CATH_BOVIN
ID CATH_BOVIN Reviewed; 335 AA.
AC Q3T0I2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Pro-cathepsin H;
DE Contains:
DE RecName: Full=Cathepsin H mini chain;
DE Contains:
DE RecName: Full=Cathepsin H;
DE EC=3.4.22.16;
DE Contains:
DE RecName: Full=Cathepsin H heavy chain;
DE Contains:
DE RecName: Full=Cathepsin H light chain;
DE Flags: Precursor;
GN Name=CTSH;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Important for the overall degradation of proteins in
CC lysosomes. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably,
CC cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16;
CC -!- SUBUNIT: Composed of a mini chain and a large chain. The large chain
CC may be split into heavy and light chain. All chains are held together
CC by disulfide bonds (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
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; BC102386; AAI02387.1; -; mRNA.
DR RefSeq; NP_001029557.1; NM_001034385.2.
DR AlphaFoldDB; Q3T0I2; -.
DR SMR; Q3T0I2; -.
DR STRING; 9913.ENSBTAP00000014593; -.
DR MEROPS; C01.040; -.
DR PaxDb; Q3T0I2; -.
DR PRIDE; Q3T0I2; -.
DR Ensembl; ENSBTAT00000014593; ENSBTAP00000014593; ENSBTAG00000010992.
DR GeneID; 510524; -.
DR KEGG; bta:510524; -.
DR CTD; 1512; -.
DR VEuPathDB; HostDB:ENSBTAG00000010992; -.
DR VGNC; VGNC:27816; CTSH.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000160227; -.
DR HOGENOM; CLU_012184_1_1_1; -.
DR InParanoid; Q3T0I2; -.
DR OMA; AYNNFGC; -.
DR OrthoDB; 1275401at2759; -.
DR TreeFam; TF328985; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000010992; Expressed in monocyte and 104 other tissues.
DR ExpressionAtlas; Q3T0I2; baseline and differential.
DR GO; GO:0097208; C:alveolar lamellar body; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0030108; F:HLA-A specific activating MHC class I receptor activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
DR GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0060448; P:dichotomous subdivision of terminal units involved in lung branching; ISS:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0002764; P:immune response-regulating signaling pathway; ISS:UniProtKB.
DR GO; GO:0033619; P:membrane protein proteolysis; ISS:UniProtKB.
DR GO; GO:0001656; P:metanephros development; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010813; P:neuropeptide catabolic process; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0010952; P:positive regulation of peptidase activity; ISS:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0032526; P:response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0043129; P:surfactant homeostasis; ISS:UniProtKB.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; ISS:UniProtKB.
DR CDD; cd02248; Peptidase_C1A; 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; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
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 Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT PROPEP 23..97
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000238112"
FT PEPTIDE 98..105
FT /note="Cathepsin H mini chain"
FT /id="PRO_0000238113"
FT PROPEP 106..115
FT /evidence="ECO:0000250"
FT /id="PRO_0000238114"
FT CHAIN 116..335
FT /note="Cathepsin H"
FT /id="PRO_0000238115"
FT CHAIN 116..292
FT /note="Cathepsin H heavy chain"
FT /id="PRO_0000238116"
FT CHAIN 293..335
FT /note="Cathepsin H light chain"
FT /id="PRO_0000238117"
FT ACT_SITE 141
FT /evidence="ECO:0000250"
FT ACT_SITE 281
FT /evidence="ECO:0000250"
FT ACT_SITE 301
FT /evidence="ECO:0000250"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 102..327
FT /evidence="ECO:0000250"
FT DISULFID 138..181
FT /evidence="ECO:0000250"
FT DISULFID 172..214
FT /evidence="ECO:0000250"
FT DISULFID 272..322
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 37351 MW; 79FDBEBB9984D227 CRC64;
MWAVLPLLCA GAWLLGAPAC GAAELAANSL EKFHFQSWMV QHQKKYSSEE YYHRLQAFAS
NLREINAHNA RNHTFKMGLN QFSDMSFDEL KRKYLWSEPQ NCSATKSNYL RGTGPYPPSM
DWRKKGNFVT PVKNQGSCGS CWTFSTTGAL ESAVAIATGK LPFLAEQQLV DCAQNFNNHG
CQGGLPSQAF EYIRYNKGIM GEDTYPYRGQ DGDCKYQPSK AIAFVKDVAN ITLNDEEAMV
EAVALHNPVS FAFEVTADFM MYRKGIYSST SCHKTPDKVN HAVLAVGYGE EKGIPYWIVK
NSWGPNWGMK GYFLIERGKN MCGLAACASF PIPLV
