CRCM1_DROME
ID CRCM1_DROME Reviewed; 351 AA.
AC Q9U6B8; B7YZJ7; Q0E937; Q1HCN1; Q7JQY5; Q7KRH6; Q8IGA6; Q9V892;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Calcium release-activated calcium channel protein 1 {ECO:0000303|PubMed:16751269, ECO:0000312|FlyBase:FBgn0041585};
DE AltName: Full=Protein orai {ECO:0000303|PubMed:16751269, ECO:0000312|FlyBase:FBgn0041585};
GN Name=Orai {ECO:0000303|PubMed:16751269, ECO:0000312|FlyBase:FBgn0041585};
GN Synonyms=CRACM1 {ECO:0000303|PubMed:16645049},
GN olf186-F {ECO:0000303|PubMed:16751269};
GN ORFNames=CG11430 {ECO:0000312|FlyBase:FBgn0041585};
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] (ISOFORM A).
RC TISSUE=Embryo;
RX PubMed=16751269; DOI=10.1073/pnas.0603161103;
RA Zhang S.L., Yeromin A.V., Zhang X.H.-F., Yu Y., Safrina O., Penna A.,
RA Roos J., Stauderman K.A., Cahalan M.D.;
RT "Genome-wide RNAi screen of Ca2+ influx identifies genes that regulate Ca2+
RT release-activated Ca2+ channel activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9357-9362(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Canton-S; TISSUE=Head;
RA Chodagam S., Tickoo S.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND E).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=16582901; DOI=10.1038/nature04702;
RA Feske S., Gwack Y., Prakriya M., Srikanth S., Puppel S.-H., Tanasa B.,
RA Hogan P.G., Lewis R.S., Daly M., Rao A.;
RT "A mutation in Orai1 causes immune deficiency by abrogating CRAC channel
RT function.";
RL Nature 441:179-185(2006).
RN [8]
RP FUNCTION.
RX PubMed=16645049; DOI=10.1126/science.1127883;
RA Vig M., Peinelt C., Beck A., Koomoa D.L., Rabah D., Koblan-Huberson M.,
RA Kraft S., Turner H., Fleig A., Penner R., Kinet J.-P.;
RT "CRACM1 is a plasma membrane protein essential for store-operated Ca2+
RT entry.";
RL Science 312:1220-1223(2006).
CC -!- FUNCTION: Ca(2+) release-activated Ca(2+) (CRAC) channel subunit which
CC mediates Ca(2+) influx following depletion of intracellular Ca(2+)
CC stores. Regulates transcription factor NFAT nuclear import.
CC {ECO:0000269|PubMed:16582901, ECO:0000269|PubMed:16645049}.
CC -!- INTERACTION:
CC Q9U6B8; Q9U6B8: Orai; NbExp=8; IntAct=EBI-118501, EBI-118501;
CC Q9U6B8; P83094: Stim; NbExp=4; IntAct=EBI-118501, EBI-109721;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A {ECO:0000312|FlyBase:FBgn0041585}; Synonyms=B
CC {ECO:0000312|FlyBase:FBgn0041585}, F {ECO:0000312|FlyBase:FBgn0041585};
CC IsoId=Q9U6B8-1; Sequence=Displayed;
CC Name=E {ECO:0000312|FlyBase:FBgn0041585}; Synonyms=G
CC {ECO:0000312|FlyBase:FBgn0041585};
CC IsoId=Q9U6B8-3; Sequence=VSP_018313;
CC Name=C {ECO:0000305};
CC IsoId=Q9U6B8-4; Sequence=VSP_021772, VSP_021773;
CC -!- MISCELLANEOUS: In Greek mythology, the 'Orai' are the keepers of the
CC gates of heaven: Eunomia (order or harmony), Dike (justice) and Eirene
CC (peace).
CC -!- SIMILARITY: Belongs to the Orai family. {ECO:0000305}.
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DR EMBL; DQ503470; ABF54966.1; -; mRNA.
DR EMBL; AF188634; AAF01457.1; -; mRNA.
DR EMBL; AE013599; AAF57780.2; -; Genomic_DNA.
DR EMBL; AE013599; AAS64814.2; -; Genomic_DNA.
DR EMBL; AE013599; ACL83150.1; -; Genomic_DNA.
DR EMBL; AE013599; AGB93595.1; -; Genomic_DNA.
DR EMBL; AY071273; AAL48895.1; -; mRNA.
DR EMBL; BT001876; AAN71648.1; -; mRNA.
DR EMBL; BT003591; AAO39594.1; -; mRNA.
DR RefSeq; NP_001137696.1; NM_001144224.2. [Q9U6B8-3]
DR RefSeq; NP_001261063.1; NM_001274134.1. [Q9U6B8-3]
DR RefSeq; NP_611273.1; NM_137429.3. [Q9U6B8-1]
DR RefSeq; NP_725727.1; NM_170626.2. [Q9U6B8-1]
DR RefSeq; NP_995881.2; NM_206159.2. [Q9U6B8-1]
DR PDB; 4HKR; X-ray; 3.35 A; A/B=133-341.
DR PDB; 4HKS; X-ray; 3.35 A; A/B=133-341.
DR PDB; 6AKI; X-ray; 4.50 A; A/B/C/D/E/F/O/P/Q/R/S/T=132-341.
DR PDB; 6BBF; X-ray; 6.71 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=133-341.
DR PDB; 6BBG; X-ray; 6.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=133-341.
DR PDB; 6BBH; X-ray; 6.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=133-341.
DR PDB; 6BBI; X-ray; 4.35 A; A/B/C=133-341.
DR PDB; 7KR5; EM; 3.30 A; A/B/C/D/E/F=133-341.
DR PDBsum; 4HKR; -.
DR PDBsum; 4HKS; -.
DR PDBsum; 6AKI; -.
DR PDBsum; 6BBF; -.
DR PDBsum; 6BBG; -.
DR PDBsum; 6BBH; -.
DR PDBsum; 6BBI; -.
DR PDBsum; 7KR5; -.
DR AlphaFoldDB; Q9U6B8; -.
DR SMR; Q9U6B8; -.
DR BioGRID; 62725; 6.
DR DIP; DIP-59770N; -.
DR IntAct; Q9U6B8; 2.
DR STRING; 7227.FBpp0113106; -.
DR TCDB; 1.A.52.1.5; the ca(2+) release-activated ca(2+) (crac) channel (crac-c) family.
DR PaxDb; Q9U6B8; -.
DR DNASU; 37040; -.
DR EnsemblMetazoa; FBtr0086795; FBpp0085974; FBgn0041585. [Q9U6B8-1]
DR EnsemblMetazoa; FBtr0086797; FBpp0085976; FBgn0041585. [Q9U6B8-1]
DR EnsemblMetazoa; FBtr0114614; FBpp0113106; FBgn0041585. [Q9U6B8-3]
DR EnsemblMetazoa; FBtr0336698; FBpp0307679; FBgn0041585. [Q9U6B8-1]
DR EnsemblMetazoa; FBtr0336699; FBpp0307680; FBgn0041585. [Q9U6B8-3]
DR GeneID; 37040; -.
DR KEGG; dme:Dmel_CG11430; -.
DR CTD; 37040; -.
DR FlyBase; FBgn0041585; Orai.
DR VEuPathDB; VectorBase:FBgn0041585; -.
DR eggNOG; KOG4298; Eukaryota.
DR GeneTree; ENSGT00390000015354; -.
DR HOGENOM; CLU_062509_0_0_1; -.
DR InParanoid; Q9U6B8; -.
DR OMA; VMIVFMA; -.
DR BioGRID-ORCS; 37040; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37040; -.
DR PRO; PR:Q9U6B8; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0041585; Expressed in embryonic/larval hemocyte (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q9U6B8; baseline and differential.
DR Genevisible; Q9U6B8; DM.
DR GO; GO:0034704; C:calcium channel complex; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005262; F:calcium channel activity; IDA:FlyBase.
DR GO; GO:0005246; F:calcium channel regulator activity; ISS:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015279; F:store-operated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:UniProtKB.
DR GO; GO:0002115; P:store-operated calcium entry; IMP:FlyBase.
DR Gene3D; 1.20.140.140; -; 1.
DR InterPro; IPR012446; CRAC_channel.
DR InterPro; IPR038350; Orai_sf.
DR PANTHER; PTHR31501; PTHR31501; 2.
DR Pfam; PF07856; Orai-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Cell membrane; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..351
FT /note="Calcium release-activated calcium channel protein 1"
FT /id="PRO_0000234388"
FT TOPO_DOM 1..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..121
FT /note="MSVWTTANNSGLETPTKSPITSSVPRAARSSAVITTGNHQQHHFQHVVAAAV
FT AAATSVATGHQFQQQFPLHAHPHPQHHSNSPTGSGSNSNNSAGFQRTSISNSLLQFPPP
FT PPPSSQNQAK -> MPPFEEGESKPEEQIPLKPPRRHKKMKSADQEAAQTPAEDHEEEQ
FT LLPGSGTSNLRYARANLSQSSLMLSHQQGSFESSTERTASSETLDVMPISRRYQVHPQP
FT NRLGIRQPASALASALHATARLAASVDAYTAAATATAATGDYGDYMRPQPNLGHAHQLP
FT LTQTTQTAQPLHHQLPAHQLGNLRASNFVGSSRYLYHSQFNSNSPQTRRFTAQRDGSPA
FT YAASVAAASAAAAASAVAPIAPLAPLASIASPPFAAQPPPFQLRTYQQNQSYRFQ (in
FT isoform E)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_018313"
FT VAR_SEQ 122..132
FT /note="PRGHHRTASSS -> AGRTVQIDCRI (in isoform C)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_021772"
FT VAR_SEQ 133..351
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_021773"
FT CONFLICT 28
FT /note="A -> S (in Ref. 1; ABF54966)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="H -> HPH (in Ref. 1; ABF54966)"
FT /evidence="ECO:0000305"
FT HELIX 158..177
FT /evidence="ECO:0007829|PDB:7KR5"
FT HELIX 189..215
FT /evidence="ECO:0007829|PDB:7KR5"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:4HKR"
FT HELIX 241..271
FT /evidence="ECO:0007829|PDB:7KR5"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:7KR5"
FT HELIX 276..303
FT /evidence="ECO:0007829|PDB:7KR5"
FT HELIX 308..331
FT /evidence="ECO:0007829|PDB:4HKR"
SQ SEQUENCE 351 AA; 38507 MW; 328A586D251D3335 CRC64;
MSVWTTANNS GLETPTKSPI TSSVPRAARS SAVITTGNHQ QHHFQHVVAA AVAAATSVAT
GHQFQQQFPL HAHPHPQHHS NSPTGSGSNS NNSAGFQRTS ISNSLLQFPP PPPPSSQNQA
KPRGHHRTAS SSMSQSGEDL HSPTYLSWRK LQLSRAKLKA SSKTSALLSG FAMVAMVEVQ
LDHDTNVPPG MLIAFAICTT LLVAVHMLAL MISTCILPNI ETVCNLHSIS LVHESPHERL
HWYIETAWAF STLLGLILFL LEIAILCWVK FYDLSPPAAW SACVVLIPVM IIFMAFAIHF
YRSLVSHKYE VTVSGIRELE MLKEQMEQDH LEHHNNIRNN GMNYGASGDI V
