ID   PVK1_PILDU              Reviewed;          11 AA.
AC   P85734;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 12.
DE   RecName: Full=Periviscerokinin-1 {ECO:0000303|PubMed:19257902};
DE            Short=PilDu-PVK-1 {ECO:0000303|PubMed:19257902};
OS   Pilema dubia (Cockroach) (Pilema reflexa).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Blaberidae;
OC   Perisphaerinae; Pilema.
OX   NCBI_TaxID=521525;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND AMIDATION AT THR-11.
RC   TISSUE=Abdominal perisympathetic organs {ECO:0000269|PubMed:19257902};
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:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the periviscerokinin family. {ECO:0000255}.
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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-1"
FT                   /evidence="ECO:0000269|PubMed:19257902"
FT                   /id="PRO_0000378763"
FT   MOD_RES         11
FT                   /note="Threonine amide"
FT                   /evidence="ECO:0000269|PubMed:19257902"
SQ   SEQUENCE   11 AA;  1105 MW;  2AF680E2D7605728 CRC64;
     GSTGLIPFGR T