ID   CATB2_GIAIN             Reviewed;         300 AA.
AC   P92132; Q9GP24;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Cathepsin B-like CP2;
DE            EC=3.4.22.-;
DE   AltName: Full=Cathepsin B-like protease B2;
DE   Flags: Precursor;
GN   Name=CP2;
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30957 / WB;
RX   PubMed=11849701; DOI=10.1016/s0166-6851(01)00438-8;
RA   Sajid M., McKerrow J.H.;
RT   "Cysteine proteases of parasitic organisms.";
RL   Mol. Biochem. Parasitol. 120:1-21(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-268, PROTEIN SEQUENCE OF 71-84,
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=ATCC 30957 / WB;
RX   PubMed=9150143; DOI=10.1016/s0092-8674(00)80224-x;
RA   Ward W., Alvarado L., Rawlings N.D., Engel J.C., Franklin C.,
RA   McKerrow J.H.;
RT   "A primitive enzyme for a primitive cell: the protease required for
RT   excystation of Giardia.";
RL   Cell 89:437-444(1997).
CC   -!- FUNCTION: Thiol protease which is required for parasite excystation and
CC       invasion of the proximal small intestine of the human host.
CC       {ECO:0000269|PubMed:9150143}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:9150143}.
CC   -!- DEVELOPMENTAL STAGE: To initiate infection, trophozoites emerge from a
CC       cyst in the host. Excystation is blocked by specific cysteine protease
CC       inhibitors. Vacuoles release it just prior to excystation. Expressed in
CC       replicating and encysting trophozoites without supplemental iron.
CC       {ECO:0000269|PubMed:9150143}.
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; AJ302012; CAC18647.1; -; Genomic_DNA.
DR   EMBL; U83276; AAB58259.1; -; Genomic_DNA.
DR   AlphaFoldDB; P92132; -.
DR   SMR; P92132; -.
DR   MEROPS; C01.094; -.
DR   VEuPathDB; GiardiaDB:DHA2_14019; -.
DR   VEuPathDB; GiardiaDB:GL50581_78; -.
DR   VEuPathDB; GiardiaDB:GL50803_0014019; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease; Signal;
KW   Thiol protease; Vacuole; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..?
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026166"
FT   CHAIN           ?..300
FT                   /note="Cathepsin B-like CP2"
FT                   /id="PRO_0000026167"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000250"
FT   DISULFID        88..115
FT                   /evidence="ECO:0000250"
FT   DISULFID        98..141
FT                   /evidence="ECO:0000250"
FT   DISULFID        134..177
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   300 AA;  33002 MW;  4D82C5DFE861636F CRC64;
     MKLFLLAAAA FSAPALTVSE LNHIKSLNPR WKAGIPKRFE GLTKDEISSL LMPVSFLKNA
     KGAAPRGTFT DKDDVPESFD FREEYPHCIP EVVDQGGCGS CWAFSSVATF GDRRCVAGLD
     KKPVKYSPQY VVSCDHGDMA CNGGWLPNVW KFLTKTGTTT DECVPYKSGS TTLRGTCPTK
     CADGSSKVHL ATATSYKDYG LDIPAMMKAL STSGPLQVAF LVHSDFMYYE SGVYQHTYGY
     MEGGHAVEMV GYGTDDDGVD YWIIKNSWGP DWGEDGYFRM IRGINDCSIE EQAYAGFFDE