STIM1_RAT
ID STIM1_RAT Reviewed; 685 AA.
AC P84903;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Stromal interaction molecule 1;
DE Flags: Precursor;
GN Name=Stim1 {ECO:0000312|RGD:1306831};
GN Synonyms=Sim {ECO:0000250|UniProtKB:Q13586};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-76; ASP-78 AND
RP GLU-87.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-512; SER-519;
RP SER-521; SER-567; SER-575; SER-660 AND SER-668, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By
CC similarity). Acts as Ca(2+) sensor in the endoplasmic reticulum via its
CC EF-hand domain. Upon Ca(2+) depletion, translocates from the
CC endoplasmic reticulum to the plasma membrane where it activates the
CC Ca(2+) release-activated Ca(2+) (CRAC) channel subunit ORAI1
CC (PubMed:16208375). Involved in enamel formation (By similarity).
CC Activated following interaction with STIMATE, leading to promote STIM1
CC conformational switch (By similarity). {ECO:0000250|UniProtKB:Q13586,
CC ECO:0000269|PubMed:16208375}.
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 (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 TMEM203. Interacts with STIMATE, promoting STIM1 conformational switch
CC (By similarity). Interacts with TMEM178A (By similarity). Interacts
CC with CASQ1 (via C-terminal end and preferentially with the monomeric
CC form); this interaction increases in response to a depletion of
CC intracellular Ca(2+), decreases both STIM1 aggregation and clustering,
CC interaction of STIM1 with ORAI1 and store-operated Ca(2+) entry (SOCE)
CC activity (By similarity). Interacts with ADCY8 (By similarity).
CC {ECO:0000250|UniProtKB:P70302, ECO:0000250|UniProtKB:Q13586}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16208375};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:16208375}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:16208375}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:16208375}.
CC Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q13586}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:16208375}. Note=Translocates from the
CC endoplasmic reticulum to the cell membrane in response to a depletion
CC of 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q13586}.
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 STIM1 Orai1-activating region/CRAC-activating domain
CC (SOAR/CAD) mediates interaction with ORAI1 to activate the channel.
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; AABR03000423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03002698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001101966.2; NM_001108496.2.
DR AlphaFoldDB; P84903; -.
DR SMR; P84903; -.
DR CORUM; P84903; -.
DR IntAct; P84903; 1.
DR STRING; 10116.ENSRNOP00000027685; -.
DR BindingDB; P84903; -.
DR ChEMBL; CHEMBL3832645; -.
DR GlyGen; P84903; 2 sites.
DR iPTMnet; P84903; -.
DR PhosphoSitePlus; P84903; -.
DR jPOST; P84903; -.
DR PaxDb; P84903; -.
DR PRIDE; P84903; -.
DR GeneID; 361618; -.
DR KEGG; rno:361618; -.
DR UCSC; RGD:1306831; rat.
DR CTD; 6786; -.
DR RGD; 1306831; Stim1.
DR VEuPathDB; HostDB:ENSRNOG00000020425; -.
DR eggNOG; KOG4403; Eukaryota.
DR HOGENOM; CLU_010588_0_0_1; -.
DR InParanoid; P84903; -.
DR OrthoDB; 373308at2759; -.
DR PhylomeDB; P84903; -.
DR TreeFam; TF313487; -.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR Reactome; R-RNO-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR PRO; PR:P84903; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020425; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; P84903; baseline and differential.
DR Genevisible; P84903; RN.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0044853; C:plasma membrane raft; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005246; F:calcium channel regulator activity; IMP:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0015279; F:store-operated calcium channel activity; IMP:RGD.
DR GO; GO:0032237; P:activation of store-operated calcium channel activity; IMP:RGD.
DR GO; GO:0006812; P:cation transport; ISO:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0005513; P:detection of calcium ion; ISS:UniProtKB.
DR GO; GO:0070166; P:enamel mineralization; ISS:UniProtKB.
DR GO; GO:0014902; P:myotube differentiation; ISO:RGD.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISS:UniProtKB.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; IMP:RGD.
DR GO; GO:0002115; P:store-operated calcium entry; IDA:RGD.
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 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 /evidence="ECO:0000255"
FT /id="PRO_0000248270"
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 /evidence="ECO:0000255"
FT DOMAIN 132..190
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 334..444
FT /note="SOAR/CAD"
FT /evidence="ECO:0000250"
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:0000250"
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:0000250"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:22673903"
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:22673903"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
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:22673903"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:22673903"
FT MOD_RES 665
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 76
FT /note="D->A: Increases Ca(2+) influx through activation of
FT CRAC channels, even when Ca(2+) stores are not depleted."
FT /evidence="ECO:0000269|PubMed:16208375"
FT MUTAGEN 78
FT /note="D->A: Increases Ca(2+) influx through activation of
FT CRAC channels, even when Ca(2+) stores are not depleted."
FT /evidence="ECO:0000269|PubMed:16208375"
FT MUTAGEN 87
FT /note="E->Q: Increases Ca(2+) influx through activation of
FT CRAC channels, even when Ca(2+) stores are not depleted."
FT /evidence="ECO:0000269|PubMed:16208375"
SQ SEQUENCE 685 AA; 77449 MW; FD2DA28427D2E41E CRC64;
MDVCARLALW LLWGLLLHQG QSLSHSHSEK NTGASSGATS EESTEAEFCR IDKPLCHSED
EKLSFEAVRN IHKLMDDDAN GDVDVEESDE FLREDLNYHD PTVKHSTFHG EDKLISVEDL
WKAWKASEVY 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 QRLTEPQHGL GSQRDLTHSD SESSLHTSDR QRVAPKPPQM
GRAADEALNA TSSNGSHRLI EGVHPGSLVE KLPDSPALAK KTILALNHGL DKAHSLMELN
PSVPPGGSPL LDSSHSHSPS SPDPDTPSPV GDSRALQGSR NTRIPHLAGK KAMAEEDNGS
IGEETDSSPG RKKFPLKIFK KPLKK
