ID   CYSP3_HOMAM             Reviewed;         321 AA.
AC   P25784;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Digestive cysteine proteinase 3;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=LCP3;
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).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA45129.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X63569; CAA45129.1; ALT_INIT; mRNA.
DR   PIR; S19651; S19651.
DR   AlphaFoldDB; P25784; -.
DR   SMR; P25784; -.
DR   MEROPS; I29.003; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Protease; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..106
FT                   /note="Activation peptide"
FT                   /id="PRO_0000026396"
FT   CHAIN           107..321
FT                   /note="Digestive cysteine proteinase 3"
FT                   /id="PRO_0000026397"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000250"
FT   DISULFID        127..170
FT                   /evidence="ECO:0000250"
FT   DISULFID        161..203
FT                   /evidence="ECO:0000250"
FT   DISULFID        261..310
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  35366 MW;  72D202DBFEC787AD CRC64;
     MKVAALFLCG LALATASPSW DHFKTQYGRK YGDAKEELYR QRVFQQNEQL IEDFNKKFEN
     GEVTFKVAMN QFGDMTNEEF NAVMKGYKKG SRGEPKAVFT AEAGPMAADV DWRTKALVTP
     VKDQEQCGSC WAFSATGALE GQHFLKNDEL VSLSEQQLVD CSTDYGNDGC GGGWMTSAFD
     YIKDNGGIDT ESSYPYEAED RSCRFDANSI GAICTGSVEV QHTEEALQEA VSGVGPISVA
     IDASHFSFQF YSSGVYYEQN CSPTFLDHGV LAVGYGTEST KDYWLVKNSW GSSWGDAGYI
     KMSRNRDNNC GIASEPSYPT V