PVK2_BLADU
ID PVK2_BLADU Reviewed; 11 AA.
AC P83929; P82699;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 11-DEC-2019, entry version 33.
DE RecName: Full=Periviscerokinin-2;
DE Short=BlaDu-PVK-2;
DE Short=PVK-2;
OS Blaptica dubia (Argentinian wood cockroach).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Blaberidae;
OC Blaberinae; Blaptica.
OX NCBI_TaxID=132935;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND AMIDATION AT VAL-11.
RC TISSUE=Abdominal perisympathetic organs;
RX PubMed=10849006; DOI=10.1046/j.1432-1327.2000.01425.x;
RA Predel R., Kellner R., Baggerman G., Steinmetzer T., Schoofs L.;
RT "Identification of novel periviscerokinins from single neurohaemal release
RT sites in insects. MS/MS fragmentation complemented by Edman degradation.";
RL Eur. J. Biochem. 267:3869-3873(2000).
RN [2]
RP PROTEIN SEQUENCE, AND AMIDATION AT VAL-11.
RC TISSUE=Abdominal perisympathetic organs;
RX PubMed=19257902; DOI=10.1186/1471-2148-9-50;
RA Roth S., Fromm B., Gaede G., Predel R.;
RT "A proteomic approach for studying insect phylogeny: CAPA peptides of
RT ancient insect taxa (Dictyoptera, Blattoptera) as a test case.";
RL BMC Evol. Biol. 9:50-50(2009).
CC -!- FUNCTION: Mediates visceral muscle contractile activity (myotropic
CC activity). {ECO:0000269|PubMed:10849006}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MASS SPECTROMETRY: Mass=1102.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10849006};
CC -!- SIMILARITY: Belongs to the periviscerokinin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR013231; Periviscerokinin.
DR Pfam; PF08259; Periviscerokin; 1.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Neuropeptide; Secreted.
FT PEPTIDE 1..11
FT /note="Periviscerokinin-2"
FT /id="PRO_0000044255"
FT MOD_RES 11
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:10849006,
FT ECO:0000269|PubMed:19257902"
SQ SEQUENCE 11 AA; 1103 MW; 2F4D9FFD85B05728 CRC64;
GSSGLISMPR V