CCH1R_DROME
ID CCH1R_DROME Reviewed; 499 AA.
AC A1ZAX0;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Neuropeptide CCHamide-1 receptor {ECO:0000303|PubMed:21110953};
GN Name=CCHa1-R {ECO:0000312|FlyBase:FBgn0050106};
GN ORFNames=CG30106 {ECO:0000312|FlyBase:FBgn0050106};
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|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAX58700.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=21110953; DOI=10.1016/j.bbrc.2010.11.089;
RA Hansen K.K., Hauser F., Williamson M., Weber S.B., Grimmelikhuijzen C.J.;
RT "The Drosophila genes CG14593 and CG30106 code for G-protein-coupled
RT receptors specifically activated by the neuropeptides CCHamide-1 and
RT CCHamide-2.";
RL Biochem. Biophys. Res. Commun. 404:184-189(2011).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=23293632; DOI=10.3389/fendo.2012.00177;
RA Ida T., Takahashi T., Tominaga H., Sato T., Sano H., Kume K., Ozaki M.,
RA Hiraguchi T., Shiotani H., Terajima S., Nakamura Y., Mori K., Yoshida M.,
RA Kato J., Murakami N., Miyazato M., Kangawa K., Kojima M.;
RT "Isolation of the bioactive peptides CCHamide-1 and CCHamide-2 from
RT Drosophila and their putative role in appetite regulation as ligands for G
RT protein-coupled receptors.";
RL Front. Endocrinol. 3:177-177(2012).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=24098432; DOI=10.1371/journal.pone.0076131;
RA Li S., Torre-Muruzabal T., Soegaard K.C., Ren G.R., Hauser F.,
RA Engelsen S.M., Poedenphanth M.D., Desjardins A., Grimmelikhuijzen C.J.;
RT "Expression patterns of the Drosophila neuropeptide CCHamide-2 and its
RT receptor may suggest hormonal signaling from the gut to the brain.";
RL PLoS ONE 8:E76131-E76131(2013).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=24067446; DOI=10.1038/srep02765;
RA Farhan A., Gulati J., Grobetae-Wilde E., Vogel H., Hansson B.S., Knaden M.;
RT "The CCHamide 1 receptor modulates sensory perception and olfactory
RT behavior in starved Drosophila.";
RL Sci. Rep. 3:2765-2765(2013).
CC -!- FUNCTION: Receptor for the neuropeptide CCHamide-1 (PubMed:21110953,
CC PubMed:23293632). Plays a role in the modulation of starvation-induced
CC olfactory behavior where starved flies show increased responsiveness to
CC food odorants, repellants and pheromones (PubMed:24067446).
CC {ECO:0000269|PubMed:21110953, ECO:0000269|PubMed:23293632,
CC ECO:0000269|PubMed:24067446}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Low levels in larval brain and gut with higher
CC levels in adult brain and gut. {ECO:0000269|PubMed:24098432}.
CC -!- DEVELOPMENTAL STAGE: Very low expression in eggs. Expression increases
CC during the first and second instar larval stages, decreases in the
CC third instar larval stage and increases again in pupae and adults.
CC {ECO:0000269|PubMed:24098432}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY842252; AAX58700.1; -; mRNA.
DR EMBL; AE013599; AAF57819.3; -; Genomic_DNA.
DR RefSeq; NP_611241.2; NM_137397.3.
DR AlphaFoldDB; A1ZAX0; -.
DR SMR; A1ZAX0; -.
DR STRING; 7227.FBpp0086052; -.
DR GlyGen; A1ZAX0; 2 sites.
DR PaxDb; A1ZAX0; -.
DR PRIDE; A1ZAX0; -.
DR EnsemblMetazoa; FBtr0086893; FBpp0086052; FBgn0050106.
DR GeneID; 37004; -.
DR KEGG; dme:Dmel_CG30106; -.
DR UCSC; CG30106-RA; d. melanogaster.
DR CTD; 37004; -.
DR FlyBase; FBgn0050106; CCHa1-R.
DR VEuPathDB; VectorBase:FBgn0050106; -.
DR eggNOG; KOG4219; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR HOGENOM; CLU_009579_6_2_1; -.
DR InParanoid; A1ZAX0; -.
DR OMA; LWFYFWP; -.
DR OrthoDB; 1153238at2759; -.
DR PhylomeDB; A1ZAX0; -.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 37004; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37004; -.
DR PRO; PR:A1ZAX0; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0050106; Expressed in oviduct (Drosophila) and 7 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0008261; F:allatostatin receptor activity; IDA:FlyBase.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; IDA: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 InterPro; IPR001556; Bombsn_rcpt-like.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00358; BOMBESINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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..499
FT /note="Neuropeptide CCHamide-1 receptor"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435023"
FT TOPO_DOM 1..85
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..348
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 154..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 499 AA; 55549 MW; 620CC8AA12F9E48A CRC64;
MIANLVSMET DLAMNIGLDT SGEAPTALPP MPNVTETLWD LAMVVSQSTQ WPLLDTGSSE
NFSELVTTET PYVPYGRRPE TYIVPILFAL IFVVGVLGNG TLIVVFLSVR QMRNVPNTYI
LSLALADLLV IITTVPLAST VYTVEYWPYG SFLCSLSEFM KDVSIGVSVF TLTALSGDRY
FAIVDPLRKF HAHGGGRRAT RMTLATAVSI WLLAILCGLP ALIGSNLKHL GINEKSIVIC
YPYPEEWGIN YAKSMVLLHF LVYYAIPLVV IAVFYVLIAL HLMYSASVPG EIQGAVRQVR
ARRKVAVTVL AFVVIFGICF LPYHVFFLWF YFWPTAQDDY NAFWHVLRIV AYCMSFANSC
ANPVALYFVS GAFRKHFNRY LFCRGASGRR KKRGQHDTFC MHRDTSLTST ASKRFQSRHS
CYQSTIRSCR LQETTITTLP NGGNQNGANI SAVELALPVL QAPGHNEAHA PPSYGFLPLN
EIVQQTRSSP AKFQESLLN
