GenomeNet

Database: UniProt
Entry: H9B8T9_CAPHI
LinkDB: H9B8T9_CAPHI
Original site: H9B8T9_CAPHI 
ID   H9B8T9_CAPHI            Unreviewed;       335 AA.
AC   H9B8T9;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Cathepsin B {ECO:0000256|ARBA:ARBA00015559};
DE            EC=3.4.22.1 {ECO:0000256|ARBA:ARBA00012537};
GN   Name=CTSB {ECO:0000313|Ensembl:ENSCHIP00000030835.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|EMBL:AFC90100.1};
RN   [1] {ECO:0000313|EMBL:AFC90100.1}
RP   NUCLEOTIDE SEQUENCE.
RA   He Z., Sun Z., Tan Z., Tang S., Han X., Zhou C., Ran T., Liu Y., Zou Y.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000030835.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSCHIP00000030835.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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; LWLT01000007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; JN986831; AFC90100.1; -; mRNA.
DR   RefSeq; NP_001301174.1; NM_001314245.1.
DR   RefSeq; XP_017907267.1; XM_018051778.1.
DR   SMR; H9B8T9; -.
DR   STRING; 9925.ENSCHIP00000030835; -.
DR   ChEMBL; CHEMBL3232689; -.
DR   MEROPS; C01.060; -.
DR   Ensembl; ENSCHIT00000038707.1; ENSCHIP00000030835.1; ENSCHIG00000025426.1.
DR   GeneID; 102173295; -.
DR   KEGG; chx:102173295; -.
DR   CTD; 1508; -.
DR   GeneTree; ENSGT00940000158680; -.
DR   OMA; DEKIPYW; -.
DR   OrthoDB; 808912at2759; -.
DR   BRENDA; 3.4.22.1; 1166.
DR   Proteomes; UP000291000; Chromosome 8.
DR   Bgee; ENSCHIG00000025426; Expressed in skin of neck and 18 other cell types or 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:Ensembl.
DR   GO; GO:0005764; C:lysosome; 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: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: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   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   2: Evidence at transcript level;
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..335
FT                   /note="Cathepsin B"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5040662696"
FT   DOMAIN          80..329
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
SQ   SEQUENCE   335 AA;  36781 MW;  E07FB52EB98E558B 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 CTHQY
//
DBGET integrated database retrieval system