ID CATB_PIG Reviewed; 335 AA. AC A1E295; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 105. DE RecName: Full=Cathepsin B; DE EC=3.4.22.1 {ECO:0000250|UniProtKB:P07858}; DE Contains: DE RecName: Full=Cathepsin B light chain {ECO:0000250|UniProtKB:P07858}; DE Contains: DE RecName: Full=Cathepsin B heavy chain {ECO:0000250|UniProtKB:P07858}; DE Flags: Precursor; GN Name=CTSB; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Chen L., Li X.W., Zhu L., Li Q., Li M.Z.; RT "Molecular cloning and polymorphism of cathepsin B (CTSB) gene in RT porcine."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=22261194; DOI=10.1161/circulationaha.111.056952; RA Barallobre-Barreiro J., Didangelos A., Schoendube F.A., Drozdov I., Yin X., RA Fernandez-Caggiano M., Willeit P., Puntmann V.O., Aldama-Lopez G., RA Shah A.M., Domenech N., Mayr M.; RT "Proteomics analysis of cardiac extracellular matrix remodeling in a RT porcine model of ischemia/reperfusion injury."; RL Circulation 125:789-802(2012). CC -!- FUNCTION: Thiol protease which is believed to participate in CC intracellular degradation and turnover of proteins (By similarity). CC Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). CC Involved in the solubilization of cross-linked TG/thyroglobulin in the CC thyroid follicle lumen (By similarity). Has also been implicated in CC tumor invasion and metastasis (By similarity). CC {ECO:0000250|UniProtKB:P00787, ECO:0000250|UniProtKB:P07858, CC ECO:0000250|UniProtKB:P10605}. 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:0000250|UniProtKB:P07858}; CC -!- SUBUNIT: Dimer of a heavy chain and a light chain cross-linked by a CC disulfide bond. Interacts with SRPX2. Directly interacts with SHKBP1. CC {ECO:0000250|UniProtKB:P07858}. CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P07858}. CC Melanosome {ECO:0000250|UniProtKB:P07858}. Secreted, extracellular CC space {ECO:0000269|PubMed:22261194}. Apical cell membrane CC {ECO:0000250|UniProtKB:P10605}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P10605}; Extracellular side CC {ECO:0000250|UniProtKB:P10605}. Note=Localizes to the lumen of thyroid CC follicles and to the apical membrane of thyroid epithelial cells. CC {ECO:0000250|UniProtKB:P10605}. CC -!- TISSUE SPECIFICITY: Expressed in heart (at protein level). CC {ECO:0000269|PubMed:22261194}. 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; EF095956; ABK96810.1; -; mRNA. DR RefSeq; NP_001090927.1; NM_001097458.1. DR RefSeq; XP_005657322.2; XM_005657265.2. DR RefSeq; XP_005657323.1; XM_005657266.2. DR RefSeq; XP_005657324.1; XM_005657267.2. DR RefSeq; XP_013845747.1; XM_013990293.1. DR AlphaFoldDB; A1E295; -. DR SMR; A1E295; -. DR IntAct; A1E295; 2. DR STRING; 9823.ENSSSCP00000024395; -. DR MEROPS; C01.060; -. DR GlyCosmos; A1E295; 1 site, No reported glycans. DR PaxDb; 9823-ENSSSCP00000024395; -. DR PeptideAtlas; A1E295; -. DR Ensembl; ENSSSCT00000049406.3; ENSSSCP00000046743.1; ENSSSCG00000023666.4. DR Ensembl; ENSSSCT00015003893.1; ENSSSCP00015001345.1; ENSSSCG00015002579.1. DR Ensembl; ENSSSCT00015003921.1; ENSSSCP00015001359.1; ENSSSCG00015002579.1. DR Ensembl; ENSSSCT00025035776.1; ENSSSCP00025014937.1; ENSSSCG00025026366.1. DR Ensembl; ENSSSCT00030004003.1; ENSSSCP00030001587.1; ENSSSCG00030002799.1. DR Ensembl; ENSSSCT00035095352.1; ENSSSCP00035040101.1; ENSSSCG00035070519.1. DR Ensembl; ENSSSCT00040104061.1; ENSSSCP00040047304.1; ENSSSCG00040075101.1. DR Ensembl; ENSSSCT00045032170.1; ENSSSCP00045022270.1; ENSSSCG00045018627.1. DR Ensembl; ENSSSCT00045032247.1; ENSSSCP00045022327.1; ENSSSCG00045018627.1. DR Ensembl; ENSSSCT00045032316.1; ENSSSCP00045022379.1; ENSSSCG00045018627.1. DR Ensembl; ENSSSCT00045032398.1; ENSSSCP00045022441.1; ENSSSCG00045018627.1. DR Ensembl; ENSSSCT00045032468.1; ENSSSCP00045022486.1; ENSSSCG00045018627.1. DR Ensembl; ENSSSCT00050073267.1; ENSSSCP00050031547.1; ENSSSCG00050053741.1. DR Ensembl; ENSSSCT00055000049.1; ENSSSCP00055000041.1; ENSSSCG00055000027.1. DR Ensembl; ENSSSCT00060041735.1; ENSSSCP00060017740.1; ENSSSCG00060030710.1. DR Ensembl; ENSSSCT00065036005.1; ENSSSCP00065015077.1; ENSSSCG00065026769.1. DR Ensembl; ENSSSCT00065036011.1; ENSSSCP00065015080.1; ENSSSCG00065026769.1. DR Ensembl; ENSSSCT00065036014.1; ENSSSCP00065015082.1; ENSSSCG00065026769.1. DR Ensembl; ENSSSCT00065036024.1; ENSSSCP00065015086.1; ENSSSCG00065026769.1. DR GeneID; 100037961; -. DR KEGG; ssc:100037961; -. DR CTD; 1508; -. DR VGNC; VGNC:87074; CTSB. DR eggNOG; KOG1543; Eukaryota. DR GeneTree; ENSGT00940000158680; -. DR HOGENOM; CLU_012184_3_3_1; -. DR InParanoid; A1E295; -. DR OrthoDB; 808912at2759; -. DR TreeFam; TF314576; -. DR Reactome; R-SSC-1442490; Collagen degradation. DR Reactome; R-SSC-1679131; Trafficking and processing of endosomal TLR. DR Reactome; R-SSC-2132295; MHC class II antigen presentation. DR Reactome; R-SSC-6798695; Neutrophil degranulation. DR Proteomes; UP000008227; Chromosome 14. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR Bgee; ENSSSCG00000023666; Expressed in adult mammalian kidney and 43 other cell types or tissues. DR ExpressionAtlas; A1E295; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL. 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; IBA:GO_Central. DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB. DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central. 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. DR Genevisible; A1E295; SS. PE 1: Evidence at protein level; KW Acetylation; Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; KW Lysosome; Membrane; Protease; Reference proteome; Secreted; Signal; KW Thiol protease; Zymogen. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT PROPEP 18..79 FT /note="Activation peptide" FT /evidence="ECO:0000250|UniProtKB:P07858" FT /id="PRO_0000330885" FT CHAIN 80..332 FT /note="Cathepsin B" FT /id="PRO_0000330886" FT CHAIN 80..126 FT /note="Cathepsin B light chain" FT /evidence="ECO:0000250|UniProtKB:P07858" FT /id="PRO_0000330887" FT CHAIN 129..332 FT /note="Cathepsin B heavy chain" FT /evidence="ECO:0000250|UniProtKB:P07858" FT /id="PRO_0000330888" FT PROPEP 333..335 FT /evidence="ECO:0000250|UniProtKB:P07688" FT /id="PRO_0000330889" FT ACT_SITE 108 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088" FT ACT_SITE 278 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089" FT ACT_SITE 298 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090" FT MOD_RES 220 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P10605" FT CARBOHYD 192 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000250|UniProtKB:P07688" FT DISULFID 93..122 FT /evidence="ECO:0000250|UniProtKB:P07858" FT DISULFID 105..150 FT /evidence="ECO:0000250|UniProtKB:P07858" FT DISULFID 141..207 FT /evidence="ECO:0000250|UniProtKB:P07858" FT DISULFID 142..146 FT /evidence="ECO:0000250|UniProtKB:P07858" FT DISULFID 179..211 FT /evidence="ECO:0000250|UniProtKB:P07858" FT DISULFID 187..198 FT /evidence="ECO:0000250|UniProtKB:P07858" FT DISULFID 227..331 FT /evidence="ECO:0000250|UniProtKB:P07858" SQ SEQUENCE 335 AA; 36901 MW; D94E13E44822C19D CRC64; MWRLLATLSC LVLLTSARES LHFQPLSDEL VNFINKQNTT WTAGHNFYNV DLSYVKKLCG TFLGGPKLPQ RAAFAADMIL PKSFDAREQW PNCPTIKEIR DQGSCGSCWA FGAVEAISDR ICIRSNGRVN VEVSAEDMLT CCGDECGDGC NGGFPSGAWN FWTKKGLVSG GLYDSHVGCR PYSIPPCEHH VNGSRPPCTG EGDTPKCSKI CEPGYTPSYK EDKHFGCSSY SISRNEKEIM AEIYKNGPVE GAFTVYSDFL QYKSGVYQHV TGDLMGGHAI RILGWGVENG TPYWLVGNSW NTDWGDNGFF KILRGQDHCG IESEIVAGIP CTPHF //