CATB_PONAB
ID CATB_PONAB Reviewed; 339 AA.
AC Q5R6D1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:P10605}.
CC Melanosome {ECO:0000250|UniProtKB:P07858}. Secreted, extracellular
CC space {ECO:0000250|UniProtKB:P10605}. 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 -!- 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; CR860464; CAH92586.1; -; mRNA.
DR EMBL; CR860560; CAH92685.1; -; mRNA.
DR RefSeq; NP_001126573.1; NM_001133101.1.
DR AlphaFoldDB; Q5R6D1; -.
DR SMR; Q5R6D1; -.
DR STRING; 9601.ENSPPYP00000020558; -.
DR MEROPS; C01.060; -.
DR Ensembl; ENSPPYT00000021385; ENSPPYP00000020558; ENSPPYG00000018345.
DR GeneID; 100173564; -.
DR KEGG; pon:100173564; -.
DR CTD; 1508; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000158680; -.
DR HOGENOM; CLU_012184_3_3_1; -.
DR InParanoid; Q5R6D1; -.
DR OMA; DEKIPYW; -.
DR OrthoDB; 865289at2759; -.
DR TreeFam; TF314576; -.
DR Proteomes; UP000001595; Chromosome 8.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:1904090; C:peptidase inhibitor complex; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0043394; F:proteoglycan binding; IEA:Ensembl.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0030574; P:collagen catabolic process; IEA:Ensembl.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0010466; P:negative regulation of peptidase activity; IEA:Ensembl.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:Ensembl.
DR GO; GO:0006590; P:thyroid hormone generation; IEA:Ensembl.
DR GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
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 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_0000330880"
FT CHAIN 80..333
FT /note="Cathepsin B"
FT /id="PRO_0000330881"
FT CHAIN 80..126
FT /note="Cathepsin B light chain"
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000330882"
FT CHAIN 129..333
FT /note="Cathepsin B heavy chain"
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000330883"
FT PROPEP 334..339
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000330884"
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:0000255"
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"
SQ SEQUENCE 339 AA; 37820 MW; 18EC5EFC7B2C6455 CRC64;
MWQLWASLCC LLALADARSR PSFHPLSDEL VNYVNKRNTT WQAGHNFYNV DVSYLKKLCG
TFLGGPKPPQ RVMFTEDLKL PESFDAREQW PQCPTIKEIR DQGSCGSCWA FGAVEAISDR
ICIHTNAHVS VEVSAEDLLT CCGSMCGDGC NGGYPAEAWN FWTRKGLVSG GLYESHVGCR
PYSIPPCEHH VNGSRPPCTG EGDTPKCSKI CEPGYSPTYK QDKHYGYNSY SVSNSERDIM
AEIYKNGPVE GAFSVYSDFL LYKSGVYQHV TGEMMGGHAI RILGWGVENG TPYWLVANSW
NTDWGDNGFF KILRGQDHCG IESEVVAGIP RTDQYWEKI
