ID G7N0H2_MACMU Unreviewed; 339 AA.
AC G7N0H2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Cathepsin B {ECO:0000256|ARBA:ARBA00015559};
DE EC=3.4.22.1 {ECO:0000256|ARBA:ARBA00012537};
GN ORFNames=EGK_18679 {ECO:0000313|EMBL:EHH28274.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH28274.1};
RN [1] {ECO:0000313|EMBL:EHH28274.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH28274.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule
CC substrates (thus differing from cathepsin L). In addition to being an
CC endopeptidase, shows peptidyl-dipeptidase activity, liberating C-
CC terminal dipeptides.; EC=3.4.22.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001754};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004465}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004465}; Extracellular side
CC {ECO:0000256|ARBA:ARBA00004465}. Lysosome
CC {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; CM001260; EHH28274.1; -; Genomic_DNA.
DR AlphaFoldDB; G7N0H2; -.
DR MEROPS; C01.060; -.
DR Proteomes; UP000013456; Chromosome 8.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02620; Peptidase_C1A_CathepsinB; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR012599; Propeptide_C1A.
DR PANTHER; PTHR12411:SF895; CATHEPSIN B; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
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; Cysteine proteinases; 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 {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..339
FT /note="Cathepsin B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018682658"
FT DOMAIN 80..329
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 339 AA; 37703 MW; 4CDA9B07FAC646CF CRC64;
MWWLWASLCC LLALGDARSR PSFHPLSDEL VNYVNKQNTT WQAGHNFYNV DVSYLKRLCG
TFLGGPKPPQ RVMFTEDLKL PESFDAREQW PQCPTIKEIR DQGSCGSCWA FGAVEAISDR
ICIHTNAHVS VEVSAEDLLT CCGIMCGDGC NGGYPAGAWN FLTRKGLVSG GLYDSHVGCR
PYSIPPCEHH VNGSRPPCTG EGDTPKCSKI CEPGYSPTYK QDKHYGYNSY SVSNSEKDIM
AEIYKNGPVE GAFSVYSDFL LYKSGVYQHV TGEMMGGHAI RILGWGVENG TPYWLVANSW
NTDWGDNGFF KILRGQDHCG IESEVVAGIP RTDQYWEKI
//
