ID   COCO_LIMPO              Reviewed;          14 AA.
AC   P35586;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Cocoonase;
DE            EC=3.4.21.-;
DE   Flags: Fragment;
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=335821; DOI=10.1002/9780470122907.ch5;
RA   Law J.H., Dunn P.E., Kramer K.J.;
RT   "Insect proteases and peptidases.";
RL   Adv. Enzymol. Relat. Areas Mol. Biol. 45:389-425(1977).
CC   -!- FUNCTION: Protease that shows preferential cleavage after Arg and Lys
CC       residues.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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   MEROPS; S01.112; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease.
FT   CHAIN           1..>14
FT                   /note="Cocoonase"
FT                   /id="PRO_0000088682"
FT   DOMAIN          1..>14
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         14
SQ   SEQUENCE   14 AA;  1452 MW;  1615FB1D73747570 CRC64;
     IVGGFTIGID TVPY