ID   PVK2_DEREJ              Reviewed;          12 AA.
AC   P84379; P84430;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   11-DEC-2019, entry version 27.
DE   RecName: Full=Periviscerokinin-2.1;
DE            Short=PVK-2.1;
DE   Contains:
DE     RecName: Full=Periviscerokinin-2.2;
DE              Short=PVK-2.2;
OS   Deropeltis cf. erythrocephala JT-2004 (Cockroach).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Blattidae;
OC   Blattinae; Deropeltis.
OX   NCBI_TaxID=303919;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND AMIDATION AT VAL-12.
RC   TISSUE=Abdominal perisympathetic organs {ECO:0000269|PubMed:15626499};
RX   PubMed=15626499; DOI=10.1016/j.peptides.2004.10.010;
RA   Predel R., Gaede G.;
RT   "Peptidomics of neurohemal organs from species of the cockroach family
RT   Blattidae: how do neuropeptides of closely related species differ?";
RL   Peptides 26:3-9(2005).
CC   -!- FUNCTION: Mediates visceral muscle contractile activity (myotropic
CC       activity). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15626499}.
CC   -!- TISSUE SPECIFICITY: Abdominal perisympathetic organs.
CC       {ECO:0000269|PubMed:15626499}.
CC   -!- MASS SPECTROMETRY: [Periviscerokinin-2.1]: Mass=1159.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15626499};
CC   -!- MASS SPECTROMETRY: [Periviscerokinin-2.2]: Mass=1102.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15626499};
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..12
FT                   /note="Periviscerokinin-2.1"
FT                   /id="PRO_0000023619"
FT   PEPTIDE         2..12
FT                   /note="Periviscerokinin-2.2"
FT                   /id="PRO_0000023620"
FT   MOD_RES         12
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:15626499"
SQ   SEQUENCE   12 AA;  1160 MW;  2F4D9FAA1EB05728 CRC64;
     GGSSGLISMP RV