ID   PVK2_EURFL              Reviewed;          12 AA.
AC   P84375; P84372;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   11-DEC-2019, entry version 28.
DE   RecName: Full=Periviscerokinin-2.1;
DE            Short=PVK-2.1;
DE   AltName: Full=Periviscerokinin-3;
DE            Short=EurFl-PVK-3;
DE   Contains:
DE     RecName: Full=Periviscerokinin-2.2;
DE              Short=PVK-2.2;
DE     AltName: Full=Periviscerokinin-2;
DE              Short=EurFl-PVK-2;
OS   Eurycotis floridana (Florida woods cockroach) (Skunk roach).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Blattidae;
OC   Polyzosteriinae; Eurycotis.
OX   NCBI_TaxID=303877;
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).
RN   [2]
RP   PROTEIN SEQUENCE, AND AMIDATION AT VAL-12.
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: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=1157.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15626499};
CC   -!- MASS SPECTROMETRY: [Periviscerokinin-2.2]: Mass=1070.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15626499};
CC   -!- SIMILARITY: Belongs to the periviscerokinin family. {ECO:0000255}.
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..12
FT                   /note="Periviscerokinin-2.1"
FT                   /id="PRO_0000023625"
FT   PEPTIDE         2..12
FT                   /note="Periviscerokinin-2.2"
FT                   /id="PRO_0000023626"
FT   MOD_RES         12
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:15626499,
FT                   ECO:0000269|PubMed:19257902"
SQ   SEQUENCE   12 AA;  1128 MW;  2F4D9FBE4EB05728 CRC64;
     GGSSGLISVP RV