CCH2R_DROME
ID CCH2R_DROME Reviewed; 489 AA.
AC Q4V622; A1Z6J7; A9UJU7; E1JGY1;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Neuropeptide CCHamide-2 receptor {ECO:0000303|PubMed:21110953};
GN Name=CCHa2-R {ECO:0000312|FlyBase:FBgn0033058};
GN ORFNames=CG14593 {ECO:0000312|FlyBase:FBgn0033058};
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:AAY54900.1};
RN [1] {ECO:0000312|EMBL:AAQ19611.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), 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:0000312|EMBL:AAY54900.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {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 [6] {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 [7] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26020940; DOI=10.1371/journal.pgen.1005209;
RA Sano H., Nakamura A., Texada M.J., Truman J.W., Ishimoto H., Kamikouchi A.,
RA Nibu Y., Kume K., Ida T., Kojima M.;
RT "The nutrient-responsive hormone CCHamide-2 controls growth by regulating
RT insulin-like peptides in the brain of Drosophila melanogaster.";
RL PLoS Genet. 11:E1005209-E1005209(2015).
RN [8]
RP ERRATUM OF PUBMED:26020940.
RX PubMed=26394035; DOI=10.1371/journal.pgen.1005481;
RA Sano H., Nakamura A., Texada M.J., Truman J.W., Ishimoto H., Kamikouchi A.,
RA Nibu Y., Kume K., Ida T., Kojima M.;
RL PLoS Genet. 11:E1005481-E1005481(2015).
CC -!- FUNCTION: Receptor for the neuropeptide CCHamide-2.
CC {ECO:0000269|PubMed:21110953, ECO:0000269|PubMed:23293632}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0033058};
CC IsoId=Q4V622-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0033058};
CC IsoId=Q4V622-2; Sequence=VSP_057998, VSP_057999;
CC -!- TISSUE SPECIFICITY: Highly expressed in larval brain (PubMed:24098432,
CC PubMed:26020940). Also highly expressed in adult brain with very low
CC levels in larval and adult gut (PubMed:24098432).
CC {ECO:0000269|PubMed:24098432, ECO:0000269|PubMed:26020940}.
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, increases again in pupae and decreases
CC slightly in adults. {ECO:0000269|PubMed:24098432}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of insulin-like peptide Ilp5 mRNA,
CC reduced secretion of Ilp2 and Ilp5 proteins in mid-L3 larvae, growth
CC defects and developmental delay during larval stages.
CC {ECO:0000269|PubMed:26020940}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY282787; AAQ19611.1; -; mRNA.
DR EMBL; AE013599; AAF57285.4; -; Genomic_DNA.
DR EMBL; AE013599; ACZ94340.1; -; Genomic_DNA.
DR EMBL; BT022484; AAY54900.1; -; mRNA.
DR RefSeq; NP_001163060.1; NM_001169589.2. [Q4V622-2]
DR RefSeq; NP_610199.2; NM_136355.4. [Q4V622-1]
DR AlphaFoldDB; Q4V622; -.
DR SMR; Q4V622; -.
DR STRING; 7227.FBpp0085328; -.
DR GlyGen; Q4V622; 3 sites.
DR PaxDb; Q4V622; -.
DR DNASU; 35535; -.
DR EnsemblMetazoa; FBtr0085975; FBpp0085328; FBgn0033058. [Q4V622-1]
DR EnsemblMetazoa; FBtr0301687; FBpp0290901; FBgn0033058. [Q4V622-2]
DR GeneID; 35535; -.
DR KEGG; dme:Dmel_CG14593; -.
DR UCSC; CG14593-RA; d. melanogaster. [Q4V622-1]
DR CTD; 35535; -.
DR FlyBase; FBgn0033058; CCHa2-R.
DR VEuPathDB; VectorBase:FBgn0033058; -.
DR eggNOG; KOG4219; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR InParanoid; Q4V622; -.
DR OMA; GHNLKQE; -.
DR PhylomeDB; Q4V622; -.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 35535; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35535; -.
DR PRO; PR:Q4V622; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033058; Expressed in VUM motorneuron (Drosophila) and 3 other tissues.
DR ExpressionAtlas; Q4V622; baseline and differential.
DR Genevisible; E1JGY1; DM.
DR GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..489
FT /note="Neuropeptide CCHamide-2 receptor"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435024"
FT TOPO_DOM 1..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..143
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 438..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 142..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 477
FT /note="S -> R (in isoform B)"
FT /id="VSP_057998"
FT VAR_SEQ 478..489
FT /note="Missing (in isoform B)"
FT /id="VSP_057999"
FT CONFLICT 261
FT /note="A -> T (in Ref. 1; AAQ19611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 53531 MW; E0BCA409B6F45FBD CRC64;
MYASLMDVGQ TLAARLADSD GNGANDSGLL ATGQGLEQEQ EGLALDMGHN ASADGGIVPY
VPVLDRPETY IVTVLYTLIF IVGVLGNGTL VIIFFRHRSM RNIPNTYILS LALADLLVIL
VCVPVATIVY TQESWPFERN MCRISEFFKD ISIGVSVFTL TALSGERYCA IVNPLRKLQT
KPLTVFTAVM IWILAILLGM PSVLFSDIKS YPVFTATGNM TIEVCSPFRD PEYAKFMVAG
KALVYYLLPL SIIGALYIMM AKRLHMSARN MPGEQQSMQS RTQARARLHV ARMVVAFVVV
FFICFFPYHV FELWYHFYPT AEEDFDEFWN VLRIVGFCTS FLNSCVNPVA LYCVSGVFRQ
HFNRYLCCIC VKRQPHLRQH STATGMMDNT SVMSMRRSTY VGGTAGNLRA SLHRNSNHGV
GGAGGGVGGG VGSGRVGSFH RQDSMPLQHG NAHGGGAGGG SSGLGAGGRT AAVSEKSFIN
RYESGVMRY
