ORAI_CAEEL
ID ORAI_CAEEL Reviewed; 293 AA.
AC Q09232;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein orai;
DE AltName: Full=Store-operated calcium channel;
GN Name=orai-1; ORFNames=C09F5.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17376526; DOI=10.1016/j.ceca.2007.02.007;
RA Strange K., Yan X., Lorin-Nebel C., Xing J.;
RT "Physiological roles of STIM1 and Orai1 homologs and CRAC channels in the
RT genetic model organism Caenorhabditis elegans.";
RL Cell Calcium 42:193-203(2007).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Ca(2+) release-activated Ca(2+)-like (CRAC-like) channel
CC subunit which mediates Ca(2+) influx and increase in Ca(2+)-selective
CC current by synergy with the Ca(2+) sensor, stim-1. Required for Ca(2+)
CC and IP3-dependent contractile activity of sheath cells and the
CC spermatheca. Affects brood size and somatic cell function.
CC {ECO:0000269|PubMed:17218360, ECO:0000269|PubMed:17376526}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in gonad sheath cells, hypodermis,
CC intestine and spermatheca. Coexpressed with stim-1.
CC {ECO:0000269|PubMed:17218360, ECO:0000269|PubMed:17376526}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit an inhibition of intestinal Ca(2+)
CC release activated Ca(2+) channel activity but has no effect on the
CC initiation of posterior body wall muscle contraction, intestinal Ca(2+)
CC oscillations or intestinal ER Ca(2+) store homeostasis. Attenuation
CC also affects sterility and brood size. {ECO:0000269|PubMed:17218360}.
CC -!- SIMILARITY: Belongs to the Orai family. {ECO:0000305}.
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DR EMBL; FO080475; CCD63980.1; -; Genomic_DNA.
DR PIR; T15476; T15476.
DR RefSeq; NP_001254834.1; NM_001267905.1.
DR AlphaFoldDB; Q09232; -.
DR SMR; Q09232; -.
DR BioGRID; 40492; 1.
DR DIP; DIP-25585N; -.
DR IntAct; Q09232; 1.
DR STRING; 6239.C09F5.2a; -.
DR EPD; Q09232; -.
DR PaxDb; Q09232; -.
DR PeptideAtlas; Q09232; -.
DR EnsemblMetazoa; C09F5.2b.1; C09F5.2b.1; WBGene00015648.
DR GeneID; 175221; -.
DR CTD; 175221; -.
DR WormBase; C09F5.2b; CE01774; WBGene00015648; orai-1.
DR eggNOG; KOG4298; Eukaryota.
DR GeneTree; ENSGT00390000015354; -.
DR HOGENOM; CLU_940845_0_0_1; -.
DR InParanoid; Q09232; -.
DR PhylomeDB; Q09232; -.
DR PRO; PR:Q09232; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015648; Expressed in material anatomical entity and 5 other tissues.
DR ExpressionAtlas; Q09232; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IMP:UniProtKB.
DR GO; GO:0015279; F:store-operated calcium channel activity; IDA:WormBase.
DR GO; GO:0045087; P:innate immune response; HEP:WormBase.
DR GO; GO:0030728; P:ovulation; IMP:WormBase.
DR GO; GO:0019953; P:sexual reproduction; IMP:UniProtKB.
DR GO; GO:0002115; P:store-operated calcium entry; IMP:WormBase.
DR Gene3D; 1.20.140.140; -; 1.
DR InterPro; IPR012446; CRAC_channel.
DR InterPro; IPR038350; Orai_sf.
DR PANTHER; PTHR31501; PTHR31501; 1.
DR Pfam; PF07856; Orai-1; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..293
FT /note="Protein orai"
FT /id="PRO_0000065170"
FT TOPO_DOM 1..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..146
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 62..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 293 AA; 32024 MW; 41267F1B729CDD92 CRC64;
MPRSHDPSRV ELLRKEGGLT EKRVSISVED IRGAVANWKN SGGAGDPITP YPLPQFFLQP
PSTAGGGSRN GVGSKEGSVT SLRMPLKKAG DDVDLGHRGE LDLSEKYNYD LSRAQLKASS
RTSALLAGFA MVCLVELQYD QSTPKPLLIV LGVVTSLLVS VHLLALMMST CILPYMEATG
CTQDSPHIKL KFYIDLSWLF STCIGLLLFL VEIGVIFYVK FTAVGYPTAG YITTAMLVPV
GVVFVVFSYL IHKNRVSHSL GRFKHKVDTM KQFLDVEANL QKSTLAPSTI RDI