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CP2B_DROPS
ID   CP2B_DROPS              Reviewed;         155 AA.
AC   Q29CA0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 55.
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   Contains:
DE     RecName: Full=CAP-2;
DE   Contains:
DE     RecName: Full=CAP-3;
DE     AltName: Full=Pyrokinin-1;
DE   Flags: Precursor;
GN   Name=capa {ECO:0000250|UniProtKB:Q9NIP6}; ORFNames=GA13779;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: CAP-1 and CAP-2, but not CAP-3 are ligands for the Capa
CC       receptor. CAP-1 and CAP-2 are probably components of the signal
CC       transduction pathway that leads to Malpighian tubule fluid secretion
CC       via the second messenger nitric oxide (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NIP6}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9NIP6}.
CC   -!- SIMILARITY: Belongs to the pyrokinin family. {ECO:0000255}.
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DR   EMBL; CM000070; EAL26746.2; -; Genomic_DNA.
DR   RefSeq; XP_001357612.2; XM_001357575.3.
DR   AlphaFoldDB; Q29CA0; -.
DR   STRING; 7237.FBpp0282948; -.
DR   EnsemblMetazoa; FBtr0284510; FBpp0282948; FBgn0073815.
DR   GeneID; 4800261; -.
DR   KEGG; dpo:Dpse_GA13779; -.
DR   eggNOG; ENOG502TAG0; Eukaryota.
DR   HOGENOM; CLU_1697372_0_0_1; -.
DR   InParanoid; Q29CA0; -.
DR   OMA; SMLVHIV; -.
DR   Proteomes; UP000001819; Chromosome 2.
DR   Bgee; FBgn0073815; Expressed in insect adult head.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0016084; F:myostimulatory hormone activity; ISS:UniProtKB.
DR   GO; GO:0005184; F:neuropeptide hormone activity; ISS:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR013231; Periviscerokinin.
DR   Pfam; PF08259; Periviscerokin; 1.
DR   PROSITE; PS00539; PYROKININ; 1.
PE   3: Inferred from homology;
KW   Amidation; Cleavage on pair of basic residues; Neuropeptide;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..33
FT                   /evidence="ECO:0000250|UniProtKB:Q9NIP6"
FT                   /id="PRO_0000339244"
FT   PEPTIDE         36..47
FT                   /note="CAP-1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NIP6"
FT                   /id="PRO_0000339245"
FT   PROPEP          50..85
FT                   /evidence="ECO:0000250|UniProtKB:Q9NIP6"
FT                   /id="PRO_0000339246"
FT   PEPTIDE         88..96
FT                   /note="CAP-2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NIP6"
FT                   /id="PRO_0000339247"
FT   PROPEP          99..117
FT                   /evidence="ECO:0000250|UniProtKB:Q9NIP6"
FT                   /id="PRO_0000339248"
FT   PEPTIDE         120..134
FT                   /note="CAP-3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NIP6"
FT                   /id="PRO_0000339249"
FT   PROPEP          138..155
FT                   /evidence="ECO:0000250|UniProtKB:Q9NIP6"
FT                   /id="PRO_0000339250"
FT   MOD_RES         47
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NIP6"
FT   MOD_RES         96
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NIP6"
FT   MOD_RES         134
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NIP6"
SQ   SEQUENCE   155 AA;  16958 MW;  4572C392A8F91481 CRC64;
     MKAIFSLYNI VSAILLLVLL AEFSTAELNH DKNRRGANMG LYAFPRVGRS DPSLANSLRD
     ASDAAVFDGL YGDASQEDYN EADYQKRAGL VAFPRVGRSD AELRKFAHLL ALQQVLDKRT
     GPSASSGLWF GPRLGKRSVD AKAFSDASKG QQEFN
 
 
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