ID   CYSP1_HOMAM             Reviewed;         322 AA.
AC   P13277;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Digestive cysteine proteinase 1;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=LCP1;
OS   Homarus americanus (American lobster).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Nephropoidea; Nephropidae; Homarus.
OX   NCBI_TaxID=6706;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Digestive gland;
RX   PubMed=1959590; DOI=10.1016/0014-5793(91)80847-v;
RA   Laycock M.V., MacKay R.M., Di Fruscio M., Gallant J.W.;
RT   "Molecular cloning of three cDNAs that encode cysteine proteinases in the
RT   digestive gland of the American lobster (Homarus americanus).";
RL   FEBS Lett. 292:115-120(1991).
RN   [2]
RP   ERRATUM OF PUBMED:1959590.
RX   PubMed=1451782; DOI=10.1016/0014-5793(92)80227-8;
RA   Laycock M.V., MacKay R.M., Di Fruscio M., Gallant J.W.;
RL   FEBS Lett. 301:125-125(1992).
RN   [3]
RP   PROTEIN SEQUENCE OF 106-133.
RC   TISSUE=Digestive juice;
RX   PubMed=2597115; DOI=10.1042/bj2630439;
RA   Laycock M.V., Hirama T., Hasnain S., Watson D., Storer A.C.;
RT   "Purification and characterization of a digestive cysteine proteinase from
RT   the American lobster (Homarus americanus).";
RL   Biochem. J. 263:439-444(1989).
CC   -!- ACTIVITY REGULATION: Inhibited by E-64, antipain, leupeptin, heavy
CC       metal ions, iodoacetic acid, dithionitrobenzene, p-hydroxymercuri-
CC       benzoate; activated by mercaptoethanol and dithiothreitol.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC       ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   EMBL; X63567; CAA45127.1; -; mRNA.
DR   PIR; S19649; S19649.
DR   AlphaFoldDB; P13277; -.
DR   SMR; P13277; -.
DR   MEROPS; I29.003; -.
DR   PRIDE; P13277; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease; Signal;
KW   Thiol protease; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..105
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:2597115"
FT                   /id="PRO_0000026392"
FT   CHAIN           106..322
FT                   /note="Digestive cysteine proteinase 1"
FT                   /id="PRO_0000026393"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000250"
FT   DISULFID        126..170
FT                   /evidence="ECO:0000250"
FT   DISULFID        160..203
FT                   /evidence="ECO:0000250"
FT   DISULFID        262..311
FT                   /evidence="ECO:0000250"
FT   CONFLICT        114
FT                   /note="K -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   322 AA;  35498 MW;  EADCD4E3D31291E9 CRC64;
     MKVVALFLFG LALAAANPSW EEFKGKFGRK YVDLEEERYR LNVFLDNLQY IEEFNKKYER
     GEVTYNLAIN QFSDMTNEKF NAVMKGYKKG PRPAAVFTST DAAPESTEVD WRTKGAVTPV
     KDQGQCGSCW AFSTTGGIEG QHFLKTGRLV SLSEQQLVDC AGGSYYNQGC NGGWVERAIM
     YVRDNGGVDT ESSYPYEARD NTCRFNSNTI GATCTGYVGI AQGSESALKT ATRDIGPISV
     AIDASHRSFQ SYYTGVYYEP SCSSSQLDHA VLAVGYGSEG GQDFWLVKNS WATSWGESGY
     IKMARNRNNN CGIATDACYP TV