ID   CYSP1_HAECO             Reviewed;         342 AA.
AC   P19092;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Cathepsin B-like cysteine proteinase 1;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=AC-1;
OS   Haemonchus contortus (Barber pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Trichostrongyloidea; Haemonchidae; Haemonchus.
OX   NCBI_TaxID=6289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Isolate BPL1;
RX   PubMed=2385265; DOI=10.1016/0166-6851(90)90093-2;
RA   Cox G.N., Pratt D., Hageman R., Boisvenue R.J.;
RT   "Molecular cloning and primary sequence of a cysteine protease expressed by
RT   Haemonchus contortus adult worms.";
RL   Mol. Biochem. Parasitol. 41:25-34(1990).
CC   -!- FUNCTION: Expression of the protease correlates with blood-feeding and
CC       suggests a role for the protease in blood digestion.
CC   -!- DEVELOPMENTAL STAGE: At low level in the third and fourth-stage larvae,
CC       and abundant in adult worms.
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; M31112; AAA29175.1; -; mRNA.
DR   PIR; A45524; A45524.
DR   AlphaFoldDB; P19092; -.
DR   SMR; P19092; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Signal; Thiol protease;
KW   Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..86
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026186"
FT   CHAIN           87..342
FT                   /note="Cathepsin B-like cysteine proteinase 1"
FT                   /id="PRO_0000026187"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        285
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        100..128
FT                   /evidence="ECO:0000250"
FT   DISULFID        111..156
FT                   /evidence="ECO:0000250"
FT   DISULFID        147..214
FT                   /evidence="ECO:0000250"
FT   DISULFID        148..152
FT                   /evidence="ECO:0000250"
FT   DISULFID        185..218
FT                   /evidence="ECO:0000250"
FT   DISULFID        193..205
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   342 AA;  38460 MW;  D33D62F7419F0471 CRC64;
     MKYLVLALCT YLCSQTGADE NAAQGIPLEA QRLTGEPLVA YLRRSQNLFE VNSAPTPNFE
     QKIMDIKYKH QKLNLMVKED PDPEVDIPPS YDPRDVWKNC TTFYIRDQAN CGSCWAVSTA
     AAISDRICIA SKAEKQVNIS ATDIMTCCRP QCGDGCEGGW PIEAWKYFIY DGVVSGGEYL
     TKDVCRPYPI HPCGHHGNDT YYGECRGTAP TPPCKRKCRP GVRKMYRIDK RYGKDAYIVK
     QSVKAIQSEI LRNGPVVASF AVYEDFRHYK SGIYKHTAGE LRGYHAVKMI GWGNENNTDF
     WLIANSWHND WGEKGYFRII RGTNDCGIEG TIAAGIVDTE SL