CAPAR_DROME
ID CAPAR_DROME Reviewed; 477 AA.
AC Q8ITC7; Q9VP15;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Neuropeptides capa receptor;
DE AltName: Full=Cap2b receptor;
DE AltName: Full=Capability receptor;
GN Name=CapaR; ORFNames=CG14575;
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 {ECO:0000312|EMBL:AAN10046.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Canton-S {ECO:0000269|PubMed:12177421};
RX PubMed=12177421; DOI=10.1073/pnas.162276199;
RA Park Y., Kim Y.-J., Adams M.E.;
RT "Identification of G protein-coupled receptors for Drosophila PRXamide
RT peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor
RT coevolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11423-11428(2002).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=12459185; DOI=10.1016/s0006-291x(02)02709-2;
RA Iversen A., Cazzamali G., Williamson M., Hauser F.,
RA Grimmelikhuijzen C.J.P.;
RT "Molecular cloning and functional expression of a Drosophila receptor for
RT the neuropeptides capa-1 and -2.";
RL Biochem. Biophys. Res. Commun. 299:628-633(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305}
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).
CC -!- FUNCTION: Acts as a receptor for the neuropeptides CAP-1 and CAP-2, but
CC not CAP-3. Probably a component of signal transduction pathway that
CC leads to Malpighian tubule fluid secretion in response to these
CC ligands. {ECO:0000269|PubMed:12177421, ECO:0000269|PubMed:12459185}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In adults, expression in thorax and/or abdomen.
CC {ECO:0000269|PubMed:12459185}.
CC -!- DEVELOPMENTAL STAGE: Expressed weakly in 16-24 hours embryos and second
CC instar larvae and strongly in first and third instar larvae and adults.
CC {ECO:0000269|PubMed:12459185}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF522193; AAN10046.1; -; mRNA.
DR EMBL; AF505865; AAO20968.1; -; mRNA.
DR EMBL; AE014296; AAS65092.1; -; Genomic_DNA.
DR RefSeq; NP_996140.1; NM_206418.3.
DR AlphaFoldDB; Q8ITC7; -.
DR SMR; Q8ITC7; -.
DR BioGRID; 65637; 1.
DR STRING; 7227.FBpp0078034; -.
DR GlyGen; Q8ITC7; 2 sites.
DR PaxDb; Q8ITC7; -.
DR PRIDE; Q8ITC7; -.
DR EnsemblMetazoa; FBtr0078379; FBpp0078034; FBgn0037100.
DR GeneID; 40393; -.
DR KEGG; dme:Dmel_CG14575; -.
DR CTD; 40393; -.
DR FlyBase; FBgn0037100; CapaR.
DR VEuPathDB; VectorBase:FBgn0037100; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01040000240430; -.
DR InParanoid; Q8ITC7; -.
DR OMA; TVCFYFV; -.
DR PhylomeDB; Q8ITC7; -.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 40393; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40393; -.
DR PRO; PR:Q8ITC7; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0037100; Expressed in adult Malpighian tubule (Drosophila) and 4 other tissues.
DR ExpressionAtlas; Q8ITC7; baseline and differential.
DR Genevisible; Q8ITC7; DM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0001607; F:neuromedin U receptor activity; IEA:InterPro.
DR GO; GO:0008188; F:neuropeptide receptor activity; IDA:UniProtKB.
DR GO; GO:0007589; P:body fluid secretion; TAS:UniProtKB.
DR GO; GO:0071465; P:cellular response to desiccation; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISM:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:FlyBase.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR005390; NeuromedU_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01565; NEUROMEDINUR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..477
FT /note="Neuropeptides capa receptor"
FT /id="PRO_0000069217"
FT TOPO_DOM 1..72
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 477 AA; 54005 MW; 34FFB13F301A9F4D CRC64;
MNSSTDPTFS ELNASFTNTP DTLFATSVSS DPSHGFGEED YACGTFNCSP KEFVAFVLGP
QTLPLYKAVL ITIIFGGIFI TGVVGNLLVC IVIIRHSAMH TATNYYLFSL AVSDLLYLLF
GLPTEVFLYW HQYPDLFGMP FCKIRAFISE ACTYVSVFTI VAFSMERFLA ICHPLHLYAM
VGFKRAIRII TALWIVSFIS AIPFGLLSDI QYLNYPLDHS RIEESAFCSM SPKIVNEIPV
FEVSFCIFFV IPMILIILLY GRMGAKIRSR TNQKLGVQQG TNNRETRNSQ MRKKTVIRML
AAVVITFFVC WFPFHLQRLI FLYAKNMDNY LDINEALFSI AGFAYYVSCT VNPIVYSVMS
RRYRVAFREL LCGKAVGAYY NSGFARDHSS FRESSAYDRV HSVHVRASQH PNKFETDSSS
ANRVLIKKTY SLPLPKNADS TVLSTTDIVI VLENSHTVCE EPKVENDIWI ENEETCI
