STIM1_CAEEL
ID STIM1_CAEEL Reviewed; 530 AA.
AC G5EF60; H2L0R4; H2L0R5;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Stromal interaction molecule 1 {ECO:0000303|PubMed:16966474};
DE Flags: Precursor;
GN Name=stim-1 {ECO:0000312|EMBL:CCD73857.1, ECO:0000312|WormBase:Y55B1BM.1a};
GN ORFNames=Y55B1BM.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABG89384.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-55 AND
RP ASP-57.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:ABG89384.1};
RX PubMed=16966474; DOI=10.1085/jgp.200609611;
RA Yan X., Xing J., Lorin-Nebel C., Estevez A.Y., Nehrke K., Lamitina T.,
RA Strange K.;
RT "Function of a STIM1 homologue in C. elegans: evidence that store-operated
RT Ca2+ entry is not essential for oscillatory Ca2+ signaling and ER Ca2+
RT homeostasis.";
RL J. Gen. Physiol. 128:443-459(2006).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CCD73857.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD73857.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP ORAI-1.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:17218360};
RX PubMed=17218360; DOI=10.1113/jphysiol.2006.124883;
RA Lorin-Nebel C., Xing J., Yan X., Strange K.;
RT "CRAC channel activity in C. elegans is mediated by Orai1 and STIM1
RT homologues and is essential for ovulation and fertility.";
RL J. Physiol. (Lond.) 580:67-85(2007).
RN [4] {ECO:0000305, ECO:0000312|PDB:3TER}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 256-391, AND SUBUNIT.
RX PubMed=22451904; DOI=10.1073/pnas.1118947109;
RA Yang X., Jin H., Cai X., Li S., Shen Y.;
RT "Structural and mechanistic insights into the activation of Stromal
RT interaction molecule 1 (STIM1).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5657-5662(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.
CC Acts as Ca(2+) sensor which upon Ca(2+) depletion, activates the Ca(2+)
CC release-activated Ca(2+) (CRAC) channel subunit, orai-1. Essential for
CC Ca (2+) and IP3-dependent contractile activity of gonad sheath cells
CC and spermatheca. Essential for fertility. Does not play a role in
CC posterior body wall muscle contraction (pBoc) rhythmicity, intestinal
CC cell oscillatory Ca(2+) signaling or intestinal ER Ca(2+) hemostasis.
CC {ECO:0000269|PubMed:16966474, ECO:0000269|PubMed:17218360}.
CC -!- SUBUNIT: Homodimer. Interacts with orai-1.
CC {ECO:0000269|PubMed:17218360, ECO:0000269|PubMed:22451904}.
CC -!- INTERACTION:
CC G5EF60; G5EF60: stim-1; NbExp=2; IntAct=EBI-15975920, EBI-15975920;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16966474,
CC ECO:0000269|PubMed:17218360}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16966474, ECO:0000269|PubMed:17218360}.
CC Note=Localizes to intracellular puncta in the anterior intestine and
CC reticular structure in the posterior intestine.
CC {ECO:0000269|PubMed:16966474, ECO:0000269|PubMed:17218360}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000269|PubMed:16966474};
CC IsoId=G5EF60-1; Sequence=Displayed;
CC Name=b {ECO:0000305};
CC IsoId=G5EF60-2; Sequence=VSP_046320;
CC Name=c {ECO:0000305};
CC IsoId=G5EF60-3; Sequence=VSP_046321, VSP_046322;
CC -!- TISSUE SPECIFICITY: Coexpressed with orai-1 in spermatheca, gonad
CC sheath cells and intestine. Also detected in neurons in the head and in
CC the uterine epithelial cells. Heterogeneously expressed in the
CC intestine with strong presence in the anterior and posterior intestine
CC and weaker in the midsection. {ECO:0000269|PubMed:16966474,
CC ECO:0000269|PubMed:17218360}.
CC -!- DISRUPTION PHENOTYPE: Sterility due to dysfunction of somatic cells.
CC Affects the store-operated Ca(2+) (SOC) activity.
CC {ECO:0000269|PubMed:16966474}.
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DR EMBL; DQ812088; ABG89384.1; -; mRNA.
DR EMBL; FO081812; CCD73857.1; -; Genomic_DNA.
DR EMBL; FO081812; CCD73858.1; -; Genomic_DNA.
DR EMBL; FO081812; CCD73859.1; -; Genomic_DNA.
DR RefSeq; NP_001022916.1; NM_001027745.3. [G5EF60-3]
DR RefSeq; NP_741073.1; NM_171065.4. [G5EF60-2]
DR RefSeq; NP_741074.1; NM_171858.4. [G5EF60-1]
DR PDB; 3TER; X-ray; 2.55 A; A/B=256-391.
DR PDB; 6PW7; X-ray; 1.89 A; A/B=25-185.
DR PDBsum; 3TER; -.
DR PDBsum; 6PW7; -.
DR AlphaFoldDB; G5EF60; -.
DR SMR; G5EF60; -.
DR BioGRID; 40475; 3.
DR DIP; DIP-60032N; -.
DR STRING; 6239.Y55B1BM.1a; -.
DR EPD; G5EF60; -.
DR PaxDb; G5EF60; -.
DR PeptideAtlas; G5EF60; -.
DR EnsemblMetazoa; Y55B1BM.1a.1; Y55B1BM.1a.1; WBGene00021910. [G5EF60-1]
DR EnsemblMetazoa; Y55B1BM.1b.1; Y55B1BM.1b.1; WBGene00021910. [G5EF60-2]
DR EnsemblMetazoa; Y55B1BM.1c.1; Y55B1BM.1c.1; WBGene00021910. [G5EF60-3]
DR GeneID; 175201; -.
DR KEGG; cel:CELE_Y55B1BM.1; -.
DR CTD; 175201; -.
DR WormBase; Y55B1BM.1a; CE29124; WBGene00021910; stim-1. [G5EF60-1]
DR WormBase; Y55B1BM.1b; CE30055; WBGene00021910; stim-1. [G5EF60-2]
DR WormBase; Y55B1BM.1c; CE34130; WBGene00021910; stim-1. [G5EF60-3]
DR eggNOG; KOG4403; Eukaryota.
DR GeneTree; ENSGT00390000000214; -.
DR InParanoid; G5EF60; -.
DR OMA; RRENKFH; -.
DR OrthoDB; 719915at2759; -.
DR PhylomeDB; G5EF60; -.
DR Reactome; R-CEL-5578775; Ion homeostasis.
DR Reactome; R-CEL-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR PRO; PR:G5EF60; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00021910; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005246; F:calcium channel regulator activity; IDA:WormBase.
DR GO; GO:0005509; F:calcium ion binding; ISS:WormBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0032237; P:activation of store-operated calcium channel activity; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0030728; P:ovulation; IMP:WormBase.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:WormBase.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IMP:WormBase.
DR GO; GO:1901341; P:positive regulation of store-operated calcium channel activity; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0002115; P:store-operated calcium entry; IGI:WormBase.
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 SUPFAM; SSF47769; SSF47769; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Coiled coil; Ion channel; Ion transport; Membrane;
KW Metal-binding; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..530
FT /note="Stromal interaction molecule 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422046"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 42..77
FT /note="EF-hand"
FT /evidence="ECO:0000255"
FT DOMAIN 113..181
FT /note="SAM"
FT /evidence="ECO:0000255"
FT REGION 409..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 208..329
FT /evidence="ECO:0000255"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT VAR_SEQ 391..410
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_046320"
FT VAR_SEQ 391..395
FT /note="ETEHI -> GKFRQ (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_046321"
FT VAR_SEQ 396..530
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_046322"
FT MUTAGEN 55
FT /note="D->A: Sterility along with defects in ovulation,
FT slow growth and stunted gonad development; pBoc arrhythmia
FT and fluid accumulation in the pseudocoel; when associated
FT with A-57."
FT /evidence="ECO:0000269|PubMed:16966474"
FT MUTAGEN 57
FT /note="D->A: Sterility along with defects in ovulation,
FT slow growth and stunted gonad development; pBoc arrhythmia
FT and fluid accumulation in the pseudocoel; when associated
FT with A-55."
FT /evidence="ECO:0000269|PubMed:16966474"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:6PW7"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:6PW7"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:6PW7"
FT HELIX 260..277
FT /evidence="ECO:0007829|PDB:3TER"
FT HELIX 290..328
FT /evidence="ECO:0007829|PDB:3TER"
FT HELIX 346..382
FT /evidence="ECO:0007829|PDB:3TER"
SQ SEQUENCE 530 AA; 60021 MW; AEF628FA03BFDB3C CRC64;
MGRVSWIIAL YLTINVVIVV NGDRVTRNVE VTAEEEKIRD KLGYEAIRDI HRDMDDDHSG
SIDRNESTGF MKEDMQMRGS ERTRRENKFH GDDDAITVDD LWEAWFESIE RTWTNERLVE
WLINDVNLPS IVEAVKAKKI DGKILPRFAS PNSDFLNKEL GIKSSVYRQK LRLNSLDVVL
FGYKDNNNRT KDILLAFLAL LLTSLIFLYV RQKQKAQQKV NELSNKLTEL KCMETEFEDV
QKMLNDERSK RSISDGVVNH TEMENLRVQL EEAERRLEAN SNGSQAPLAL QPLLRRTCEN
EMAFLEKQRQ DCFKEMKEAI EMVDRLQKKQ GSVLSSLKLA TGAASTSDQV DSKIFALKSR
MEKIHTLTRE TQERWLQIES LCGFPLLYLN ETEHINRSIA SSHFYNKSHE GSSSSGSISN
AHSNPNAVNS NFVKKVSPPI PPSQQTANLR FVPTEQSDSI HSEDTSPIVE DVAISRSLTQ
DLAEADMQSI VSGSTNGSGS VAALKKRKGI FPKLFRRNTS KSSSLGGTSN
