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Cardio acceleratory peptide 2b (Capability protein) (Myotropin-CAP2b-like protein) [Cleaved into: CAP-1 (CAP2b-1) (Capa-1); CAP-2 (CAP2b-2) (Capa-2); CAP-3 (CAP2b-3) (Capa-3) (Myotropin) (Pyrokinin-1)]

 CP2B_DROME              Reviewed;         151 AA.
Q9NIP6; Q9VAE2;
17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
05-JUL-2017, entry version 108.
RecName: Full=Cardio acceleratory peptide 2b;
AltName: Full=Capability protein;
AltName: Full=Myotropin-CAP2b-like protein;
Contains:
RecName: Full=CAP-1;
AltName: Full=CAP2b-1;
AltName: Full=Capa-1;
Contains:
RecName: Full=CAP-2;
AltName: Full=CAP2b-2;
AltName: Full=Capa-2;
Contains:
RecName: Full=CAP-3;
AltName: Full=CAP2b-3;
AltName: Full=Capa-3;
AltName: Full=Myotropin;
AltName: Full=Pyrokinin-1;
Flags: Precursor;
Name=Capa; Synonyms=MT-CAP2b; ORFNames=CG15520;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=11959669; DOI=10.1152/ajpregu.00584.2001;
Kean L., Cazenave W., Costes L., Broderick K.E., Graham S.,
Pollock V.P., Davies S.A., Veenstra J.A., Dow J.A.;
"Two nitridergic peptides are encoded by the gene capability in
Drosophila melanogaster.";
Am. J. Physiol. 282:R1297-R1307(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Vanden Broeck J.J.M.;
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
PROTEIN SEQUENCE OF 31-42 AND 83-92, AND AMIDATION AT VAL-42; VAL-92
AND LEU-130.
TISSUE=Larva;
PubMed=12171930; DOI=10.1074/jbc.M206257200;
Baggerman G., Cerstiaens A., De Loof A., Schoofs L.;
"Peptidomics of the larval Drosophila melanogaster central nervous
system.";
J. Biol. Chem. 277:40368-40374(2002).
[7]
FUNCTION.
STRAIN=Canton-S;
PubMed=12177421; DOI=10.1073/pnas.162276199;
Park Y., Kim Y.-J., Adams M.E.;
"Identification of G protein-coupled receptors for Drosophila PRXamide
peptides, CCAP, corazonin, and AKH supports a theory of ligand-
receptor coevolution.";
Proc. Natl. Acad. Sci. U.S.A. 99:11423-11428(2002).
[8]
FUNCTION.
PubMed=12459185; DOI=10.1016/S0006-291X(02)02709-2;
Iversen A., Cazzamali G., Williamson M., Hauser F.,
Grimmelikhuijzen C.J.P.;
"Molecular cloning and functional expression of a Drosophila receptor
for the neuropeptides capa-1 and -2.";
Biochem. Biophys. Res. Commun. 299:628-633(2002).
[9]
REVIEW.
PubMed=11179818; DOI=10.1016/S0196-9781(00)00376-4;
Vanden Broeck J.J.M.;
"Neuropeptides and their precursors in the fruitfly, Drosophila
melanogaster.";
Peptides 22:241-254(2001).
[10]
FUNCTION.
PubMed=16054112; DOI=10.1016/j.bbrc.2005.07.038;
Cazzamali G., Torp M., Hauser F., Williamson M.,
Grimmelikhuijzen C.J.;
"The Drosophila gene CG9918 codes for a pyrokinin-1 receptor.";
Biochem. Biophys. Res. Commun. 33:14-19(2005).
-!- FUNCTION: CAP-1 and CAP-2, but not CAP-3 are ligands for the Capa
receptor (PubMed:12177421, PubMed:12459185). CAP-1 and CAP-2 are
probably components of the signal transduction pathway that leads
to Malpighian tubule fluid secretion via the second messenger
nitric oxide (PubMed:11959669). CAP-3 is a ligand for the PK1-R G-
protein coupled receptor (PubMed:16054112).
{ECO:0000269|PubMed:11959669, ECO:0000269|PubMed:12177421,
ECO:0000269|PubMed:12459185, ECO:0000269|PubMed:16054112}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11959669}.
Note=Released from the neuroendocrine cells into the hemolymph.
-!- TISSUE SPECIFICITY: In larvae, the precursor peptide is
exclusively present in a single pair of neuroendocrine cells in
the labial neuromere (subesophageal ganglion) and three pairs of
cells in the ventral ganglion abdominal neuromeres.
{ECO:0000269|PubMed:11959669}.
-!- SIMILARITY: Belongs to the pyrokinin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF203878; AAF62876.1; -; mRNA.
EMBL; AJ291724; CAC17603.1; -; mRNA.
EMBL; AE014297; AAF56969.2; -; Genomic_DNA.
EMBL; AY069234; AAL39379.1; -; mRNA.
RefSeq; NP_524552.1; NM_079828.3.
UniGene; Dm.2221; -.
ProteinModelPortal; Q9NIP6; -.
BioGrid; 68398; 4.
DIP; DIP-22273N; -.
IntAct; Q9NIP6; 1.
MINT; MINT-783841; -.
STRING; 7227.FBpp0084880; -.
PaxDb; Q9NIP6; -.
PRIDE; Q9NIP6; -.
EnsemblMetazoa; FBtr0085514; FBpp0084880; FBgn0039722.
GeneID; 43541; -.
KEGG; dme:Dmel_CG15520; -.
CTD; 43541; -.
FlyBase; FBgn0039722; Capa.
eggNOG; ENOG410J786; Eukaryota.
eggNOG; ENOG410Y3PV; LUCA.
InParanoid; Q9NIP6; -.
OMA; YNEADFQ; -.
OrthoDB; EOG091G16SI; -.
PhylomeDB; Q9NIP6; -.
GenomeRNAi; 43541; -.
PRO; PR:Q9NIP6; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0039722; -.
ExpressionAtlas; Q9NIP6; differential.
Genevisible; Q9NIP6; DM.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:FlyBase.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0008613; F:diuretic hormone activity; IDA:FlyBase.
GO; GO:0016084; F:myostimulatory hormone activity; IMP:UniProtKB.
GO; GO:0005184; F:neuropeptide hormone activity; IMP:UniProtKB.
GO; GO:0071855; F:neuropeptide receptor binding; IPI:FlyBase.
GO; GO:0005102; F:receptor binding; ISS:FlyBase.
GO; GO:0006812; P:cation transport; TAS:FlyBase.
GO; GO:0042045; P:epithelial fluid transport; IDA:FlyBase.
GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; IDA:FlyBase.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:FlyBase.
PROSITE; PS00539; PYROKININ; 1.
1: Evidence at protein level;
Amidation; Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Neuropeptide; Reference proteome; Secreted;
Signal.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 28
/FTId=PRO_0000029901.
PEPTIDE 31 42 CAP-1.
/FTId=PRO_0000029902.
PROPEP 45 80
/FTId=PRO_0000029903.
PEPTIDE 83 92 CAP-2.
/FTId=PRO_0000029904.
PROPEP 95 113
/FTId=PRO_0000029905.
PEPTIDE 116 130 CAP-3.
/FTId=PRO_0000029906.
PROPEP 134 151
/FTId=PRO_0000029907.
MOD_RES 42 42 Valine amide.
{ECO:0000269|PubMed:12171930}.
MOD_RES 92 92 Valine amide.
{ECO:0000269|PubMed:12171930}.
MOD_RES 130 130 Leucine amide.
{ECO:0000269|PubMed:12171930}.
SEQUENCE 151 AA; 16507 MW; F9E97535665B37E5 CRC64;
MKSMLVHIVL VIFIIAEFST AETDHDKNRR GANMGLYAFP RVGRSDPSLA NSLRDGLEAG
VLDGIYGDAS QEDYNEADFQ KKASGLVAFP RVGRGDAELR KWAHLLALQQ VLDKRTGPSA
SSGLWFGPRL GKRSVDAKSF ADISKGQKEL N


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