STIM2_MOUSE
ID STIM2_MOUSE Reviewed; 746 AA.
AC P83093; Q69ZI3; Q80VF4;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Stromal interaction molecule 2;
DE Flags: Precursor;
GN Name=Stim2; Synonyms=Kiaa1482;
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 [LARGE SCALE MRNA].
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 82-227.
RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 374-746.
RC TISSUE=Mammary 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
RP 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-640 AND SER-650, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomer with STIM1. Interacts with ORAI1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Note=Dynamically
CC translocates from a uniform endoplasmic reticulum distribution to
CC punctual endoplasmic reticulum-plasma membrane junctions in response to
CC decrease in endoplasmic reticulum Ca(2+) concentration. {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated predominantly on Ser residues. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32461.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173183; BAD32461.1; ALT_INIT; mRNA.
DR EMBL; AF328907; AAK82339.1; -; mRNA.
DR EMBL; BC043455; AAH43455.1; -; mRNA.
DR CCDS; CCDS39089.2; -.
DR RefSeq; NP_001074572.2; NM_001081103.2.
DR AlphaFoldDB; P83093; -.
DR BMRB; P83093; -.
DR SMR; P83093; -.
DR BioGRID; 228048; 5.
DR STRING; 10090.ENSMUSP00000113174; -.
DR ChEMBL; CHEMBL4296085; -.
DR GlyGen; P83093; 1 site.
DR iPTMnet; P83093; -.
DR PhosphoSitePlus; P83093; -.
DR SwissPalm; P83093; -.
DR EPD; P83093; -.
DR jPOST; P83093; -.
DR MaxQB; P83093; -.
DR PaxDb; P83093; -.
DR PRIDE; P83093; -.
DR ProteomicsDB; 257491; -.
DR Antibodypedia; 10303; 284 antibodies from 36 providers.
DR DNASU; 116873; -.
DR Ensembl; ENSMUST00000117661; ENSMUSP00000113174; ENSMUSG00000039156.
DR GeneID; 116873; -.
DR KEGG; mmu:116873; -.
DR UCSC; uc008xlq.2; mouse.
DR CTD; 57620; -.
DR MGI; MGI:2151156; Stim2.
DR VEuPathDB; HostDB:ENSMUSG00000039156; -.
DR eggNOG; KOG4403; Eukaryota.
DR GeneTree; ENSGT00390000000214; -.
DR HOGENOM; CLU_010588_2_0_1; -.
DR InParanoid; P83093; -.
DR OMA; ISDPCMS; -.
DR OrthoDB; 373308at2759; -.
DR PhylomeDB; P83093; -.
DR TreeFam; TF313487; -.
DR BioGRID-ORCS; 116873; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Stim2; mouse.
DR PRO; PR:P83093; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P83093; protein.
DR Bgee; ENSMUSG00000039156; Expressed in vestibular membrane of cochlear duct and 224 other tissues.
DR ExpressionAtlas; P83093; baseline and differential.
DR Genevisible; P83093; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005246; F:calcium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0015279; F:store-operated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0032237; P:activation of store-operated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISS: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 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; Coiled coil; 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:0000255"
FT CHAIN 15..746
FT /note="Stromal interaction molecule 2"
FT /id="PRO_0000218282"
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 490..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..394
FT /evidence="ECO:0000255"
FT COMPBIAS 504..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..720
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:0000250"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P246"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P246"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P246"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P246"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P246"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P246"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 746 AA; 83925 MW; EE48455117B4E0BD CRC64;
MLLFGLLVAG VADGCDLVPR HLRGRRASGS AGAAASPSAA AAGERQALLT DPCMSLSPPC
FTEEDRFSLE ALQTIHKQMD DDKDGGIEVD ESDEFIREDM KYKDATNKHS HLHREDKHIT
VEDLWKQWKT SEVHNWTLED TLQWLIEFVE LPQYEKNFRD NNVKGTTLPR IAVHETSFMI
SQLKISDRSH RQKLQLKALD VVLFGPLTRP PHNWMKDFIL TISIVIGVGG CWFAYTQNKT
SKEHVAKMMK DLESLQTAEQ SLMDLQERLE KAQEENRTVA VEKQNLERKM MDEINYAKEE
ACRLRELREG AECELSRRQY AEQELEQVRM ALKKAEKEFE LRSSWSVPDA LQKWLQLTHE
VEVQYYNIKR QNAEMQLAIA KDEAEKIKKK RSTVFGTLHV AHSSSLDEVD HKILEAKKAL
SELTTCLRER LFRWQQIEKI CGFQIAHNSG LPSLTSSLYS DHSWVVMPRV SIPPYPIAGG
VDDLDEDTPP IVPQFPGTVA KPAGSLARSS SLCRSRRSIV PSSPQSQRAQ LPAHAPLAAH
PRHPHHPQHP QHSLPSPDPD ILSVSSCPAL YRNEEEEEAI YFTAEKQWEV PDTASECDSL
NSSSGRKPSP PSSLEMYQTL SSRKISRDEL SLEDSSRGES PVTADVSRGS PECVGLTETK
SMIFSPASRV YNGILEKSCS MHQLSSGIPV PHPRHTSCSS AGNDSKPVQE ASNVSRVSSI
PHDLCHNGEK SKKPSKIKSL FKKKSK
