CP2B_DROME
ID CP2B_DROME Reviewed; 151 AA.
AC Q9NIP6; Q9VAE2;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cardio acceleratory peptide 2b;
DE AltName: Full=Capability protein;
DE AltName: Full=Myotropin-CAP2b-like protein;
DE Contains:
DE RecName: Full=CAP-1;
DE AltName: Full=CAP2b-1;
DE AltName: Full=Capa-1;
DE Contains:
DE RecName: Full=CAP-2;
DE AltName: Full=CAP2b-2;
DE AltName: Full=Capa-2;
DE Contains:
DE RecName: Full=CAP-3;
DE AltName: Full=CAP2b-3;
DE AltName: Full=Capa-3;
DE AltName: Full=Myotropin;
DE AltName: Full=Pyrokinin-1;
DE Flags: Precursor;
GN Name=Capa; Synonyms=MT-CAP2b; ORFNames=CG15520;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11959669; DOI=10.1152/ajpregu.00584.2001;
RA Kean L., Cazenave W., Costes L., Broderick K.E., Graham S., Pollock V.P.,
RA Davies S.A., Veenstra J.A., Dow J.A.;
RT "Two nitridergic peptides are encoded by the gene capability in Drosophila
RT melanogaster.";
RL Am. J. Physiol. 282:R1297-R1307(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Vanden Broeck J.J.M.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PROTEIN SEQUENCE OF 31-42 AND 83-92, AND AMIDATION AT VAL-42; VAL-92 AND
RP LEU-130.
RC TISSUE=Larva;
RX PubMed=12171930; DOI=10.1074/jbc.m206257200;
RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.;
RT "Peptidomics of the larval Drosophila melanogaster central nervous
RT system.";
RL J. Biol. Chem. 277:40368-40374(2002).
RN [7]
RP FUNCTION.
RC STRAIN=Canton-S;
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 [8]
RP FUNCTION.
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 [9]
RP REVIEW.
RX PubMed=11179818; DOI=10.1016/s0196-9781(00)00376-4;
RA Vanden Broeck J.J.M.;
RT "Neuropeptides and their precursors in the fruitfly, Drosophila
RT melanogaster.";
RL Peptides 22:241-254(2001).
RN [10]
RP FUNCTION.
RX PubMed=16054112; DOI=10.1016/j.bbrc.2005.07.038;
RA Cazzamali G., Torp M., Hauser F., Williamson M., Grimmelikhuijzen C.J.;
RT "The Drosophila gene CG9918 codes for a pyrokinin-1 receptor.";
RL Biochem. Biophys. Res. Commun. 33:14-19(2005).
CC -!- FUNCTION: CAP-1 and CAP-2, but not CAP-3 are ligands for the Capa
CC receptor (PubMed:12177421, PubMed:12459185). CAP-1 and CAP-2 are
CC probably components of the signal transduction pathway that leads to
CC Malpighian tubule fluid secretion via the second messenger nitric oxide
CC (PubMed:11959669). CAP-3 is a ligand for the PK1-R G-protein coupled
CC receptor (PubMed:16054112). {ECO:0000269|PubMed:11959669,
CC ECO:0000269|PubMed:12177421, ECO:0000269|PubMed:12459185,
CC ECO:0000269|PubMed:16054112}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11959669}.
CC Note=Released from the neuroendocrine cells into the hemolymph.
CC -!- TISSUE SPECIFICITY: In larvae, the precursor peptide is exclusively
CC present in a single pair of neuroendocrine cells in the labial
CC neuromere (subesophageal ganglion) and three pairs of cells in the
CC ventral ganglion abdominal neuromeres. {ECO:0000269|PubMed:11959669}.
CC -!- SIMILARITY: Belongs to the pyrokinin family. {ECO:0000305}.
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DR EMBL; AF203878; AAF62876.1; -; mRNA.
DR EMBL; AJ291724; CAC17603.1; -; mRNA.
DR EMBL; AE014297; AAF56969.2; -; Genomic_DNA.
DR EMBL; AY069234; AAL39379.1; -; mRNA.
DR RefSeq; NP_524552.1; NM_079828.3.
DR AlphaFoldDB; Q9NIP6; -.
DR BioGRID; 68398; 7.
DR DIP; DIP-22273N; -.
DR IntAct; Q9NIP6; 1.
DR STRING; 7227.FBpp0084880; -.
DR PaxDb; Q9NIP6; -.
DR PRIDE; Q9NIP6; -.
DR DNASU; 43541; -.
DR EnsemblMetazoa; FBtr0085514; FBpp0084880; FBgn0039722.
DR GeneID; 43541; -.
DR KEGG; dme:Dmel_CG15520; -.
DR CTD; 43541; -.
DR FlyBase; FBgn0039722; Capa.
DR VEuPathDB; VectorBase:FBgn0039722; -.
DR eggNOG; ENOG502TAG0; Eukaryota.
DR HOGENOM; CLU_1697372_0_0_1; -.
DR InParanoid; Q9NIP6; -.
DR OMA; SMLVHIV; -.
DR OrthoDB; 1570798at2759; -.
DR PhylomeDB; Q9NIP6; -.
DR BioGRID-ORCS; 43541; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43541; -.
DR PRO; PR:Q9NIP6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039722; Expressed in insect adult head and 8 other tissues.
DR ExpressionAtlas; Q9NIP6; baseline and differential.
DR Genevisible; Q9NIP6; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0008613; F:diuretic hormone activity; IDA:FlyBase.
DR GO; GO:0016084; F:myostimulatory hormone activity; IMP:UniProtKB.
DR GO; GO:0005184; F:neuropeptide hormone activity; IMP:UniProtKB.
DR GO; GO:0071855; F:neuropeptide receptor binding; IPI:FlyBase.
DR GO; GO:0006812; P:cation transport; TAS:FlyBase.
DR GO; GO:0042045; P:epithelial fluid transport; IDA:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
DR GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; IDA:FlyBase.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:FlyBase.
DR InterPro; IPR013231; Periviscerokinin.
DR Pfam; PF08259; Periviscerokin; 2.
DR PROSITE; PS00539; PYROKININ; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..28
FT /id="PRO_0000029901"
FT PEPTIDE 31..42
FT /note="CAP-1"
FT /id="PRO_0000029902"
FT PROPEP 45..80
FT /id="PRO_0000029903"
FT PEPTIDE 83..92
FT /note="CAP-2"
FT /id="PRO_0000029904"
FT PROPEP 95..113
FT /id="PRO_0000029905"
FT PEPTIDE 116..130
FT /note="CAP-3"
FT /id="PRO_0000029906"
FT PROPEP 134..151
FT /id="PRO_0000029907"
FT MOD_RES 42
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
FT MOD_RES 92
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
FT MOD_RES 130
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
SQ SEQUENCE 151 AA; 16507 MW; F9E97535665B37E5 CRC64;
MKSMLVHIVL VIFIIAEFST AETDHDKNRR GANMGLYAFP RVGRSDPSLA NSLRDGLEAG
VLDGIYGDAS QEDYNEADFQ KKASGLVAFP RVGRGDAELR KWAHLLALQQ VLDKRTGPSA
SSGLWFGPRL GKRSVDAKSF ADISKGQKEL N
