ID   PVK2_NAUCI              Reviewed;          11 AA.
AC   P83927; P82699;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 1.
DT   11-DEC-2019, entry version 30.
DE   RecName: Full=Periviscerokinin-2;
DE            Short=PVK-2;
OS   Nauphoeta cinerea (Cinereous cockroach) (Gray cockroach).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Blaberidae;
OC   Oxyhaloinae; Nauphoeta.
OX   NCBI_TaxID=6990;
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).
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}.
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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_0000044265"
FT   MOD_RES         11
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:10849006"
SQ   SEQUENCE   11 AA;  1103 MW;  2F4D9FFD85B05728 CRC64;
     GSSGLISMPR V