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Q9NIP6 (CP2B_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cardio acceleratory peptide 2b
Alternative name(s):
Capability protein
Myotropin-CAP2b-like protein

Cleaved into the following 3 chains:

  1. CAP-1
    Alternative name(s):
    CAP2b-1
    Capa-1
  2. CAP-2
    Alternative name(s):
    CAP2b-2
    Capa-2
  3. CAP-3
    Alternative name(s):
    CAP2b-3
    Capa-3
    Myotropin
    Pyrokinin-1
Gene names
Name:capa
Synonyms:MT-CAP2b
ORF Names:CG15520
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

CAP-1 and CAP-2, but not CAP-3 are ligands for the Capa receptor. 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. CAP-3 may be a ligand for the CG8795 G protein coupled receptors. Ref.1 Ref.7 Ref.8

Subcellular location

Secreted. Note: Released from the neuroendocrine cells into the hemolymph. Ref.1

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. Ref.1

Sequence similarities

Belongs to the pyrokinin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG7191Q9VLX61EBI-155503,EBI-121750

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 287
PRO_0000029901
Peptide31 – 4212CAP-1 Ref.6
PRO_0000029902
Propeptide45 – 8036
PRO_0000029903
Peptide83 – 9210CAP-2
PRO_0000029904
Propeptide95 – 11319
PRO_0000029905
Peptide116 – 13015CAP-3
PRO_0000029906
Propeptide134 – 15118
PRO_0000029907

Amino acid modifications

Modified residue421Valine amide
Modified residue921Valine amide
Modified residue1301Leucine amide

Sequences

Sequence LengthMass (Da)Tools
Q9NIP6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F9E97535665B37E5

FASTA15116,507
        10         20         30         40         50         60 
MKSMLVHIVL VIFIIAEFST AETDHDKNRR GANMGLYAFP RVGRSDPSLA NSLRDGLEAG 

        70         80         90        100        110        120 
VLDGIYGDAS QEDYNEADFQ KKASGLVAFP RVGRGDAELR KWAHLLALQQ VLDKRTGPSA 

       130        140        150 
SSGLWFGPRL GKRSVDAKSF ADISKGQKEL N 

« Hide

References

« Hide 'large scale' references
[1]"Two nitridergic peptides are encoded by the gene capability in Drosophila melanogaster."
Kean L., Cazenave W., Costes L., Broderick K.E., Graham S., Pollock V.P., Davies S.A., Veenstra J.A., Dow J.A.
Am. J. Physiol. 282:R1297-R1307(2002) [PubMed: 11959669] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]Vanden Broeck J.J.M.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , 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.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
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.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[6]"Peptidomics of the larval Drosophila melanogaster central nervous system."
Baggerman G., Cerstiaens A., De Loof A., Schoofs L.
J. Biol. Chem. 277:40368-40374(2002) [PubMed: 12171930] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-42 AND 83-92, AMIDATION.
Tissue: Larva.
[7]"Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution."
Park Y., Kim Y.-J., Adams M.E.
Proc. Natl. Acad. Sci. U.S.A. 99:11423-11428(2002) [PubMed: 12177421] [Abstract]
Cited for: FUNCTION.
Strain: Canton-S.
[8]"Molecular cloning and functional expression of a Drosophila receptor for the neuropeptides capa-1 and -2."
Iversen A., Cazzamali G., Williamson M., Hauser F., Grimmelikhuijzen C.J.P.
Biochem. Biophys. Res. Commun. 299:628-633(2002) [PubMed: 12459185] [Abstract]
Cited for: FUNCTION.
[9]"Neuropeptides and their precursors in the fruitfly, Drosophila melanogaster."
Vanden Broeck J.J.M.
Peptides 22:241-254(2001) [PubMed: 11179818] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF203878 mRNA. Translation: AAF62876.1.
AJ291724 mRNA. Translation: CAC17603.1.
AE014297 Genomic DNA. Translation: AAF56969.2.
AY069234 mRNA. Translation: AAL39379.1.
RefSeqNP_524552.1. NM_079828.2.
UniGeneDm.2221.

3D structure databases

ProteinModelPortalQ9NIP6.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-22273N.
IntActQ9NIP6. 1 interaction.
MINTMINT-783841.
STRINGQ9NIP6.

Proteomic databases

PRIDEQ9NIP6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085514; FBpp0084880; FBgn0039722.
GeneID43541.
KEGGdme:Dmel_CG15520.
NMPDRfig|7227.3.peg.15331.

Organism-specific databases

CTD43541.
FlyBaseFBgn0039722. capa.

Phylogenomic databases

eggNOGinNOG11760.
GeneTreeEMGT00050000017710.
InParanoidQ9NIP6.
OMAKNRRGAN.
OrthoDBEOG48SF9H.
PhylomeDBQ9NIP6.

Gene expression databases

BgeeQ9NIP6.
GermOnlineCG15520. Drosophila melanogaster.

Family and domain databases

PROSITEPS00539. PYROKININ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio834452.

Entry information

Entry nameCP2B_DROME
AccessionPrimary (citable) accession number: Q9NIP6
Secondary accession number(s): Q9VAE2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families