ID CATB_MACFA Reviewed; 339 AA. AC Q4R5M2; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Cathepsin B; DE EC=3.4.22.1; DE Contains: DE RecName: Full=Cathepsin B light chain; DE Contains: DE RecName: Full=Cathepsin B heavy chain; DE Flags: Precursor; GN Name=CTSB; ORFNames=QccE-13673; OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG International consortium for macaque cDNA sequencing and analysis; RT "DNA sequences of macaque genes expressed in brain or testis and its RT evolutionary implications."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Thiol protease which is believed to participate in CC intracellular degradation and turnover of proteins. Has also been CC implicated in tumor invasion and metastasis (By similarity). CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity CC for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in CC small molecule substrates (thus differing from cathepsin L). In CC addition to being an endopeptidase, shows peptidyl-dipeptidase CC activity, liberating C-terminal dipeptides. CC -!- SUBUNIT: Dimer of a heavy chain and a light chain cross-linked by CC a disulfide bond (By similarity). CC -!- SUBCELLULAR LOCATION: Lysosome (By similarity). Melanosome (By CC similarity). CC -!- SIMILARITY: Belongs to the peptidase C1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB169521; BAE01603.1; -; mRNA. DR SMR; Q4R5M2; 18-333. DR MEROPS; C01.060; -. DR HOVERGEN; Q4R5M2; -. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro. DR InterPro; IPR000169; Pept_cys_AS. DR InterPro; IPR013128; Peptidase_C1A. DR InterPro; IPR000668; Peptidase_C1A_C. DR InterPro; IPR015643; Peptidase_C1A_cathepsin-B. DR InterPro; IPR012599; Propeptide_C1A. DR PANTHER; PTHR12411:SF16; CathepsinB_like; 1. DR PANTHER; PTHR12411; Peptidase_C1A; 1. DR Pfam; PF00112; Peptidase_C1; 1. DR Pfam; PF08127; Propeptide_C1; 1. DR PRINTS; PR00705; PAPAIN. DR ProDom; PD000158; Peptidase_C1; 1. DR SMART; SM00645; Pept_C1; 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; Lysosome; Protease; Signal; KW Thiol protease; Zymogen. FT SIGNAL 1 17 Potential. FT PROPEP 18 79 Activation peptide (By similarity). FT /FTId=PRO_0000330875. FT CHAIN 80 333 Cathepsin B. FT /FTId=PRO_0000330876. FT CHAIN 80 126 Cathepsin B light chain (By similarity). FT /FTId=PRO_0000330877. FT CHAIN 129 333 Cathepsin B heavy chain (By similarity). FT /FTId=PRO_0000330878. FT PROPEP 334 339 By similarity. FT /FTId=PRO_0000330879. FT ACT_SITE 108 108 By similarity. FT ACT_SITE 278 278 By similarity. FT ACT_SITE 298 298 By similarity. FT CARBOHYD 192 192 N-linked (GlcNAc...) (Potential). FT DISULFID 93 122 By similarity. FT DISULFID 105 150 By similarity. FT DISULFID 141 207 By similarity. FT DISULFID 142 146 By similarity. FT DISULFID 179 211 By similarity. FT DISULFID 187 198 By similarity. SQ SEQUENCE 339 AA; 37776 MW; 57D18B0CE1CD56CF CRC64; MWWLWASLCC LLALGDARSR PSFHPLSDEL VNYVNKQNTT WQAGHNFYNV DVSYLKRLCG TFLGGPKPPQ RVMFTEDLKL PESFDAREQW PQCPTIKEIR DQGSCGSCWA FGAVEAISDR ICIHTNAHVS VEVSAEDLLT CCGIMCGDGC NGGYPAGAWN FWTRKGLVSG GLYDSHVGCR PYSIPPCEHH VNGSRPPCTG EGDTPKCSKI CEPGYSPTYK QDKHYGYNSY SVSNSEKDIM AEIYKNGPVE GAFSVYSDFL LYKSGVYQHV TGEMMGGHAI RILGWGVENG TPYWLVANSW NTDWGDNGFF KILRGQDHCG IESEVVAGIP RTDQYWEKI //