STIM_DROME
ID STIM_DROME Reviewed; 570 AA.
AC P83094; Q9VXL6;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Stromal interaction molecule homolog;
DE Flags: Precursor;
GN Name=Stim; ORFNames=CG9126;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
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 [6]
RP MUTAGENESIS OF ASP-155; ASP-157 AND GLU-166.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539 AND SER-546, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Plays a role in mediating Ca(2+) influx following depletion
CC of intracellular Ca(2+) stores. {ECO:0000269|PubMed:15866891}.
CC -!- INTERACTION:
CC P83094; Q9U6B8: Orai; NbExp=4; IntAct=EBI-109721, EBI-118501;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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DR EMBL; AF328906; AAK82338.1; -; mRNA.
DR EMBL; AE014298; AAF48542.2; -; Genomic_DNA.
DR EMBL; AY069686; AAL39831.1; -; mRNA.
DR RefSeq; NP_523357.2; NM_078633.4.
DR AlphaFoldDB; P83094; -.
DR SMR; P83094; -.
DR BioGRID; 58902; 17.
DR DIP; DIP-22915N; -.
DR IntAct; P83094; 16.
DR STRING; 7227.FBpp0073955; -.
DR GlyGen; P83094; 1 site.
DR iPTMnet; P83094; -.
DR PaxDb; P83094; -.
DR PRIDE; P83094; -.
DR DNASU; 32556; -.
DR EnsemblMetazoa; FBtr0074159; FBpp0073955; FBgn0045073.
DR GeneID; 32556; -.
DR KEGG; dme:Dmel_CG9126; -.
DR CTD; 32556; -.
DR FlyBase; FBgn0045073; Stim.
DR VEuPathDB; VectorBase:FBgn0045073; -.
DR eggNOG; KOG4403; Eukaryota.
DR GeneTree; ENSGT00390000000214; -.
DR HOGENOM; CLU_010588_1_0_1; -.
DR InParanoid; P83094; -.
DR OMA; FLCCVLK; -.
DR PhylomeDB; P83094; -.
DR Reactome; R-DME-5578775; Ion homeostasis.
DR Reactome; R-DME-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; P83094; -.
DR BioGRID-ORCS; 32556; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Ranbp16; fly.
DR GenomeRNAi; 32556; -.
DR PRO; PR:P83094; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0045073; Expressed in oviduct (Drosophila) and 40 other tissues.
DR ExpressionAtlas; P83094; baseline and differential.
DR Genevisible; P83094; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048763; F:calcium-induced calcium release activity; IMP:FlyBase.
DR GO; GO:0015279; F:store-operated calcium channel activity; IMP:FlyBase.
DR GO; GO:0032237; P:activation of store-operated calcium channel activity; IMP:FlyBase.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0005513; P:detection of calcium ion; IDA:UniProtKB.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0051924; P:regulation of calcium ion transport; IDA:UniProtKB.
DR GO; GO:0002115; P:store-operated calcium entry; IMP:FlyBase.
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 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; Cell membrane; Coiled coil; Glycoprotein;
KW Ion transport; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..570
FT /note="Stromal interaction molecule homolog"
FT /id="PRO_0000033329"
FT TOPO_DOM 24..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 142..177
FT /note="EF-hand"
FT DOMAIN 213..281
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 40..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 310..407
FT /evidence="ECO:0000255"
FT COILED 420..462
FT /evidence="ECO:0000255"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 155
FT /note="D->A,N: Increases Ca(2+) influx through activation
FT of CRAC channels and arrests cell growth."
FT /evidence="ECO:0000269|PubMed:16208375"
FT MUTAGEN 157
FT /note="D->A,N: Increases Ca(2+) influx through activation
FT of CRAC channels and arrests cell growth."
FT /evidence="ECO:0000269|PubMed:16208375"
FT MUTAGEN 166
FT /note="E->A,Q: Increases Ca(2+) influx through activation
FT of CRAC channels and arrests cell growth."
FT /evidence="ECO:0000269|PubMed:16208375"
SQ SEQUENCE 570 AA; 64797 MW; B8DC7917F379D0B5 CRC64;
MRKNTIWNYS LIFFCCVLKS ISTLDHGPHT VSVDSNRHNT QHQYKQNPNV ASQRHSSHES
GQSLHNSQSE HVTHIAASHA GSGGEHSTHL AQNLHRSSYN LLSEAMSQAV SNEFSSMGSG
SADGACAADD FDCYSGSVQD RFGMEAIASL HRQLDDDDNG NIDLSESDDF LREELKYDSG
YEKRQKAFHF NDDMHISVKE LWEAWLRSEV HNWTIEQTTD WLAQSVQLPQ YVDLFKLHKV
TGAALPRLAV NNLQYVGNVL GIKDPIHKQK ISLKAMDVVL FGPPRETGTR WKDYILVTLL
LSAIIGCWYA YQQNKNAKRH LRRMAQDMEG LQRAEQSLQE MQKELERARM EQENVATEKL
DLERRLKEAP TLSSSNSDLE VQQLKKEIEM LRNELSRAEF ELVDNCWSPP PQLQSWLQYT
YELESKNHQK KRTSAEKQLQ SAREACEKLR KKRSSLVGAF VSTHGKSIDD VDRSIVEARN
ALGDVTNELQ ERLHRWKQIE TCLGLNIVNN NGLPYLENVL YGRNGGLQSS MGMSSTKGSR
ARITNSTEDL DDESIQGKLN FENFSLLATE
