ID   CYSP1_OSTOS             Reviewed;         341 AA.
AC   P25802;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 3.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Cathepsin B-like cysteine proteinase 1;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=CP-1;
OS   Ostertagia ostertagi (Brown stomach worm) (Strongylus ostertagi).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Trichostrongyloidea; Haemonchidae; Ostertagia.
OX   NCBI_TaxID=6317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Larva;
RX   PubMed=1475000; DOI=10.1016/0166-6851(92)90152-a;
RA   Pratt D., Boisvenue R.J., Cox G.N.;
RT   "Isolation of putative cysteine protease genes of Ostertagia ostertagi.";
RL   Mol. Biochem. Parasitol. 56:39-48(1992).
CC   -!- FUNCTION: Expression of the protease correlates with blood-feeding and
CC       suggests a role for the protease in blood digestion.
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; M88503; AAA29433.1; -; Genomic_DNA.
DR   EMBL; M88503; AAA29434.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M88504; AAA29435.1; -; Genomic_DNA.
DR   PIR; A48454; A48454.
DR   AlphaFoldDB; P25802; -.
DR   SMR; P25802; -.
DR   MEROPS; C01.101; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Signal; Thiol protease;
KW   Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..88
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026200"
FT   CHAIN           89..341
FT                   /note="Cathepsin B-like cysteine proteinase 1"
FT                   /id="PRO_0000026201"
FT   ACT_SITE        119
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        308
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        104..133
FT                   /evidence="ECO:0000250"
FT   DISULFID        116..160
FT                   /evidence="ECO:0000250"
FT   DISULFID        152..218
FT                   /evidence="ECO:0000250"
FT   DISULFID        153..156
FT                   /evidence="ECO:0000250"
FT   DISULFID        189..222
FT                   /evidence="ECO:0000250"
FT   DISULFID        197..209
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   341 AA;  38439 MW;  07968646E3D920F6 CRC64;
     MKYLFFALCL YLYQGISEAE VPAEQIPLEA QALSGLPLVE YLQKNQRLFE VTATPVPYFK
     QRLMDLKYID QNNIPDEEVE DEELEENNDD IPESYDPRIQ WANCSSLFHI PDQANCGSCW
     AVSSAAAMSD RICIASKGAK QVLISAQDVV SCCTWCGDGC EGGWPISAFR FHADEGVVTG
     GDYNTKGSCR PYEIHPCGHH GNETYYGECV GMADTPRCKR RCLLGYPKSY PSDRYYKKAY
     QLKNSVKAIQ KDIMKNGPVV ATYTVYEDFA HYRSGIYKHK AGRKTGLHAV KVIGWGEEKG
     TPYWIVANSW HDDWGENGFF RMHRGSNDCG FEERMAAGSV Q