYS-426.
RX PubMed=24621671; DOI=10.1177/0022034514527971;
RA Wang S., Choi M., Richardson A.S., Reid B.M., Seymen F., Yildirim M.,
RA Tuna E., Gencay K., Simmer J.P., Hu J.C.;
RT "STIM1 and SLC24A4 are critical for enamel maturation.";
RL J. Dent. Res. 93:94S-100S(2014).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512; THR-517; SER-519;
RP SER-521; SER-523; SER-567; SER-602 AND SER-608, AND IDENTIFICATION BY MASS
RP 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 [40]
RP FUNCTION, INVOLVEMENT IN STRMK, VARIANT STRMK TRP-304, CHARACTERIZATION OF
RP VARIANT STRMK TRP-304, AND MUTAGENESIS OF ASP-76.
RX PubMed=24591628; DOI=10.1073/pnas.1312520111;
RA Nesin V., Wiley G., Kousi M., Ong E.C., Lehmann T., Nicholl D.J., Suri M.,
RA Shahrizaila N., Katsanis N., Gaffney P.M., Wierenga K.J., Tsiokas L.;
RT "Activating mutations in STIM1 and ORAI1 cause overlapping syndromes of
RT tubular myopathy and congenital miosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4197-4202(2014).
RN [41]
RP INTERACTION WITH SPPL3.
RX PubMed=25384971; DOI=10.1128/mcb.01124-14;
RA Makowski S.L., Wang Z., Pomerantz J.L.;
RT "A protease-independent function for SPPL3 in NFAT activation.";
RL Mol. Cell. Biol. 35:451-467(2015).
RN [42]
RP INTERACTION WITH TMEM203.
RX PubMed=25996873; DOI=10.1371/journal.pone.0127480;
RA Shambharkar P.B., Bittinger M., Latario B., Xiong Z., Bandyopadhyay S.,
RA Davis V., Lin V., Yang Y., Valdez R., Labow M.A.;
RT "TMEM203 is a novel regulator of intracellular calcium homeostasis and is
RT required for spermatogenesis.";
RL PLoS ONE 10:E0127480-E0127480(2015).
RN [43]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STIMATE, AND MUTAGENESIS
RP OF ASP-76 AND LEU-258.
RX PubMed=26322679; DOI=10.1038/ncb3234;
RA Jing J., He L., Sun A., Quintana A., Ding Y., Ma G., Tan P., Liang X.,
RA Zheng X., Chen L., Shi X., Zhang S.L., Zhong L., Huang Y., Dong M.Q.,
RA Walker C.L., Hogan P.G., Wang Y., Zhou Y.;
RT "Proteomic mapping of ER-PM junctions identifies STIMATE as a regulator of
RT Ca(2+) influx.";
RL Nat. Cell Biol. 17:1339-1347(2015).
RN [44]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [45]
RP INTERACTION WITH ORAI1, AND SUBCELLULAR LOCATION.
RX PubMed=27185316; DOI=10.1159/000445574;
RA Zhang L., Wang L., Li S., Xue J., Luo D.;
RT "Calsequestrin-1 regulates store-operated Ca2+ entry by inhibiting STIM1
RT aggregation.";
RL Cell. Physiol. Biochem. 38:2183-2193(2016).
RN [46]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ORAI1.
RX PubMed=28219928; DOI=10.15252/embj.201592481;
RA Ben-Kasus Nissim T., Zhang X., Elazar A., Roy S., Stolwijk J.A., Zhou Y.,
RA Motiani R.K., Gueguinou M., Hempel N., Hershfinkel M., Gill D.L.,
RA Trebak M., Sekler I.;
RT "Mitochondria control store-operated Ca(2+) entry through Na(+) and redox
RT signals.";
RL EMBO J. 36:797-815(2017).
RN [47]
RP INTERACTION WITH EFHB; ORAI1 AND SARAF.
RX PubMed=30481768; DOI=10.1159/000495494;
RA Albarran L., Lopez J.J., Jardin I., Sanchez-Collado J., Berna-Erro A.,
RA Smani T., Camello P.J., Salido G.M., Rosado J.A.;
RT "EFHB is a Novel Cytosolic Ca2+ Sensor That Modulates STIM1-SARAF
RT Interaction.";
RL Cell. Physiol. Biochem. 51:1164-1178(2018).
RN [48]
RP STRUCTURE BY NMR OF 58-201 IN COMPLEX WITH CALCIUM, FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, CALCIUM-BINDING, AND MUTAGENESIS OF GLU-87; PHE-108;
RP GLY-110 AND LEU-195.
RX PubMed=18854159; DOI=10.1016/j.cell.2008.08.006;
RA Stathopulos P.B., Zheng L., Li G.Y., Plevin M.J., Ikura M.;
RT "Structural and mechanistic insights into STIM1-mediated initiation of
RT store-operated calcium entry.";
RL Cell 135:110-122(2008).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 344-444, COILED-COIL DOMAIN, AND
RP SUBUNIT.
RX PubMed=22451904; DOI=10.1073/pnas.1118947109;
RA Yang X., Jin H., Cai X., Li S., Shen Y.;
RT "Structural and mechanistic insights into the activation of Stromal
RT interaction molecule 1 (STIM1).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5657-5662(2012).
RN [50]
RP STRUCTURE BY NMR OF 312-387 IN COMPLEX WITH ORAI1, INTERACTION WITH ORAI1,
RP SUBUNIT, FUNCTION, COILED COIL, MUTAGENESIS OF 318-GLU--GLU-322; VAL-324;
RP LEU-347; LEU-351; 361-TYR-TYR-362; ALA-380 AND 382-LYS--LYS-386, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=24351972; DOI=10.1038/ncomms3963;
RA Stathopulos P.B., Schindl R., Fahrner M., Zheng L., Gasmi-Seabrook G.M.,
RA Muik M., Romanin C., Ikura M.;
RT "STIM1/Orai1 coiled-coil interplay in the regulation of store-operated
RT calcium entry.";
RL Nat. Commun. 4:2963-2963(2013).
RN [51]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 237-340, FUNCTION, COILED COIL,
RP AND SUBUNIT.
RX PubMed=24069340; DOI=10.1371/journal.pone.0074735;
RA Cui B., Yang X., Li S., Lin Z., Wang Z., Dong C., Shen Y.;
RT "The inhibitory helix controls the intramolecular conformational switching
RT of the C-terminus of STIM1.";
RL PLoS ONE 8:E74735-E74735(2013).
RN [52]
RP VARIANT IMD10 CYS-429.
RX PubMed=22190180; DOI=10.4049/jimmunol.1102507;
RA Fuchs S., Rensing-Ehl A., Speckmann C., Bengsch B., Schmitt-Graeff A.,
RA Bondzio I., Maul-Pavicic A., Bass T., Vraetz T., Strahm B., Ankermann T.,
RA Benson M., Caliebe A., Foelster-Holst R., Kaiser P., Thimme R.,
RA Schamel W.W., Schwarz K., Feske S., Ehl S.;
RT "Antiviral and regulatory T cell immunity in a patient with stromal
RT interaction molecule 1 deficiency.";
RL J. Immunol. 188:1523-1533(2012).
RN [53]
RP VARIANTS TAM1 GLN-72; GLY-84; ARG-109 AND ASN-109, AND CHARACTERIZATION OF
RP VARIANTS TAM1 GLN-72; GLY-84; ARG-109 AND ASN-109.
RX PubMed=23332920; DOI=10.1016/j.ajhg.2012.12.007;
RA Boehm J., Chevessier F., Maues De Paula A., Koch C., Attarian S., Feger C.,
RA Hantai D., Laforet P., Ghorab K., Vallat J.M., Fardeau M.,
RA Figarella-Branger D., Pouget J., Romero N.B., Koch M., Ebel C., Levy N.,
RA Krahn M., Eymard B., Bartoli M., Laporte J.;
RT "Constitutive activation of the calcium sensor STIM1 causes tubular-
RT aggregate myopathy.";
RL Am. J. Hum. Genet. 92:271-278(2013).
RN [54]
RP VARIANTS TAM1 THR-80; VAL-96; ILE-108; LEU-108 AND ASN-109,
RP CHARACTERIZATION OF VARIANTS TAM1 THR-80; VAL-96; ILE-108; LEU-108 AND
RP ASN-109, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25326555; DOI=10.1136/jmedgenet-2014-102623;
RA Boehm J., Chevessier F., Koch C., Peche G.A., Mora M., Morandi L.,
RA Pasanisi B., Moroni I., Tasca G., Fattori F., Ricci E.,
RA Penisson-Besnier I., Nadaj-Pakleza A., Fardeau M., Joshi P.R.,
RA Deschauer M., Romero N.B., Eymard B., Laporte J.;
RT "Clinical, histological and genetic characterisation of patients with
RT tubular aggregate myopathy caused by mutations in STIM1.";
RL J. Med. Genet. 51:824-833(2014).
RN [55]
RP VARIANTS TAM1 ARG-109 AND PHE-115.
RX PubMed=24570283; DOI=10.1007/s00415-014-7287-x;
RA Hedberg C., Niceta M., Fattori F., Lindvall B., Ciolfi A., D'Amico A.,
RA Tasca G., Petrini S., Tulinius M., Tartaglia M., Oldfors A., Bertini E.;
RT "Childhood onset tubular aggregate myopathy associated with de novo STIM1
RT mutations.";
RL J. Neurol. 261:870-876(2014).
RN [56]
RP VARIANTS STRMK PHE-115 AND TRP-304.
RX PubMed=25577287; DOI=10.1016/j.ymgme.2014.12.307;
RA Markello T., Chen D., Kwan J.Y., Horkayne-Szakaly I., Morrison A.,
RA Simakova O., Maric I., Lozier J., Cullinane A.R., Kilo T., Meister L.,
RA Pakzad K., Bone W., Chainani S., Lee E., Links A., Boerkoel C., Fischer R.,
RA Toro C., White J.G., Gahl W.A., Gunay-Aygun M.;
RT "York platelet syndrome is a CRAC channelopathy due to gain-of-function
RT mutations in STIM1.";
RL Mol. Genet. Metab. 114:474-482(2015).
RN [57]
RP VARIANT TAM1 ASP-81, AND CHARACTERIZATION OF VARIANT TAM1 ASP-81.
RX PubMed=25953320; DOI=10.1016/j.nmd.2015.04.005;
RA Walter M.C., Rossius M., Zitzelsberger M., Vorgerd M., Mueller-Felber W.,
RA Ertl-Wagner B., Zhang Y., Brinkmeier H., Senderek J., Schoser B.;
RT "50 years to diagnosis: Autosomal dominant tubular aggregate myopathy
RT caused by a novel STIM1 mutation.";
RL Neuromuscul. Disord. 25:577-584(2015).
CC -!- FUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE),
CC a Ca(2+) influx following depletion of intracellular Ca(2+) stores
CC (PubMed:15866891, PubMed:16005298, PubMed:16208375, PubMed:16537481,
CC PubMed:16733527, PubMed:16766533, PubMed:16807233, PubMed:18854159,
CC PubMed:19249086, PubMed:22464749, PubMed:24069340, PubMed:24351972,
CC PubMed:24591628, PubMed:26322679, PubMed:25326555, PubMed:28219928).
CC Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand
CC domain. Upon Ca(2+) depletion, translocates from the endoplasmic
CC reticulum to the plasma membrane where it activates the Ca(2+) release-
CC activated Ca(2+) (CRAC) channel subunit ORAI1 (PubMed:16208375,
CC PubMed:16537481). Involved in enamel formation (PubMed:24621671).
CC Activated following interaction with STIMATE, leading to promote STIM1
CC conformational switch (PubMed:26322679). {ECO:0000269|PubMed:15866891,
CC ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375,
CC ECO:0000269|PubMed:16537481, ECO:0000269|PubMed:16733527,
CC ECO:0000269|PubMed:16766533, ECO:0000269|PubMed:16807233,
CC ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19249086,
CC ECO:0000269|PubMed:22464749, ECO:0000269|PubMed:24069340,
CC ECO:0000269|PubMed:24351972, ECO:0000269|PubMed:24591628,
CC ECO:0000269|PubMed:24621671, ECO:0000269|PubMed:25326555,
CC ECO:0000269|PubMed:26322679, ECO:0000269|PubMed:28219928}.
CC -!- SUBUNIT: Monomer in the presence of Ca(2+); it oligomerizes in absence
CC of Ca(2+) (PubMed:18854159). Forms homooligomers and heterooligomers
CC with STIM2 (PubMed:11463338, PubMed:11983428, PubMed:18854159,
CC PubMed:22451904, PubMed:24351972, PubMed:24069340). Interacts (via the
CC transmembrane region and the SOAR/CAD domain) with SPPL3; the
CC interaction promotes the binding of STIM1 to ORAI1 (PubMed:25384971).
CC Interacts with ORAI1 (PubMed:17905723, PubMed:19249086,
CC PubMed:27185316, PubMed:24351972, PubMed:28219928, PubMed:30481768).
CC Interacts with MAPRE1; probably required for targeting to the growing
CC microtubule plus ends (PubMed:19632184). Interacts with
CC CRACR2A/EFCAB4B; the interaction is direct and takes place in absence
CC of Ca(2+) (PubMed:20418871). Forms a complex with CRACR2A/EFCAB4B and
CC ORAI1 at low concentration of Ca(2+), the complex dissociates at
CC elevated Ca(2+) concentrations (PubMed:20418871). Interacts with SARAF,
CC promoting a slow inactivation of STIM1-dependent SOCE activity,
CC possibly by facilitating the deoligomerization of STIM1
CC (PubMed:22464749, PubMed:30481768). Interacts with EFHB; the
CC interaction takes place upon Ca(2+)-store depletion and inhibits the
CC association with SARAF (PubMed:30481768). Interacts with ASPH (isoform
CC 8) (PubMed:22586105). Interacts with SLC35G1; intracellular Ca(2+)-
CC dependent. May interact with ATP1A1, ATP2A2, ATP2B1, ATP2B4, KPNB1 and
CC XPO1; through SLC35G1 (PubMed:22084111). Interacts with TMEM203
CC (PubMed:25996873). Interacts with STIMATE, promoting STIM1
CC conformational switch (PubMed:26322679). Interacts with TMEM178A (By
CC similarity). Interacts with CASQ1 (via C-terminal end and
CC preferentially with the monomeric form); this interaction increases in
CC response to a depletion of intracellular Ca(2+), decreases both STIM1
CC aggregation and clustering, interaction of STIM1 with ORAI1 and store-
CC operated Ca(2+) entry (SOCE) activity (PubMed:27185316). Interacts with
CC ADCY8 (PubMed:22494970). {ECO:0000250|UniProtKB:P70302,
CC ECO:0000269|PubMed:11463338, ECO:0000269|PubMed:11983428,
CC ECO:0000269|PubMed:17905723, ECO:0000269|PubMed:18854159,
CC ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:19632184,
CC ECO:0000269|PubMed:20418871, ECO:0000269|PubMed:22084111,
CC ECO:0000269|PubMed:22451904, ECO:0000269|PubMed:22464749,
CC ECO:0000269|PubMed:22494970, ECO:0000269|PubMed:22586105,
CC ECO:0000269|PubMed:24069340, ECO:0000269|PubMed:24351972,
CC ECO:0000269|PubMed:25384971, ECO:0000269|PubMed:25996873,
CC ECO:0000269|PubMed:26322679, ECO:0000269|PubMed:27185316,
CC ECO:0000269|PubMed:28219928, ECO:0000269|PubMed:30481768}.
CC -!- INTERACTION:
CC Q13586; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-448878, EBI-739773;
CC Q13586; Q8N7U6: EFHB; NbExp=3; IntAct=EBI-448878, EBI-25602059;
CC Q13586; P22607: FGFR3; NbExp=3; IntAct=EBI-448878, EBI-348399;
CC Q13586; Q14957: GRIN2C; NbExp=3; IntAct=EBI-448878, EBI-8285963;
CC Q13586; Q5SUL5: HLA-A; NbExp=3; IntAct=EBI-448878, EBI-8561769;
CC Q13586; P01112: HRAS; NbExp=4; IntAct=EBI-448878, EBI-350145;
CC Q13586; P15260: IFNGR1; NbExp=3; IntAct=EBI-448878, EBI-1030755;
CC Q13586; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-448878, EBI-8503746;
CC Q13586; Q92993: KAT5; NbExp=3; IntAct=EBI-448878, EBI-399080;
CC Q13586; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-448878, EBI-11742507;
CC Q13586; Q96CV9: OPTN; NbExp=3; IntAct=EBI-448878, EBI-748974;
CC Q13586; Q96D31: ORAI1; NbExp=21; IntAct=EBI-448878, EBI-2291476;
CC Q13586; P30101: PDIA3; NbExp=3; IntAct=EBI-448878, EBI-979862;
CC Q13586; P62937-2: PPIA; NbExp=3; IntAct=EBI-448878, EBI-25884072;
CC Q13586; P23284: PPIB; NbExp=3; IntAct=EBI-448878, EBI-359252;
CC Q13586; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-448878, EBI-712367;
CC Q13586; Q96BY9: SARAF; NbExp=4; IntAct=EBI-448878, EBI-722561;
CC Q13586; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-448878, EBI-9090795;
CC Q13586; P30825: SLC7A1; NbExp=3; IntAct=EBI-448878, EBI-4289564;
CC Q13586; Q13586: STIM1; NbExp=9; IntAct=EBI-448878, EBI-448878;
CC Q13586; Q9P246: STIM2; NbExp=5; IntAct=EBI-448878, EBI-448891;
CC Q13586; P48995: TRPC1; NbExp=6; IntAct=EBI-448878, EBI-929665;
CC Q13586; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-448878, EBI-741480;
CC Q13586; P61981: YWHAG; NbExp=3; IntAct=EBI-448878, EBI-359832;
CC Q13586; Q9Y649; NbExp=3; IntAct=EBI-448878, EBI-25900580;
CC Q13586; P62157: CALM; Xeno; NbExp=2; IntAct=EBI-448878, EBI-397403;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:11004585, ECO:0000269|PubMed:16005298,
CC ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:18854159,
CC ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:27185316,
CC ECO:0000269|PubMed:28219928}. Endoplasmic reticulum membrane; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:16005298,
CC ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:18854159,
CC ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:26322679,
CC ECO:0000269|PubMed:27185316}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19632184}. Sarcoplasmic reticulum
CC {ECO:0000269|PubMed:25326555}. Note=Translocates from the endoplasmic
CC reticulum to the cell membrane in response to a depletion of
CC intracellular calcium and is detected at punctae corresponding to
CC junctions between the endoplasmic reticulum and the cell membrane
CC (PubMed:19249086, PubMed:16005298, PubMed:16208375, PubMed:18854159).
CC Associated with the microtubule network at the growing distal tip of
CC microtubules (PubMed:19632184). Colocalizes with ORAI1 at the cell
CC membrane (PubMed:27185316). Colocalizes preferentially with CASQ1 at
CC endoplasmic reticulum in response to a depletion of intracellular
CC calcium (PubMed:27185316). {ECO:0000269|PubMed:16005298,
CC ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:18854159,
CC ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:19632184,
CC ECO:0000269|PubMed:27185316}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13586-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13586-2; Sequence=VSP_055150, VSP_055151;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in various human primary
CC cells and tumor cell lines. {ECO:0000269|PubMed:11004585,
CC ECO:0000269|PubMed:11463338}.
CC -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates
CC interaction with MAPRE1 and targeting to the growing microtubule plus
CC ends. {ECO:0000269|PubMed:19632184}.
CC -!- DOMAIN: The STIM1 Orai1-activating region/CRAC-activating domain
CC (SOAR/CAD) mediates interaction with ORAI1 to activate the channel.
CC {ECO:0000269|PubMed:19632184}.
CC -!- PTM: Glycosylation is required for cell surface expression.
CC {ECO:0000269|PubMed:11004585, ECO:0000269|PubMed:11983428,
CC ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16263699,
CC ECO:0000269|PubMed:19159218}.
CC -!- PTM: Phosphorylated predominantly on Ser residues.
CC {ECO:0000269|PubMed:11004585}.
CC -!- DISEASE: Immunodeficiency 10 (IMD10) [MIM:612783]: An immune disorder
CC characterized by recurrent infections, impaired activation and
CC proliferative response of T-cells, decreased T-cell production of
CC cytokines, lymphadenopathy, and normal lymphocytes counts and serum
CC immunoglobulin levels. Additional features include thrombocytopenia,
CC autoimmune hemolytic anemia, myopathy, partial iris hypoplasia,
CC hepatosplenomegaly and defective enamel dentition.
CC {ECO:0000269|PubMed:19420366, ECO:0000269|PubMed:22190180}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Myopathy, tubular aggregate, 1 (TAM1) [MIM:160565]: A rare
CC congenital myopathy characterized by regular arrays of membrane tubules
CC on muscle biopsies without additional histopathological hallmarks.
CC Tubular aggregates in muscle are structures of variable appearance
CC consisting of an outer tubule containing either one or more
CC microtubule-like structures or amorphous material. They may occur in a
CC variety of circumstances, including inherited myopathies, alcohol- and
CC drug-induced myopathies, exercise-induced cramps or muscle weakness.
CC {ECO:0000269|PubMed:23332920, ECO:0000269|PubMed:24570283,
CC ECO:0000269|PubMed:25326555, ECO:0000269|PubMed:25953320}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Stormorken syndrome (STRMK) [MIM:185070]: A rare autosomal
CC dominant disease characterized by mild bleeding tendency,
CC thrombocytopathy, thrombocytopenia, mild anemia, asplenia, tubular
CC aggregate myopathy, miosis, headache, and ichthyosis.
CC {ECO:0000269|PubMed:24591628, ECO:0000269|PubMed:24619930,
CC ECO:0000269|PubMed:25577287}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Transfection of STIM1 into cells derived from a rhabdoid
CC tumor and from a rhabdomyosarcoma that do not express detectable levels
CC of STIM1 can induce cell death, suggesting a possible role in the
CC control of rhabdomyosarcomas and rhabdoid tumors.
CC {ECO:0000269|PubMed:9377559}.
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DR EMBL; U52426; AAC51627.1; -; mRNA.
DR EMBL; AK314928; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC015689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471158; EAX02581.1; -; Genomic_DNA.
DR EMBL; BC021300; AAH21300.1; -; mRNA.
DR CCDS; CCDS60706.1; -. [Q13586-2]
DR CCDS; CCDS7749.1; -. [Q13586-1]
DR RefSeq; NP_001264891.1; NM_001277962.1. [Q13586-2]
DR RefSeq; NP_003147.2; NM_003156.3. [Q13586-1]
DR PDB; 2K60; NMR; -; A=58-201.
DR PDB; 2MAJ; NMR; -; A/C=312-387.
DR PDB; 2MAK; NMR; -; A/C=312-387.
DR PDB; 3TEQ; X-ray; 1.90 A; A/B/C/D=344-444.
DR PDB; 4O9B; X-ray; 2.60 A; A/B/C/D=237-340.
DR PDB; 6YEL; NMR; -; A=234-343.
DR PDBsum; 2K60; -.
DR PDBsum; 2MAJ; -.
DR PDBsum; 2MAK; -.
DR PDBsum; 3TEQ; -.
DR PDBsum; 4O9B; -.
DR PDBsum; 6YEL; -.
DR AlphaFoldDB; Q13586; -.
DR BMRB; Q13586; -.
DR SMR; Q13586; -.
DR BioGRID; 112662; 363.
DR CORUM; Q13586; -.
DR DIP; DIP-31121N; -.
DR ELM; Q13586; -.
DR IntAct; Q13586; 70.
DR MINT; Q13586; -.
DR BindingDB; Q13586; -.
DR ChEMBL; CHEMBL3832644; -.
DR ChEMBL; CHEMBL4296083; -.
DR ChEMBL; CHEMBL4296084; -.
DR TCDB; 1.A.52.1.1; the ca(2+) release-activated ca(2+) (crac) channel (crac-c) family.
DR GlyConnect; 1771; 6 N-Linked glycans (1 site).
DR GlyGen; Q13586; 4 sites, 6 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q13586; -.
DR MetOSite; Q13586; -.
DR PhosphoSitePlus; Q13586; -.
DR BioMuta; STIM1; -.
DR DMDM; 209572721; -.
DR EPD; Q13586; -.
DR jPOST; Q13586; -.
DR MassIVE; Q13586; -.
DR MaxQB; Q13586; -.
DR PaxDb; Q13586; -.
DR PeptideAtlas; Q13586; -.
DR PRIDE; Q13586; -.
DR ProteomicsDB; 23035; -.
DR ProteomicsDB; 59584; -. [Q13586-1]
DR Antibodypedia; 2591; 550 antibodies from 45 providers.
DR DNASU; 6786; -.
DR Ensembl; ENST00000300737.8; ENSP00000300737.4; ENSG00000167323.12. [Q13586-1]
DR Ensembl; ENST00000527651.5; ENSP00000436208.1; ENSG00000167323.12. [Q13586-2]
DR GeneID; 6786; -.
DR KEGG; hsa:6786; -.
DR UCSC; uc001lyv.3; human. [Q13586-1]
DR CTD; 6786; -.
DR DisGeNET; 6786; -.
DR GeneCards; STIM1; -.
DR HGNC; HGNC:11386; STIM1.
DR HPA; ENSG00000167323; Low tissue specificity.
DR MalaCards; STIM1; -.
DR MIM; 160565; phenotype.
DR MIM; 185070; phenotype.
DR MIM; 605921; gene.
DR MIM; 612783; phenotype.
DR neXtProt; NX_Q13586; -.
DR OpenTargets; ENSG00000167323; -.
DR Orphanet; 317430; Combined immunodeficiency due to STIM1 deficiency.
DR Orphanet; 3204; Stormorken-Sjaastad-Langslet syndrome.
DR Orphanet; 2593; Tubular aggregate myopathy.
DR PharmGKB; PA36195; -.
DR VEuPathDB; HostDB:ENSG00000167323; -.
DR eggNOG; KOG4403; Eukaryota.
DR GeneTree; ENSGT00390000000214; -.
DR HOGENOM; CLU_010588_0_1_1; -.
DR InParanoid; Q13586; -.
DR OMA; FLCCVLK; -.
DR PhylomeDB; Q13586; -.
DR TreeFam; TF313487; -.
DR PathwayCommons; Q13586; -.
DR Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-HSA-5578775; Ion homeostasis.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; Q13586; -.
DR SIGNOR; Q13586; -.
DR BioGRID-ORCS; 6786; 12 hits in 1080 CRISPR screens.
DR ChiTaRS; STIM1; human.
DR EvolutionaryTrace; Q13586; -.
DR GeneWiki; STIM1; -.
DR GenomeRNAi; 6786; -.
DR Pharos; Q13586; Tbio.
DR PRO; PR:Q13586; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13586; protein.
DR Bgee; ENSG00000167323; Expressed in gastrocnemius and 165 other tissues.
DR ExpressionAtlas; Q13586; baseline and differential.
DR Genevisible; Q13586; HS.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005246; F:calcium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0032237; P:activation of store-operated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0005513; P:detection of calcium ion; IDA:UniProtKB.
DR GO; GO:0070166; P:enamel mineralization; IMP:UniProtKB.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0051924; P:regulation of calcium ion transport; IDA:UniProtKB.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; IMP:UniProtKB.
DR GO; GO:0002115; P:store-operated calcium entry; IDA:UniProtKB.
DR CDD; cd09573; SAM_STIM1; 1.
DR CDD; cd11722; SOAR; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR032393; SOAR.
DR InterPro; IPR037608; STIM.
DR InterPro; IPR037609; STIM1_SAM.
DR InterPro; IPR030463; STM1.
DR PANTHER; PTHR15136; PTHR15136; 1.
DR PANTHER; PTHR15136:SF9; PTHR15136:SF9; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF16533; SOAR; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium transport;
KW Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Disease variant;
KW Endoplasmic reticulum; Glycoprotein; Ion transport; Membrane;
KW Metal-binding; Microtubule; Phosphoprotein; Reference proteome;
KW Sarcoplasmic reticulum; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..685
FT /note="Stromal interaction molecule 1"
FT /id="PRO_0000033326"
FT TOPO_DOM 23..213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 63..98
FT /note="EF-hand"
FT DOMAIN 132..200
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 334..444
FT /note="SOAR/CAD"
FT REGION 490..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 248..442
FT /evidence="ECO:0000269|PubMed:22451904,
FT ECO:0000269|PubMed:24069340, ECO:0000269|PubMed:24351972"
FT MOTIF 642..645
FT /note="Microtubule tip localization signal"
FT COMPBIAS 490..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P70302"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 517
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70302"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 665
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11983428"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11983428,
FT ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16263699,
FT ECO:0000269|PubMed:19159218"
FT VAR_SEQ 515..540
FT /note="DLTHSDSESSLHMSDRQRVAPKPPQM -> GSSLKANRLSSKGFDPFRFGVL
FT PPHE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055150"
FT VAR_SEQ 541..685
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055151"
FT VARIANT 72
FT /note="H -> Q (in TAM1; myoblasts with the mutation have
FT significantly increased clustering of STIM1, regardless of
FT calcium levels, indicating that calcium sensing in the
FT sarcoplasmic reticulum is impaired; dbSNP:rs397515436)"
FT /evidence="ECO:0000269|PubMed:23332920"
FT /id="VAR_069892"
FT VARIANT 80
FT /note="N -> T (in TAM1; myoblasts with the mutation have
FT significantly increased clustering of STIM1, regardless of
FT calcium levels, indicating that calcium sensing in the
FT sarcoplasmic reticulum is impaired; dbSNP:rs748277951)"
FT /evidence="ECO:0000269|PubMed:25326555"
FT /id="VAR_075619"
FT VARIANT 81
FT /note="G -> D (in TAM1; increases store-operated Ca(2+)
FT influx)"
FT /evidence="ECO:0000269|PubMed:25953320"
FT /id="VAR_075620"
FT VARIANT 84
FT /note="D -> G (in TAM1; myoblasts with the mutation have
FT significantly increased clustering of STIM1, regardless of
FT calcium levels, indicating that calcium sensing in the
FT sarcoplasmic reticulum is impaired; dbSNP:rs397514675)"
FT /evidence="ECO:0000269|PubMed:23332920"
FT /id="VAR_069893"
FT VARIANT 96
FT /note="L -> V (in TAM1; myoblasts with the mutation have
FT significantly increased clustering of STIM1, regardless of
FT calcium levels, indicating that calcium sensing in the
FT sarcoplasmic reticulum is impaired)"
FT /evidence="ECO:0000269|PubMed:25326555"
FT /id="VAR_075621"
FT VARIANT 108
FT /note="F -> I (in TAM1; myoblasts with the mutation have
FT significantly increased clustering of STIM1, regardless of
FT calcium levels, indicating that calcium sensing in the
FT sarcoplasmic reticulum is impaired)"
FT /evidence="ECO:0000269|PubMed:25326555"
FT /id="VAR_075622"
FT VARIANT 108
FT /note="F -> L (in TAM1; myoblasts with the mutation have
FT significantly increased clustering of STIM1, regardless of
FT calcium levels, indicating that calcium sensing in the
FT sarcoplasmic reticulum is impaired)"
FT /evidence="ECO:0000269|PubMed:25326555"
FT /id="VAR_075623"
FT VARIANT 109
FT /note="H -> N (in TAM1; myoblasts with the mutation have
FT significantly increased clustering of STIM1, regardless of
FT calcium levels, indicating that calcium sensing in the
FT sarcoplasmic reticulum is impaired; dbSNP:rs397514676)"
FT /evidence="ECO:0000269|PubMed:23332920,
FT ECO:0000269|PubMed:25326555"
FT /id="VAR_069894"
FT VARIANT 109
FT /note="H -> R (in TAM1; myoblasts with the mutation have
FT significantly increased clustering of STIM1, regardless of
FT calcium levels, indicating that calcium sensing in the
FT sarcoplasmic reticulum is impaired; dbSNP:rs397514677)"
FT /evidence="ECO:0000269|PubMed:23332920,
FT ECO:0000269|PubMed:24570283"
FT /id="VAR_069895"
FT VARIANT 115
FT /note="I -> F (in STRMK and TAM1; dbSNP:rs527236030)"
FT /evidence="ECO:0000269|PubMed:24570283,
FT ECO:0000269|PubMed:25577287"
FT /id="VAR_074037"
FT VARIANT 304
FT /note="R -> W (in STRMK; autosomal dominant; promotes
FT constitutive activation of the Ca(2+) release-activated
FT Ca(2+) (CRAC) channel; dbSNP:rs483352867)"
FT /evidence="ECO:0000269|PubMed:24591628,
FT ECO:0000269|PubMed:24619930, ECO:0000269|PubMed:25577287"
FT /id="VAR_071476"
FT VARIANT 426
FT /note="R -> C (probable disease-associated variant found in
FT a patient with autosomal recessive hypomaturation enamel
FT malformations, nail dysplasia and frequent throat
FT infections; dbSNP:rs1057519505)"
FT /evidence="ECO:0000269|PubMed:24621671"
FT /id="VAR_071477"
FT VARIANT 429
FT /note="R -> C (in IMD10; dbSNP:rs397514671)"
FT /evidence="ECO:0000269|PubMed:22190180"
FT /id="VAR_069896"
FT VARIANT 538
FT /note="P -> S (in dbSNP:rs35960304)"
FT /id="VAR_061878"
FT MUTAGEN 76
FT /note="D->A,N: Increases Ca(2+) influx even when Ca(2+)
FT stores are not depleted. Promotes constitutive activation
FT of the Ca2+ release-activated Ca2+ (CRAC) channel."
FT /evidence="ECO:0000269|PubMed:16005298,
FT ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:24591628,
FT ECO:0000269|PubMed:26322679"
FT MUTAGEN 78
FT /note="D->N: Increases Ca(2+) influx even when Ca(2+)
FT stores are not depleted."
FT /evidence="ECO:0000269|PubMed:16807233"
FT MUTAGEN 87
FT /note="E->A,Q: Increases Ca(2+) influx through activation
FT of CRAC channels, even when Ca(2+) stores are not
FT depleted."
FT /evidence="ECO:0000269|PubMed:16537481,
FT ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:18854159"
FT MUTAGEN 108
FT /note="F->D: Constitutive localization in punctae at the
FT cell membrane and constitutive activation of CRAC channels;
FT when associated with D-110."
FT /evidence="ECO:0000269|PubMed:18854159"
FT MUTAGEN 110
FT /note="G->D: Constitutive localization in punctae at the
FT cell membrane and constitutive activation of CRAC channels;
FT when associated with D-108."
FT /evidence="ECO:0000269|PubMed:18854159"
FT MUTAGEN 195
FT /note="L->R: Constitutive localization in punctae at the
FT cell membrane and constitutive activation of CRAC
FT channels."
FT /evidence="ECO:0000269|PubMed:18854159"
FT MUTAGEN 258
FT /note="L->G: Promotes constitutive activation of the Ca2+
FT release-activated Ca2+ (CRAC) channel."
FT /evidence="ECO:0000269|PubMed:26322679"
FT MUTAGEN 318..322
FT /note="EEELE->QQQLQ: Constitutive activation of CRAC
FT channels."
FT /evidence="ECO:0000269|PubMed:24351972"
FT MUTAGEN 324
FT /note="V->P: Reduces activation of CRAC channels."
FT /evidence="ECO:0000269|PubMed:24351972"
FT MUTAGEN 347
FT /note="L->R: Abolishes colocalization with ORAI1 and
FT activation of CRAC channels."
FT /evidence="ECO:0000269|PubMed:24351972"
FT MUTAGEN 351
FT /note="L->R: Abolishes colocalization with ORAI1 and
FT activation of CRAC channels."
FT /evidence="ECO:0000269|PubMed:24351972"
FT MUTAGEN 361..362
FT /note="YY->KK: Abolishes activation of CRAC channels."
FT /evidence="ECO:0000269|PubMed:24351972"
FT MUTAGEN 380
FT /note="A->R: Constitutive activation of CRAC channels."
FT /evidence="ECO:0000269|PubMed:24351972"
FT MUTAGEN 382..386
FT /note="KIKKK->EIEEE: Abolishes activation of CRAC
FT channels."
FT /evidence="ECO:0000269|PubMed:24351972"
FT MUTAGEN 383
FT /note="I->R: Abolishes activation of CRAC channels."
FT MUTAGEN 644..645
FT /note="IP->NN: Loss of interaction with MAPRE1 and
FT association with the growing microtubule plus ends."
FT /evidence="ECO:0000269|PubMed:19632184"
FT CONFLICT 505
FT /note="E -> G (in Ref. 2; AK314928)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="S -> R (in Ref. 1; AAC51627)"
FT /evidence="ECO:0000305"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:2K60"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2K60"
FT TURN 85..90
FT /evidence="ECO:0007829|PDB:2K60"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:2K60"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:2K60"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2K60"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:2K60"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:2K60"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:2K60"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:2K60"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:2K60"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:2K60"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:2K60"
FT HELIX 249..271
FT /evidence="ECO:0007829|PDB:4O9B"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:4O9B"
FT HELIX 276..334
FT /evidence="ECO:0007829|PDB:4O9B"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:2MAK"
FT HELIX 345..391
FT /evidence="ECO:0007829|PDB:3TEQ"
FT HELIX 393..397
FT /evidence="ECO:0007829|PDB:3TEQ"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:3TEQ"
FT HELIX 408..437
FT /evidence="ECO:0007829|PDB:3TEQ"
SQ SEQUENCE 685 AA; 77423 MW; FFB5E7CB3D68A7A6 CRC64;
MDVCVRLALW LLWGLLLHQG QSLSHSHSEK ATGTSSGANS EESTAAEFCR IDKPLCHSED
EKLSFEAVRN IHKLMDDDAN GDVDVEESDE FLREDLNYHD PTVKHSTFHG EDKLISVEDL
WKAWKSSEVY NWTVDEVVQW LITYVELPQY EETFRKLQLS GHAMPRLAVT NTTMTGTVLK
MTDRSHRQKL QLKALDTVLF GPPLLTRHNH LKDFMLVVSI VIGVGGCWFA YIQNRYSKEH
MKKMMKDLEG LHRAEQSLHD LQERLHKAQE EHRTVEVEKV HLEKKLRDEI NLAKQEAQRL
KELREGTENE RSRQKYAEEE LEQVREALRK AEKELESHSS WYAPEALQKW LQLTHEVEVQ
YYNIKKQNAE KQLLVAKEGA EKIKKKRNTL FGTFHVAHSS SLDDVDHKIL TAKQALSEVT
AALRERLHRW QQIEILCGFQ IVNNPGIHSL VAALNIDPSW MGSTRPNPAH FIMTDDVDDM
DEEIVSPLSM QSPSLQSSVR QRLTEPQHGL GSQRDLTHSD SESSLHMSDR QRVAPKPPQM
SRAADEALNA MTSNGSHRLI EGVHPGSLVE KLPDSPALAK KALLALNHGL DKAHSLMELS
PSAPPGGSPH LDSSRSHSPS SPDPDTPSPV GDSRALQASR NTRIPHLAGK KAVAEEDNGS
IGEETDSSPG RKKFPLKIFK KPLKK
