CATZ_BOVIN
ID CATZ_BOVIN Reviewed; 304 AA.
AC P05689; Q0IIK1;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Cathepsin Z;
DE EC=3.4.18.1 {ECO:0000250|UniProtKB:Q9UBR2};
DE Flags: Precursor;
GN Name=CTSZ;
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=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 232-304.
RX PubMed=3838468; DOI=10.1042/bj2250707;
RA Gay N.J., Walker J.E.;
RT "Molecular cloning of a bovine cathepsin.";
RL Biochem. J. 225:707-712(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 232-304.
RA Salvesen G., Gay N.J., Walker J.E.;
RT "Cloning of a bovine protein homologous with cysteine proteinases and
RT identification of the gene.";
RL (In) Turk V. (eds.);
RL Cysteine proteinases and their inhibitors, pp.55-62, Walter de Gruyter,
RL Berlin and New York (1986).
CC -!- FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase
CC activity (By similarity). Capable of producing kinin potentiating
CC peptides (By similarity). {ECO:0000250|UniProtKB:Q9R1T3,
CC ECO:0000250|UniProtKB:Q9UBR2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of C-terminal amino acid residues with broad
CC specificity, but lacks action on C-terminal proline. Shows weak
CC endopeptidase activity.; EC=3.4.18.1;
CC Evidence={ECO:0000250|UniProtKB:Q9UBR2};
CC -!- ACTIVITY REGULATION: The disulfide bridge formed between Cys-34 in the
CC propeptide and the active site residue Cys-93 may prevent activation of
CC the zymogen through formation of a reversible covalent bond with the
CC active site residue. {ECO:0000250|UniProtKB:Q9UBR2}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10090}.
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DR EMBL; BC122603; AAI22604.1; -; mRNA.
DR EMBL; X01809; CAA25952.1; -; mRNA.
DR PIR; A29172; A29172.
DR RefSeq; NP_001071303.1; NM_001077835.1.
DR AlphaFoldDB; P05689; -.
DR SMR; P05689; -.
DR STRING; 9913.ENSBTAP00000025007; -.
DR MEROPS; C01.013; -.
DR PaxDb; P05689; -.
DR PeptideAtlas; P05689; -.
DR PRIDE; P05689; -.
DR Ensembl; ENSBTAT00000025007; ENSBTAP00000025007; ENSBTAG00000018784.
DR GeneID; 404187; -.
DR KEGG; bta:404187; -.
DR CTD; 1522; -.
DR VEuPathDB; HostDB:ENSBTAG00000018784; -.
DR VGNC; VGNC:27820; CTSZ.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000155569; -.
DR InParanoid; P05689; -.
DR OMA; ECHTIQN; -.
DR OrthoDB; 1275401at2759; -.
DR BRENDA; 3.4.18.1; 908.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000018784; Expressed in lung and 102 other tissues.
DR ExpressionAtlas; P05689; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd02698; Peptidase_C1A_CathepsinX; 1.
DR InterPro; IPR033157; CTSZ.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR PANTHER; PTHR12411:SF569; PTHR12411:SF569; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..62
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000284523"
FT CHAIN 63..304
FT /note="Cathepsin Z"
FT /id="PRO_0000050537"
FT ACT_SITE 93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT ACT_SITE 242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT ACT_SITE 262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..93
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 90..133
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 127..165
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 155..171
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 174..180
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 215..297
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
SQ SEQUENCE 304 AA; 33886 MW; C283E2F0DBC5855E CRC64;
MASSGPLVPP LLLLLVLLAG AARAGLHFRP GRGCYRPLRG DRLTQLGRRT YPRPHEYLSP
SDLPKSWDWR NVNGVNYASV TRNQHIPQYC GSCWAHGSTS AMADRINIKR KGAWPSTLLS
VQHVIDCGDA GSCEGGNDLP VWEYAHRHGI PDETCNNYQA KDQECDKFNQ CGTCTEFKEC
HVIKNYTLWK VGDYGSLSGR EKMMAEIYTN GPISCGIMAT EKMSNYTGGI YSEYNDQAFI
NHIVSVAGWG VSDGMEYWIV RNSWGEPWGE HGWMRIVTST YKGGEGARYN LAIEESCTFG
DPIV
