CCHA1_DROME
ID CCHA1_DROME Reviewed; 182 AA.
AC Q4V4I9; Q9VFN6;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Neuropeptide CCHamide-1 {ECO:0000303|PubMed:21110953};
DE Flags: Precursor;
GN Name=CCHa1 {ECO:0000312|FlyBase:FBgn0038199};
GN ORFNames=CG14358 {ECO:0000312|FlyBase:FBgn0038199};
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:AAY55433.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-35, FUNCTION, MASS
RP SPECTROMETRY, AMIDATION AT HIS-35, AND DISULFIDE BOND.
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 [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:AAY55433.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PROTEIN SEQUENCE OF 23-35, IDENTIFICATION BY MASS SPECTROMETRY, MASS
RP SPECTROMETRY, AMIDATION AT HIS-35, AND DISULFIDE BOND.
RC TISSUE=Midgut {ECO:0000303|PubMed:21214272};
RX PubMed=21214272; DOI=10.1021/pr101116g;
RA Reiher W., Shirras C., Kahnt J., Baumeister S., Isaac R.E., Wegener C.;
RT "Peptidomics and peptide hormone processing in the Drosophila midgut.";
RL J. Proteome Res. 10:1881-1892(2011).
RN [6] {ECO:0000305}
RP 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 [7] {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 [8] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=24850274; DOI=10.1007/s00441-014-1880-2;
RA Veenstra J.A., Ida T.;
RT "More Drosophila enteroendocrine peptides: Orcokinin B and the CCHamides 1
RT and 2.";
RL Cell Tissue Res. 357:607-621(2014).
RN [9] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=26168160; DOI=10.1371/journal.pone.0133017;
RA Ren G.R., Hauser F., Rewitz K.F., Kondo S., Engelbrecht A.F.,
RA Didriksen A.K., Schjoett S.R., Sembach F.E., Li S., Soegaard K.C.,
RA Soendergaard L., Grimmelikhuijzen C.J.;
RT "CCHamide-2 is an orexigenic brain-gut peptide in Drosophila.";
RL PLoS ONE 10:E0133017-E0133017(2015).
CC -!- FUNCTION: Ligand for the CCHamide-1 receptor CCHa1-R.
CC {ECO:0000269|PubMed:21110953, ECO:0000269|PubMed:23293632}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in endocrine cells of the larval midgut
CC (at protein level) (PubMed:24098432, PubMed:24850274). Low levels in
CC larval brain with higher levels in larval and adult gut and adult brain
CC (PubMed:24098432). {ECO:0000269|PubMed:24098432,
CC ECO:0000269|PubMed:24850274}.
CC -!- DEVELOPMENTAL STAGE: Very low expression in eggs. Expression increases
CC during larval stages, decreases in pupae and increases again in adults.
CC {ECO:0000269|PubMed:24098432}.
CC -!- MASS SPECTROMETRY: Mass=1445.30; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:23293632};
CC -!- MASS SPECTROMETRY: Mass=1446.57; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21214272};
CC -!- DISRUPTION PHENOTYPE: No effect on developmental timing or on levels of
CC the insulin-like peptides Ilp2 and Ilp3. {ECO:0000269|PubMed:26168160}.
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DR EMBL; AE014297; AAF55014.2; -; Genomic_DNA.
DR EMBL; BT022941; AAY55357.1; -; mRNA.
DR EMBL; BT023017; AAY55433.1; -; mRNA.
DR RefSeq; NP_001097784.1; NM_001104314.2.
DR AlphaFoldDB; Q4V4I9; -.
DR STRING; 7227.FBpp0112144; -.
DR PaxDb; Q4V4I9; -.
DR DNASU; 41711; -.
DR EnsemblMetazoa; FBtr0113232; FBpp0112144; FBgn0038199.
DR GeneID; 41711; -.
DR KEGG; dme:Dmel_CG14358; -.
DR UCSC; CG14358-RB; d. melanogaster.
DR CTD; 41711; -.
DR FlyBase; FBgn0038199; CCHa1.
DR VEuPathDB; VectorBase:FBgn0038199; -.
DR eggNOG; ENOG502TD7N; Eukaryota.
DR HOGENOM; CLU_1534182_0_0_1; -.
DR InParanoid; Q4V4I9; -.
DR OMA; MWYSKCS; -.
DR OrthoDB; 1617959at2759; -.
DR PhylomeDB; Q4V4I9; -.
DR BioGRID-ORCS; 41711; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41711; -.
DR PRO; PR:Q4V4I9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038199; Expressed in brain and 13 other tissues.
DR ExpressionAtlas; Q4V4I9; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0005184; F:neuropeptide hormone activity; IDA:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
DR InterPro; IPR037729; CCHa1/2.
DR PANTHER; PTHR35980; PTHR35980; 1.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Disulfide bond; Hormone;
KW Neuropeptide; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:21214272,
FT ECO:0000269|PubMed:23293632"
FT PEPTIDE 23..35
FT /note="Neuropeptide CCHamide-1"
FT /evidence="ECO:0000269|PubMed:21214272,
FT ECO:0000269|PubMed:23293632"
FT /id="PRO_0000435025"
FT PROPEP 39..182
FT /evidence="ECO:0000269|PubMed:21214272,
FT ECO:0000269|PubMed:23293632"
FT /id="PRO_0000435026"
FT REGION 67..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Histidine amide"
FT /evidence="ECO:0000269|PubMed:21214272,
FT ECO:0000269|PubMed:23293632"
FT DISULFID 24..31
FT /evidence="ECO:0000269|PubMed:21214272,
FT ECO:0000269|PubMed:23293632"
SQ SEQUENCE 182 AA; 20468 MW; E29DABAA441F97C7 CRC64;
MWYSKCSWTL VVLVALFALV TGSCLEYGHS CWGAHGKRSG GKAVIDAKQH PLPNSYGLDS
VVEQLYNNNN NNQNNQDDDN NDDDSNRNTN ANSANNIPLA APAIISRRES EDRRIGGLKW
AQLMRQHRYQ LRQLQDQQQQ GRGRGGQGQY DAAAESWRKL QQALQAQIDA DNENYSGYEL
TK
