CYSP_SCHJA
ID CYSP_SCHJA Reviewed; 342 AA.
AC P43157;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Cathepsin B-like cysteine proteinase;
DE EC=3.4.22.-;
DE AltName: Full=Antigen Sj31;
DE Flags: Precursor;
GN Name=CATB;
OS Schistosoma japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Chinese;
RX PubMed=7899786;
RA Merckelbach A., Hasse S., Dell R., Eschlbeck A., Ruppel A.;
RT "cDNA sequences of Schistosoma japonicum coding for two cathepsin B-like
RT proteins and Sj32.";
RL Trop. Med. Parasitol. 45:193-198(1994).
CC -!- FUNCTION: Thiol protease. Has a role as a digestive enzyme.
CC -!- TISSUE SPECIFICITY: Intestine (gut).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X70968; CAA50305.1; -; mRNA.
DR PIR; S31907; S31907.
DR AlphaFoldDB; P43157; -.
DR SMR; P43157; -.
DR MEROPS; C01.062; -.
DR PRIDE; P43157; -.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro.
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; IPR012599; Propeptide_C1A.
DR Pfam; PF00112; Peptidase_C1; 1.
DR Pfam; PF08127; Propeptide_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; Hydrolase; Protease; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..89
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026170"
FT CHAIN 90..342
FT /note="Cathepsin B-like cysteine proteinase"
FT /id="PRO_0000026171"
FT ACT_SITE 118
FT /evidence="ECO:0000250"
FT ACT_SITE 288
FT /evidence="ECO:0000250"
FT ACT_SITE 308
FT /evidence="ECO:0000250"
FT DISULFID 103..132
FT /evidence="ECO:0000250"
FT DISULFID 115..159
FT /evidence="ECO:0000250"
FT DISULFID 151..217
FT /evidence="ECO:0000250"
FT DISULFID 152..155
FT /evidence="ECO:0000250"
FT DISULFID 188..221
FT /evidence="ECO:0000250"
FT DISULFID 196..207
FT /evidence="ECO:0000250"
SQ SEQUENCE 342 AA; 38796 MW; 81BA89CD61A68B4C CRC64;
MLKIAVYIVS LFTFLEAHVT TRNNQRIEPL SDEMISFINE HPDAGWKADK SDRFHSLDDA
RILMGARKED AEMKRNRRPT VDHHDLNVEI PSQFDSRKKW PHCKSISQIR DQSRCGSCWA
FGAVEAMTDR ICIQSGGGQS AELSALDLIS CCKDCGDGCQ GGFPGVAWDY WVKRGIVTGG
SKENHTGCQP YPFPKCEHHT KGKYPACGTK IYKTPQCKQT CQKGYKTPYE QDKHYGDESY
NVQNNEKVIQ RDIMMYGPVE AAFDVYEDFL NYKSGIYRHV TGSIVGGHAI RIIGWGVEKR
TPYWLIANSW NEDWGEKGLF RMVRGRDECS IESDVVAGLI KT