ID   CYSP2_HOMAM             Reviewed;         323 AA.
AC   P25782;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Digestive cysteine proteinase 2;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=LCP2;
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}.
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DR   EMBL; X63568; CAA45128.1; -; mRNA.
DR   PIR; S19650; S19650.
DR   AlphaFoldDB; P25782; -.
DR   SMR; P25782; -.
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..107
FT                   /note="Activation peptide"
FT                   /id="PRO_0000026394"
FT   CHAIN           108..323
FT                   /note="Digestive cysteine proteinase 2"
FT                   /id="PRO_0000026395"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250"
FT   DISULFID        128..171
FT                   /evidence="ECO:0000250"
FT   DISULFID        162..204
FT                   /evidence="ECO:0000250"
FT   DISULFID        263..312
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   323 AA;  35401 MW;  1AD93FC73C6E9831 CRC64;
     MKVAVLFLCG VALAAASPSW EHFKGKYGRQ YVDAEEDSYR RVIFEQNQKY IEEFNKKYEN
     GEVTFNLAMN KFGDMTLEEF NAVMKGNIPR RSAPVSVFYP KKETGPQATE VDWRTKGAVT
     PVKDQGQCGS CWAFSTTGSL EGQHFLKTGS LISLAEQQLV DCSRPYGPQG CNGGWMNDAF
     DYIKANNGID TEAAYPYEAR DGSCRFDSNS VAATCSGHTN IASGSETGLQ QAVRDIGPIS
     VTIDAAHSSF QFYSSGVYYE PSCSPSYLDH AVLAVGYGSE GGQDFWLVKN SWATSWGDAG
     YIKMSRNRNN NCGIATVASY PLV