CCAPR_DROME
ID CCAPR_DROME Reviewed; 495 AA.
AC Q868T3; Q8ITD2; Q9VBJ8;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 4.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cardioacceleratory peptide receptor;
DE AltName: Full=Crustacean cardioactive peptide receptor;
GN Name=CCAP-R; Synonyms=CcapR; ORFNames=CG33344;
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] {ECO:0000305, ECO:0000312|EMBL:AAN10041.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Canton-S {ECO:0000312|EMBL:AAN10041.1};
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, ECO:0000312|EMBL:AAO66429.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12646179; DOI=10.1016/s0006-291x(03)00302-4;
RA Cazzamali G., Hauser F., Kobberup S., Williamson M.,
RA Grimmelikhuijzen C.J.P.;
RT "Molecular identification of a Drosophila G protein-coupled receptor
RT specific for crustacean cardioactive peptide.";
RL Biochem. Biophys. Res. Commun. 303:146-152(2003).
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: Binds to the cardioactive peptide (CCAP), which is a
CC neuropeptide. {ECO:0000269|PubMed:12177421,
CC ECO:0000269|PubMed:12646179}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12177421,
CC ECO:0000269|PubMed:12646179}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12177421, ECO:0000269|PubMed:12646179}.
CC -!- TISSUE SPECIFICITY: In adults, expressed abundantly in the head and
CC very weakly in the body. {ECO:0000269|PubMed:12646179}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all stages, with abundance in embryo
CC and only very weakly in larvae. {ECO:0000269|PubMed:12646179}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Vasopressin/oxytocin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO66429.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF522188; AAN10041.1; -; mRNA.
DR EMBL; AY219842; AAO66429.1; ALT_SEQ; mRNA.
DR EMBL; AE014297; AAF56536.5; -; Genomic_DNA.
DR RefSeq; NP_996297.3; NM_206574.4.
DR AlphaFoldDB; Q868T3; -.
DR SMR; Q868T3; -.
DR BioGRID; 77556; 4.
DR IntAct; Q868T3; 1.
DR STRING; 7227.FBpp0293006; -.
DR GlyGen; Q868T3; 1 site.
DR PaxDb; Q868T3; -.
DR DNASU; 2768688; -.
DR EnsemblMetazoa; FBtr0304043; FBpp0293006; FBgn0039396.
DR GeneID; 2768688; -.
DR KEGG; dme:Dmel_CG33344; -.
DR CTD; 2768688; -.
DR FlyBase; FBgn0039396; CCAP-R.
DR VEuPathDB; VectorBase:FBgn0039396; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_15_0_1; -.
DR InParanoid; Q868T3; -.
DR OrthoDB; 1034048at2759; -.
DR BioGRID-ORCS; 2768688; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 2768688; -.
DR PRO; PR:Q868T3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039396; Expressed in VUM neuron (Drosophila) and 4 other tissues.
DR ExpressionAtlas; Q868T3; baseline and differential.
DR Genevisible; Q868T3; DM.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0008188; F:neuropeptide receptor activity; IPI:FlyBase.
DR GO; GO:0005000; F:vasopressin receptor activity; IEA:InterPro.
DR GO; GO:0018990; P:ecdysis, chitin-based cuticle; TAS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001817; Vasoprsn_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00896; VASOPRESSINR.
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; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..495
FT /note="Cardioacceleratory peptide receptor"
FT /id="PRO_0000069218"
FT TOPO_DOM 1..54
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..164
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 24..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 45
FT /note="A -> V (in Ref. 1; AAN10041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 54648 MW; 28A1AB5C01504716 CRC64;
MLHLRLFDSS LYYTLASASE SSGLASSTST ERSFNGTQGA GGVAAGGESL TPTDVAAVNL
TYFTPAISHV MLAPTTIATT TASATMVQIQ TTAAPSHDLE TGGNSTSSDP GEFDNLNSFY
FYETEQFAVL WILFTVIVLG NSAVLFVMFI NKNRKSRMNY FIKQLALADL CVGLLNVLTD
IIWRITISWR AGNLACKAIR FSQVCVTYSS TYVLVAMSID RYDAITHPMN FSKSWKRARH
LVAGAWLISA LFSLPILVLY EEKLIQGHPQ CWIELGSPIA WQVYMSLVSA TLFAIPALII
SACYAIIVKT IWAKGSIFVP TERAGFGAAP ARRASSRGII PRAKVKTVKM TLTIVFVFII
CWSPYIIFDL LQVFGQIPHS QTNIAIATFI QSLAPLNSAA NPLIYCLFSS QVFRTLSRFP
PFKWFTCCCK SYRNNSQQNR CHTVGRRLHN SCDSMRTLTT SLTVSRRSTN KTNARVVICE
RPTKVVTVPA MSERV
