ID   PRCT_CARMA              Reviewed;           5 AA.
AC   P67857; P01373;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Proctolin;
OS   Carcinus maenas (Common shore crab) (Green crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Portunoidea; Carcinidae; Carcinus.
OX   NCBI_TaxID=6759;
RN   [1]
RP   PROTEIN SEQUENCE, AND TISSUE SPECIFICITY.
RX   PubMed=2872661; DOI=10.1016/0196-9781(86)90063-x;
RA   Stangier J., Dircksen H., Keller R.;
RT   "Identification and immunocytochemical localization of proctolin in
RT   pericardial organs of the shore crab, Carcinus maenas.";
RL   Peptides 7:67-72(1986).
RN   [2]
RP   FUNCTION, AND SYNTHESIS.
RC   TISSUE=Venom;
RX   PubMed=26056922; DOI=10.1016/j.peptides.2015.05.013;
RA   Duzzi B., Cajado-Carvalho D., Kuniyoshi A.K., Kodama R.T., Gozzo F.C.,
RA   Fioramonte M., Tambourgi D.V., Portaro F.V., Rioli V.;
RT   "[des-Arg(1)]-proctolin: a novel NEP-like enzyme inhibitor identified in
RT   Tityus serrulatus venom.";
RL   Peptides 80:18-24(2016).
CC   -!- FUNCTION: Stimulates cardiac output and hindgut motility, modulates
CC       visceral and skeletal muscle in many arthropods. Also inhibits
CC       activities of the human peptidase neprilysin (NEP/MME)
CC       (PubMed:26056922). {ECO:0000269|PubMed:26056922}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Found in the crab pericardial organs.
CC       {ECO:0000269|PubMed:2872661}.
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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Neuropeptide; Protease; Secreted;
KW   Serine protease.
FT   PEPTIDE         1..5
FT                   /note="Proctolin"
FT                   /evidence="ECO:0000269|PubMed:2872661"
FT                   /id="PRO_0000044209"
SQ   SEQUENCE   5 AA;  649 MW;  71B7673B44600000 CRC64;
     RYLPT