STIM2_HUMAN
ID STIM2_HUMAN Reviewed; 746 AA.
AC Q9P246; A6H8L7; B7ZVY0; Q96BF1; Q9BQH2; Q9H8R1;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Stromal interaction molecule 2;
DE Flags: Precursor;
GN Name=STIM2; Synonyms=KIAA1482;
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), PROTEIN SEQUENCE OF 15-24, SUBUNIT,
RP TISSUE SPECIFICITY, GLYCOSYLATION, AND PHOSPHORYLATION.
RC TISSUE=Fetal brain, and Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 192-746 (ISOFORM 1).
RC TISSUE=Brain, and Retina;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-746 (ISOFORM 1).
RC TISSUE=Ovarian carcinoma;
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 [6]
RP FUNCTION.
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-80 AND GLU-91.
RX PubMed=16860747; DOI=10.1016/j.cub.2006.05.051;
RA Soboloff J., Spassova M.A., Hewavitharana T., He L.P., Xu W.,
RA Johnstone L.S., Dziadek M.A., Gill D.L.;
RT "STIM2 is an inhibitor of STIM1-mediated store-operated Ca2+ entry.";
RL Curr. Biol. 16:1465-1470(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-80.
RX PubMed=18160041; DOI=10.1016/j.cell.2007.11.039;
RA Brandman O., Liou J., Park W.S., Meyer T.;
RT "STIM2 is a feedback regulator that stabilizes basal cytosolic and
RT endoplasmic reticulum Ca2+ levels.";
RL Cell 131:1327-1339(2007).
RN [9]
RP CALCIUM-BINDING.
RX PubMed=18166150; DOI=10.1016/j.bbrc.2007.12.129;
RA Zheng L., Stathopulos P.B., Li G.-Y., Ikura M.;
RT "Biophysical characterization of the EF-hand and SAM domain containing Ca2+
RT sensory region of STIM1 and STIM2.";
RL Biochem. Biophys. Res. Commun. 369:240-246(2008).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-609; SER-621; SER-661 AND
RP SER-680, 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 [12]
RP OLIGOMERIZATION.
RX PubMed=19019825; DOI=10.1074/jbc.c800178200;
RA Stathopulos P.B., Zheng L., Ikura M.;
RT "Stromal interaction molecule (STIM) 1 and STIM2 calcium sensing regions
RT exhibit distinct unfolding and oligomerization kinetics.";
RL J. Biol. Chem. 284:728-732(2009).
RN [13]
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 [14]
RP FUNCTION.
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 [15]
RP FUNCTION.
RX PubMed=23359669; DOI=10.1113/jphysiol.2012.245399;
RA Thiel M., Lis A., Penner R.;
RT "STIM2 drives Ca2+ oscillations through store-operated Ca2+ entry caused by
RT mild store depletion.";
RL J. Physiol. (Lond.) 591:1433-1445(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; SER-609; SER-661 AND
RP SER-665, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, 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 [18]
RP STRUCTURE BY NMR OF 62-205 IN COMPLEX WITH CALCIUM IONS, FUNCTION, AND
RP CIRCULAR DICHROISM.
RX PubMed=21217057; DOI=10.1073/pnas.1015125108;
RA Zheng L., Stathopulos P.B., Schindl R., Li G.Y., Romanin C., Ikura M.;
RT "Auto-inhibitory role of the EF-SAM domain of STIM proteins in store-
RT operated calcium entry.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1337-1342(2011).
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 Functions as a highly sensitive Ca(2+) sensor in the endoplasmic
CC reticulum which activates both store-operated and store-independent
CC Ca(2+)-influx. Regulates basal cytosolic and endoplasmic reticulum
CC Ca(2+) concentrations. Upon mild variations of the endoplasmic
CC reticulum Ca(2+) concentration, translocates from the endoplasmic
CC reticulum to the plasma membrane where it probably activates the Ca(2+)
CC release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May
CC inhibit STIM1-mediated Ca(2+) influx. {ECO:0000269|PubMed:16005298,
CC ECO:0000269|PubMed:16860747, ECO:0000269|PubMed:17905723,
CC ECO:0000269|PubMed:18160041, ECO:0000269|PubMed:21217057,
CC ECO:0000269|PubMed:22464749, ECO:0000269|PubMed:23359669}.
CC -!- SUBUNIT: Oligomer with STIM1. Interacts with ORAI1.
CC {ECO:0000269|PubMed:11463338, ECO:0000269|PubMed:17905723,
CC ECO:0000269|PubMed:21217057}.
CC -!- INTERACTION:
CC Q9P246; Q13586: STIM1; NbExp=5; IntAct=EBI-448891, EBI-448878;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16860747, ECO:0000269|PubMed:17905723,
CC ECO:0000269|PubMed:18160041}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16860747, ECO:0000269|PubMed:17905723,
CC ECO:0000269|PubMed:18160041}. Note=Dynamically translocates from a
CC uniform endoplasmic reticulum distribution to punctual endoplasmic
CC reticulum-plasma membrane junctions in response to decrease in
CC endoplasmic reticulum Ca(2+) concentration.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9P246-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P246-2; Sequence=VSP_057171, VSP_057172;
CC Name=3;
CC IsoId=Q9P246-3; Sequence=VSP_057173, VSP_057174;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues and tumor cell lines
CC examined. {ECO:0000269|PubMed:11463338}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11463338}.
CC -!- PTM: Phosphorylated predominantly on Ser residues.
CC {ECO:0000269|PubMed:11463338}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96006.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
CC Sequence=BAB14545.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14545.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=CAB66512.2; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
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DR EMBL; AF328905; AAK82337.1; -; mRNA.
DR EMBL; AB040915; BAA96006.1; ALT_SEQ; mRNA.
DR EMBL; AL136577; CAB66512.2; ALT_SEQ; mRNA.
DR EMBL; BC015659; AAH15659.2; -; mRNA.
DR EMBL; BC057231; AAH57231.1; -; mRNA.
DR EMBL; BC136449; AAI36450.1; -; mRNA.
DR EMBL; BC146661; AAI46662.1; -; mRNA.
DR EMBL; BC152554; AAI52555.1; -; mRNA.
DR EMBL; BC171766; AAI71766.1; -; mRNA.
DR EMBL; AK023369; BAB14545.1; ALT_SEQ; mRNA.
DR CCDS; CCDS3440.2; -. [Q9P246-1]
DR CCDS; CCDS54752.1; -. [Q9P246-3]
DR RefSeq; NP_001162588.1; NM_001169117.1. [Q9P246-3]
DR RefSeq; NP_001162589.1; NM_001169118.1.
DR RefSeq; NP_065911.3; NM_020860.3. [Q9P246-1]
DR PDB; 2L5Y; NMR; -; A=62-205.
DR PDBsum; 2L5Y; -.
DR AlphaFoldDB; Q9P246; -.
DR BMRB; Q9P246; -.
DR SMR; Q9P246; -.
DR BioGRID; 121666; 147.
DR IntAct; Q9P246; 20.
DR MINT; Q9P246; -.
DR STRING; 9606.ENSP00000417569; -.
DR ChEMBL; CHEMBL4296084; -.
DR TCDB; 1.A.52.1.1; the ca(2+) release-activated ca(2+) (crac) channel (crac-c) family.
DR GlyGen; Q9P246; 1 site.
DR iPTMnet; Q9P246; -.
DR PhosphoSitePlus; Q9P246; -.
DR BioMuta; STIM2; -.
DR DMDM; 17369338; -.
DR EPD; Q9P246; -.
DR jPOST; Q9P246; -.
DR MassIVE; Q9P246; -.
DR MaxQB; Q9P246; -.
DR PaxDb; Q9P246; -.
DR PeptideAtlas; Q9P246; -.
DR PRIDE; Q9P246; -.
DR ProteomicsDB; 83730; -. [Q9P246-1]
DR Antibodypedia; 10303; 284 antibodies from 36 providers.
DR DNASU; 57620; -.
DR Ensembl; ENST00000467011.6; ENSP00000419383.2; ENSG00000109689.19. [Q9P246-3]
DR Ensembl; ENST00000467087.7; ENSP00000419073.2; ENSG00000109689.19. [Q9P246-1]
DR GeneID; 57620; -.
DR KEGG; hsa:57620; -.
DR MANE-Select; ENST00000467087.7; ENSP00000419073.2; NM_020860.4; NP_065911.3.
DR UCSC; uc003gsg.6; human. [Q9P246-1]
DR CTD; 57620; -.
DR DisGeNET; 57620; -.
DR GeneCards; STIM2; -.
DR HGNC; HGNC:19205; STIM2.
DR HPA; ENSG00000109689; Tissue enhanced (choroid).
DR MIM; 610841; gene.
DR neXtProt; NX_Q9P246; -.
DR OpenTargets; ENSG00000109689; -.
DR PharmGKB; PA134926985; -.
DR VEuPathDB; HostDB:ENSG00000109689; -.
DR eggNOG; KOG4403; Eukaryota.
DR GeneTree; ENSGT00390000000214; -.
DR HOGENOM; CLU_010588_2_0_1; -.
DR InParanoid; Q9P246; -.
DR OrthoDB; 373308at2759; -.
DR PhylomeDB; Q9P246; -.
DR PathwayCommons; Q9P246; -.
DR SignaLink; Q9P246; -.
DR BioGRID-ORCS; 57620; 10 hits in 1029 CRISPR screens.
DR ChiTaRS; STIM2; human.
DR GeneWiki; STIM2; -.
DR GenomeRNAi; 57620; -.
DR Pharos; Q9P246; Tbio.
DR PRO; PR:Q9P246; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9P246; protein.
DR Bgee; ENSG00000109689; Expressed in olfactory segment of nasal mucosa and 170 other tissues.
DR ExpressionAtlas; Q9P246; baseline and differential.
DR Genevisible; Q9P246; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005246; F:calcium channel regulator activity; IMP:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0015279; F:store-operated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0032237; P:activation of store-operated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:UniProtKB.
DR GO; GO:0002115; P:store-operated calcium entry; IBA:GO_Central.
DR CDD; cd09574; SAM_STIM2; 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; IPR037610; STIM2_SAM.
DR PANTHER; PTHR15136; PTHR15136; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF16533; SOAR; 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 Coiled coil; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..14
FT /evidence="ECO:0000269|PubMed:11463338"
FT CHAIN 15..746
FT /note="Stromal interaction molecule 2"
FT /id="PRO_0000033328"
FT TOPO_DOM 15..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..746
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 67..102
FT /note="EF-hand"
FT DOMAIN 136..204
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 483..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..394
FT /evidence="ECO:0000255"
FT COMPBIAS 504..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P83093"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P83093"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MNAAGIRAPEAAGADGTRLAPGGSPCLRRRGRPEESPAAVVAPRGAG
FT ELQAAGAPLRFYPASPRRLHRASTPGPAWGWLLRRRRWAAL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057171"
FT VAR_SEQ 383
FT /note="E -> EVAASYLIQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057172"
FT VAR_SEQ 588..599
FT /note="WEVPDTASECDS -> CIHLGLGACKSE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057173"
FT VAR_SEQ 600..746
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057174"
FT MUTAGEN 80
FT /note="D->A: No effect on inhibitory activity; when
FT associated with A-91."
FT /evidence="ECO:0000269|PubMed:16860747,
FT ECO:0000269|PubMed:18160041"
FT MUTAGEN 91
FT /note="E->A: No effect on inhibitory activity; when
FT associated with A-80."
FT /evidence="ECO:0000269|PubMed:16860747"
FT CONFLICT 9
FT /note="A -> P (in Ref. 3; CAB66512)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="R -> G (in Ref. 4; AAH57231)"
FT /evidence="ECO:0000305"
FT HELIX 63..79
FT /evidence="ECO:0007829|PDB:2L5Y"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2L5Y"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:2L5Y"
FT TURN 97..103
FT /evidence="ECO:0007829|PDB:2L5Y"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:2L5Y"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2L5Y"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:2L5Y"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:2L5Y"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:2L5Y"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:2L5Y"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2L5Y"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:2L5Y"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:2L5Y"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:2L5Y"
FT HELIX 188..204
FT /evidence="ECO:0007829|PDB:2L5Y"
SQ SEQUENCE 746 AA; 83971 MW; B83855557F126254 CRC64;
MLVLGLLVAG AADGCELVPR HLRGRRATGS AATAASSPAA AAGDSPALMT DPCMSLSPPC
FTEEDRFSLE ALQTIHKQMD DDKDGGIEVE ESDEFIREDM KYKDATNKHS HLHREDKHIT
IEDLWKRWKT SEVHNWTLED TLQWLIEFVE LPQYEKNFRD NNVKGTTLPR IAVHEPSFMI
SQLKISDRSH RQKLQLKALD VVLFGPLTRP PHNWMKDFIL TVSIVIGVGG CWFAYTQNKT
SKEHVAKMMK DLESLQTAEQ SLMDLQERLE KAQEENRNVA VEKQNLERKM MDEINYAKEE
ACRLRELREG AECELSRRQY AEQELEQVRM ALKKAEKEFE LRSSWSVPDA LQKWLQLTHE
VEVQYYNIKR QNAEMQLAIA KDEAEKIKKK RSTVFGTLHV AHSSSLDEVD HKILEAKKAL
SELTTCLRER LFRWQQIEKI CGFQIAHNSG LPSLTSSLYS DHSWVVMPRV SIPPYPIAGG
VDDLDEDTPP IVSQFPGTMA KPPGSLARSS SLCRSRRSIV PSSPQPQRAQ LAPHAPHPSH
PRHPHHPQHT PHSLPSPDPD ILSVSSCPAL YRNEEEEEAI YFSAEKQWEV PDTASECDSL
NSSIGRKQSP PLSLEIYQTL SPRKISRDEV SLEDSSRGDS PVTVDVSWGS PDCVGLTETK
SMIFSPASKV YNGILEKSCS MNQLSSGIPV PKPRHTSCSS AGNDSKPVQE APSVARISSI
PHDLCHNGEK SKKPSKIKSL FKKKSK
