CATB_SHEEP
ID CATB_SHEEP Reviewed; 335 AA.
AC P83205; S5FR89; W5Q0Z2;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Cathepsin B;
DE EC=3.4.22.1 {ECO:0000250|UniProtKB:P07858};
DE AltName: Full=Cathepsin B1;
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000305};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Qi X., Tian S.;
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000312|Ensembl:ENSOARP00000016378};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [3]
RP PROTEIN SEQUENCE OF 80-89.
RC TISSUE=Placenta;
RX PubMed=12506352; DOI=10.1002/mrd.10246;
RA El Amiri B., Remy B., Sousa N.M., Joris B., Ottiers N.G., Perenyi Z.,
RA Mboko H.B., Beckers J.-F.M.P.;
RT "Isolation and partial characterization of three pregnancy-associated
RT glycoproteins from the ewe placenta.";
RL Mol. Reprod. Dev. 64:199-206(2003).
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; KC699918; AGQ42753.1; -; mRNA.
DR EMBL; AMGL01051277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001295516.1; NM_001308587.1.
DR RefSeq; XP_004004501.1; XM_004004452.2.
DR RefSeq; XP_011984446.1; XM_012129056.2.
DR RefSeq; XP_011984453.1; XM_012129063.2.
DR AlphaFoldDB; P83205; -.
DR SMR; P83205; -.
DR STRING; 9940.ENSOARP00000016378; -.
DR MEROPS; C01.060; -.
DR Ensembl; ENSOART00000016613; ENSOARP00000016378; ENSOARG00000015263.
DR Ensembl; ENSOART00020012789; ENSOARP00020010526; ENSOARG00020008336.
DR GeneID; 780470; -.
DR KEGG; oas:780470; -.
DR CTD; 1508; -.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_3_3_1; -.
DR OMA; DEKIPYW; -.
DR OrthoDB; 865289at2759; -.
DR Proteomes; UP000002356; Chromosome 2.
DR Bgee; ENSOARG00000015263; Expressed in thyroid gland and 53 other tissues.
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.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Lysosome; Membrane; Protease; Reference proteome;
KW Secreted; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..79
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:12506352"
FT /id="PRO_0000445804"
FT CHAIN 80..335
FT /note="Cathepsin B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000050534"
FT CHAIN 80..126
FT /note="Cathepsin B light chain"
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000445805"
FT CHAIN 129..333
FT /note="Cathepsin B heavy chain"
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000445806"
FT PROPEP 333..335
FT /evidence="ECO:0000250|UniProtKB:P07688"
FT /id="PRO_0000445807"
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"
FT CONFLICT 332..335
FT /note="AHQH -> THQY (in Ref. 1; AGQ42753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 36725 MW; FACFB532C98E558B CRC64;
MWQLLATLSC LLVLTSARSS LHFPPLSDEM VNYVNKQNTT WKAGHNFYNV DLSYVKKLCG
AILGGPKLPQ RDAFAADMVL PDSFDAREQW PNCPTIKEIR DQGSCGSCWA FGAVEAISDR
ICIHSKGRVN VEVSAEDMLT CCGSECGDGC NGGFPSGAWN FWTKKGLVSG GLYDSHVGCR
PYSIPPCEHH VNGSRPPCTG EGDTPKCSKI CEPGYSPSYK DDKHFGCSSY SVSSNEKEIM
AEIYKNGPVE GAFSVYSDFL LYKSGVYQHV SGEMMGGHAI RILGWGVEND TPYWLVGNSW
NTDWGDKGFF KILRGQDHCG IESEIVAGMP CAHQH
