PRCT_LIMPO
ID PRCT_LIMPO Reviewed; 5 AA.
AC P67858; P01373;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Proctolin;
OS Limulus polyphemus (Atlantic horseshoe crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC Xiphosura; Limulidae; Limulus.
OX NCBI_TaxID=6850;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2356151; DOI=10.1016/0196-9781(90)90072-d;
RA Groome J.R., Tillinghast E.K., Townley M.A., Vetrovs A., Watson W.H. III,
RA Hunt D.F., Griffin P.R., Alexander J.E., Shabanowitz J.;
RT "Identification of proctolin in the central nervous system of the horseshoe
RT crab, Limulus polyphemus.";
RL Peptides 11:205-211(1990).
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.
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DR PIR; A60411; A60411.
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:2356151"
FT /id="PRO_0000044210"
SQ SEQUENCE 5 AA; 649 MW; 71B7673B44600000 CRC64;
RYLPT