ID   STIM1_MOUSE             Reviewed;         685 AA.
AC   P70302; Q8K1E1;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   02-SEP-2026, entry version 196.
DE   RecName: Full=Stromal interaction molecule 1;
DE   Flags: Precursor;
GN   Name=Stim1; Synonyms=Sim;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6 X DBA/2; TISSUE=Bone marrow stroma;
RX   PubMed=8707854; DOI=10.1083/jcb.134.3.771;
RA   Oritani K., Kincade P.W.;
RT   "Identification of stromal cell products that interact with pre-B cells.";
RL   J. Cell Biol. 134:771-782(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-504; SER-512 AND SER-575, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; THR-504; SER-512;
RP   SER-519; SER-521; SER-524; SER-567; SER-575; SER-660; THR-665 AND SER-668,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   TISSUE SPECIFICITY.
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   [9]
RP   INTERACTION WITH TMEM178A.
RX   PubMed=26644563; DOI=10.1073/pnas.1511285112;
RA   Decker C.E., Yang Z., Rimer R., Park-Min K.H., Macaubas C., Mellins E.D.,
RA   Novack D.V., Faccio R.;
RT   "Tmem178 acts in a novel negative feedback loop targeting NFATc1 to
RT   regulate bone mass.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:15654-15659(2015).
RN   [10]
RP   INTERACTION WITH TMEM203.
RX   PubMed=31346090; DOI=10.1073/pnas.1901090116;
RA   Li Y., James S.J., Wyllie D.H., Wynne C., Czibula A., Bukhari A., Pye K.,
RA   Bte Mustafah S.M., Fajka-Boja R., Szabo E., Angyal A., Hegedus Z.,
RA   Kovacs L., Hill A.V.S., Jefferies C.A., Wilson H.L., Yongliang Z.,
RA   Kiss-Toth E.;
RT   "TMEM203 is a binding partner and regulator of STING-mediated inflammatory
RT   signaling in macrophages.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:16479-16488(2019).
CC   -!- FUNCTION: Acts as a Ca(2+) sensor that gates two major inward
CC       rectifying Ca(2+) channels at the plasma membrane: Ca(2+) release-
CC       activated Ca(2+) (CRAC) channels and arachidonate-regulated Ca(2+)-
CC       selective (ARC) channels. Plays a role in mediating store-operated
CC       Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of
CC       intracellular Ca(2+) stores. Upon Ca(2+) depletion, translocates from
CC       the endoplasmic reticulum to the plasma membrane where it activates
CC       CRAC channel pore-forming subunits ORA1, ORA2 and ORAI3 to generate
CC       sustained and oscillatory Ca(2+) entry. Involved in enamel formation.
CC       Plays a role in regulating the type I interferon response by retaining
CC       the signaling adapter STING at the endoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:Q13586}.
CC   -!- SUBUNIT: Monomer in the presence of Ca(2+). It oligomerizes in absence
CC       of Ca(2+). Forms homooligomers and heterooligomers with STIM2.
CC       Interacts with pore-forming subunits of CRAC channels, ORAI1, ORAI2 and
CC       ORAI3; this interaction is potentiated upon Ca(2+) store depletion.
CC       Interacts (via the transmembrane region and the SOAR/CAD domain) with
CC       SPPL3; the interaction promotes the binding of STIM1 to ORAI1.
CC       Interacts with ORAI1. Interacts with MAPRE1; probably required for
CC       targeting to the growing microtubule plus ends. Interacts with
CC       CRACR2A/EFCAB4B; the interaction is direct and takes place in absence
CC       of Ca(2+). Forms a complex with CRACR2A/EFCAB4B and ORAI1 at low
CC       concentration of Ca(2+), the complex dissociates at elevated Ca(2+)
CC       concentrations. Interacts with SARAF, promoting a slow inactivation of
CC       STIM1-dependent SOCE activity, possibly by facilitating the
CC       deoligomerization of STIM1 (By similarity). Interacts with EFHB; the
CC       interaction takes place upon Ca(2+)-store depletion and inhibits the
CC       association with SARAF (By similarity). Interacts with ASPH. Interacts
CC       with SLC35G1; intracellular Ca(2+)-dependent. May interact with ATP1A1,
CC       ATP2A2, ATP2B1, ATP2B4, KPNB1 and XPO1; through SLC35G1. Interacts with
CC       STIMATE, promoting STIM1 conformational switch (By similarity).
CC       Interacts with TMEM178A (PubMed:26644563). Interacts with CASQ1 (via C-
CC       terminal end and preferentially with the monomeric form); this
CC       interaction increases in response to a depletion of intracellular
CC       Ca(2+), decreases both STIM1 aggregation and clustering, interaction of
CC       STIM1 with ORAI1 and store-operated Ca(2+) entry (SOCE) activity (By
CC       similarity). Interacts with ADCY8 (By similarity). Interacts with
CC       TMEM203 (PubMed:31346090). Interacts with STING1; this interaction
CC       retains STING1 in the endoplasmic reticulum membrane (By similarity).
CC       {ECO:0000250|UniProtKB:Q13586, ECO:0000269|PubMed:26644563,
CC       ECO:0000269|PubMed:31346090}.
CC   -!- INTERACTION:
CC       P70302; P70302: Stim1; NbExp=2; IntAct=EBI-8402335, EBI-8402335;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13586};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13586}.
CC       Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q13586}; Single-
CC       pass type I membrane protein {ECO:0000250|UniProtKB:Q13586}. Cytoplasm,
CC       cytoskeleton {ECO:0000250|UniProtKB:Q13586}. Sarcoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q13586}. 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       Associated with the microtubule network at the growing distal tip of
CC       microtubules. Colocalizes with ORAI1 at the cell membrane. Colocalizes
CC       preferentially with CASQ1 at endoplasmic reticulum in response to a
CC       depletion of intracellular calcium. {ECO:0000250|UniProtKB:Q13586}.
CC   -!- TISSUE SPECIFICITY: Expressed in maturation-stage ameloblasts (at
CC       protein level). Expressed in all tissues examined and in many cell
CC       types, including bone marrow stroma, fibroblast, B-cell precursors,
CC       lymphoma and erythroleukemia. {ECO:0000269|PubMed:24621671,
CC       ECO:0000269|PubMed:8707854}.
CC   -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates
CC       interaction with MAPRE1 and targeting to the growing microtubule plus
CC       ends. {ECO:0000250|UniProtKB:Q13586}.
CC   -!- DOMAIN: The EF-hand domain is responsible for Ca(2+) sensitivity. It
CC       consists of a canonical helix-loop-helix EF motif (alpha1beta1alpha2;
CC       EF-hand 1) paired to a second helix-loop-helix EF motif
CC       (alpha3beta2alpha4; EF-hand 2). EF-hand 1 binds Ca(2+) whereas EF-hand
CC       2 mediates the interactions with SAM domain.
CC       {ECO:0000250|UniProtKB:Q13586}.
CC   -!- DOMAIN: The sterile alpha motif (SAM) domain folds into a
CC       characteristic 5-helix bundle (alpha6-alpha10) which interacts with the
CC       EF-hand pairs enabling concerted folding and stability of EF-hand and
CC       SAM domains. {ECO:0000250|UniProtKB:Q13586}.
CC   -!- DOMAIN: The STIM1 Orai-activating region/CRAC-activating domain
CC       (SOAR/CAD) directly interacts with ORAI1 subunits and mediates CRAC
CC       channel gating. {ECO:0000250|UniProtKB:Q13586}.
CC   -!- DOMAIN: The polybasic Lys-rich region (residues 672-685) functionally
CC       interacts with the Pro-rich region of ORAI1 (residues 3-47) and
CC       regulates CRAC channel gating at negative membrane potentials.
CC       {ECO:0000250|UniProtKB:Q13586}.
CC   -!- PTM: Glycosylation is required for cell surface expression.
CC       {ECO:0000250|UniProtKB:Q13586}.
CC   -!- PTM: Phosphorylated predominantly on Ser residues.
CC       {ECO:0000250|UniProtKB:Q13586}.
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DR   EMBL; U47323; AAC52715.1; -; mRNA.
DR   EMBL; AK041944; BAC31106.1; -; mRNA.
DR   EMBL; CH466531; EDL16597.1; -; Genomic_DNA.
DR   EMBL; BC021644; AAH21644.1; -; mRNA.
DR   CCDS; CCDS21530.1; -.
DR   RefSeq; NP_033313.2; NM_009287.5.
DR   AlphaFoldDB; P70302; -.
DR   SMR; P70302; -.
DR   BioGRID; 203538; 14.
DR   DIP; DIP-48770N; -.
DR   FunCoup; P70302; 2082.
DR   IntAct; P70302; 1.
DR   STRING; 10090.ENSMUSP00000033289; -.
DR   ChEMBL; CHEMBL4296085; -.
DR   GlyConnect; P70302; 4 N-Linked glycans (1 site).
DR   GlyCosmos; P70302; 2 sites, 4 glycans.
DR   GlyGen; P70302; 8 sites, 7 N-linked glycans (3 sites), 1 O-linked glycan (4 sites).
DR   iPTMnet; P70302; -.
DR   PhosphoSitePlus; P70302; -.
DR   SwissPalm; P70302; -.
DR   jPOST; P70302; -.
DR   PaxDb; 10090-ENSMUSP00000033289; -.
DR   PeptideAtlas; P70302; -.
DR   ProteomicsDB; 257091; -.
DR   Pumba; P70302; -.
DR   Antibodypedia; 2591; 562 antibodies from 47 providers.
DR   DNASU; 20866; -.
DR   Ensembl; ENSMUST00000033289.6; ENSMUSP00000033289.5; ENSMUSG00000030987.6.
DR   GeneID; 20866; -.
DR   KEGG; mmu:20866; -.
DR   UCSC; uc009irm.1; mouse.
DR   AGR; MGI:107476; -.
DR   CTD; 6786; -.
DR   MGI; MGI:107476; Stim1.
DR   VEuPathDB; HostDB:ENSMUSG00000030987; -.
DR   eggNOG; KOG4403; Eukaryota.
DR   GeneTree; ENSGT00390000000214; -.
DR   HOGENOM; CLU_010588_0_0_1; -.
DR   InParanoid; P70302; -.
DR   OMA; FLCCVLK; -.
DR   PhylomeDB; P70302; -.
DR   Reactome; R-MMU-5578775; Ion homeostasis.
DR   Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   BioGRID-ORCS; 20866; 4 hits in 79 CRISPR screens.
DR   PRO; PR:P70302; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P70302; protein.
DR   Bgee; ENSMUSG00000030987; Expressed in extra-ocular muscle and 229 other cell types or tissues.
DR   ExpressionAtlas; P70302; baseline and differential.
DR   GO; GO:0032541; C:cortical endoplasmic reticulum; ISO:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0030426; C:growth cone; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0044853; C:plasma membrane raft; ISS:UniProtKB.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0005246; F:calcium channel regulator activity; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0099103; F:channel activator activity; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR   GO; GO:0002020; F:protease binding; ISO:GO_Central.
DR   GO; GO:0015279; F:store-operated calcium channel activity; ISO:GO_Central.
DR   GO; GO:0032237; P:activation of store-operated calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0005513; P:detection of calcium ion; ISS:UniProtKB.
DR   GO; GO:0070166; P:enamel mineralization; ISS:UniProtKB.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006812; P:monoatomic cation transport; IMP:MGI.
DR   GO; GO:0014902; P:myotube differentiation; IMP:MGI.
DR   GO; GO:0007207; P:phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway; IDA:MGI.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:GO_Central.
DR   GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISS:UniProtKB.
DR   GO; GO:2001256; P:regulation of store-operated calcium entry; ISS:UniProtKB.
DR   GO; GO:0002115; P:store-operated calcium entry; IMP:MGI.
DR   CDD; cd09573; SAM_STIM1; 1.
DR   CDD; cd11722; SOAR; 1.
DR   FunFam; 1.10.150.50:FF:000009; Stromal interaction molecule 1; 1.
DR   FunFam; 1.10.238.180:FF:000001; Stromal interaction molecule 1; 1.
DR   FunFam; 1.10.287.3550:FF:000001; Stromal interaction molecule 1; 1.
DR   FunFam; 1.20.5.340:FF:000011; Stromal interaction molecule 1; 1.
DR   Gene3D; 1.10.238.180; -; 1.
DR   Gene3D; 1.10.287.3550; -; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR057835; EF-hand_STIM1/2.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR032393; SOAR_STIM1/2.
DR   InterPro; IPR037608; STIM1/2.
DR   InterPro; IPR037609; STIM1_SAM.
DR   PANTHER; PTHR15136:SF9; STROMAL INTERACTION MOLECULE 1; 1.
DR   PANTHER; PTHR15136; STROMAL INTERACTION MOLECULE HOMOLOG; 1.
DR   Pfam; PF25578; EF-hand_STIM1; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   Pfam; PF16533; SOAR; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Calcium; Calcium transport; Cell membrane; Coiled coil; Cytoplasm;
KW   Cytoskeleton; 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_0000033327"
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          64..97
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   DOMAIN          102..126
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   DOMAIN          132..200
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          24..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..442
FT                   /note="SOAR/CAD"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   REGION          475..483
FT                   /note="Contributes to fast Ca(2+)-dependent inactivation of
FT                   CRAC channels"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   REGION          490..541
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   REGION          672..685
FT                   /note="Required for generation of inwardly rectifying CRAC
FT                   currents"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   COILED          248..442
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   MOTIF           642..645
FT                   /note="Microtubule tip localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   COMPBIAS        32..41
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..499
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..620
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..666
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..685
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         76
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   BINDING         78
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   BINDING         80
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   BINDING         82
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   BINDING         87
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   MOD_RES         257
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17208939,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         504
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         512
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         517
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   MOD_RES         519
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         521
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         523
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   MOD_RES         524
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         567
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         575
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         602
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   MOD_RES         608
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   MOD_RES         618
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   MOD_RES         621
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   MOD_RES         628
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   MOD_RES         660
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         665
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         668
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13586"
FT   CONFLICT        331
FT                   /note="A -> S (in Ref. 1; AAC52715)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   685 AA;  77567 MW;  F4DADF67436790FD CRC64;
     MDVCARLALW LLWGLLLHQG QSLSHSHSEK NTGASSGATS EESTEAEFCR IDKPLCHSED
     EKLSFEAVRN IHKLMDDDAN GDVDVEESDE FLREDLNYHD PTVKHSTFHG EDKLISVEDL
     WKAWKSSEVY NWTVDEVIQW LITYVELPQY EETFRKLQLT GHAMPRLAVT NTTMTGTVLK
     MTDRSHRQKL QLKALDTVLF GPPLLTRHNH LKDFMLVVSI VIGVGGCWFA YIQNRYSKEH
     MKKMMKDLEG LHRAEQSLHD LQERLHKAQE EHRTVEVEKV HLEKKLRDEI NLAKQEAQRL
     KELREGTENE RSRQKYAEEE LEQVREALRK AEKELESHSS WYAPEALQKW LQLTHEVEVQ
     YYNIKKQNAE RQLLVAKEGA EKIKKKRNTL FGTFHVAHSS SLDDVDHKIL TAKQALSEVT
     AALRERLHRW QQIEILCGFQ IVNNPGIHSL VAALNIDPSW MGSTRPNPAH FIMTDDVDDM
     DEEIVSPLSM QSPSLQSSVR QRLTEPQLGL GSQRDLTHSD SESSLHMSDR QRVAPKPPQM
     GRAADEALNA MPSNGSHRLI EGVHPGSLVE KLPDSPALAK KTFMALNHGL DKAHSLMELN
     PSVPPGGSPL LDSSHSLSPS SPDPDTPSPV GDNRALQGSR NTRIPHLAGK KAMAEEDNGS
     IGEETDSSPG RKKFPLKIFK KPLKK
//