CATZ_RAT
ID CATZ_RAT Reviewed; 306 AA.
AC Q9R1T3; Q5BKD9;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cathepsin Z;
DE EC=3.4.18.1 {ECO:0000269|PubMed:10615013, ECO:0000269|PubMed:12553736};
DE AltName: Full=Cathepsin Y;
DE Flags: Precursor;
GN Name=Ctsz; Synonyms=Ctsy;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Spleen;
RX PubMed=12553736; DOI=10.1515/bc.2002.223;
RA Nakazono E., Kamata Y., Yamafuji K.;
RT "Determination of the mRNA sequence of cathepsin Y, a cysteine
RT endopeptidase from rat spleen, and confirmation of its ubiquitous
RT expression.";
RL Biol. Chem. 383:1971-1975(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PRELIMINARY NUCLEOTIDE SEQUENCE OF 64-306, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=Wistar; TISSUE=Spleen;
RX PubMed=10615013; DOI=10.1016/s0162-3109(99)00079-x;
RA Sakamoto E., Sakao Y., Taniguchi Y., Yamafuji K.;
RT "Cathepsin Y (a novel thiol enzyme) produces kinin potentiating peptide
RT from the component protein of rat plasma.";
RL Immunopharmacology 45:207-214(1999).
CC -!- FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase
CC activity (PubMed:12553736, PubMed:10615013). Capable of producing kinin
CC potentiating peptides (PubMed:10615013). {ECO:0000269|PubMed:10615013,
CC ECO:0000269|PubMed:12553736}.
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:0000269|PubMed:10615013, ECO:0000269|PubMed:12553736};
CC -!- ACTIVITY REGULATION: The disulfide bridge formed between Cys-35 in the
CC propeptide and the active site residue Cys-94 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.6 uM for the synthetic substrate Z-Phe-Arg-NMec
CC {ECO:0000269|PubMed:12553736};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12553736}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10090}.
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DR EMBL; AB023781; BAA82844.2; -; mRNA.
DR EMBL; BC091110; AAH91110.1; -; mRNA.
DR RefSeq; NP_899159.1; NM_183330.1.
DR AlphaFoldDB; Q9R1T3; -.
DR SMR; Q9R1T3; -.
DR STRING; 10116.ENSRNOP00000066523; -.
DR BindingDB; Q9R1T3; -.
DR ChEMBL; CHEMBL3308941; -.
DR MEROPS; C01.125; -.
DR GlyGen; Q9R1T3; 2 sites.
DR PaxDb; Q9R1T3; -.
DR PRIDE; Q9R1T3; -.
DR Ensembl; ENSRNOT00000072069; ENSRNOP00000066523; ENSRNOG00000050697.
DR GeneID; 252929; -.
DR KEGG; rno:252929; -.
DR CTD; 1522; -.
DR RGD; 708479; Ctsz.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000155569; -.
DR HOGENOM; CLU_012184_2_1_1; -.
DR InParanoid; Q9R1T3; -.
DR OMA; ECHTIQN; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9R1T3; -.
DR Reactome; R-RNO-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q9R1T3; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000050697; Expressed in spleen and 20 other tissues.
DR Genevisible; Q9R1T3; RN.
DR GO; GO:0005938; C:cell cortex; IDA:CAFA.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0030426; C:growth cone; IDA:CAFA.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0004180; F:carboxypeptidase activity; ISO:RGD.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:CAFA.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:CAFA.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:CAFA.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:1901214; P:regulation of neuron death; ISO:RGD.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..63
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026289"
FT CHAIN 64..306
FT /note="Cathepsin Z"
FT /id="PRO_0000026290"
FT ACT_SITE 94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT ACT_SITE 243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT ACT_SITE 264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..94
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 91..134
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 128..166
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 156..172
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 175..181
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
FT DISULFID 216..299
FT /evidence="ECO:0000250|UniProtKB:Q9UBR2"
SQ SEQUENCE 306 AA; 34194 MW; A4B3C6646087BCB5 CRC64;
MASSGSVQQL RLVLLMLLLA GAARASLYFR PGQTCYRPLH RDHLALLGRR TYPRPHEYLS
PADLPKNWDW RNVNGVNYAS VTRNQHIPQY CGSCWAHGST SALADRINIK RKGAWPSTLL
SVQNVIDCGN AGSCEGGNDL PVWEYAHKHG IPDETCNNYQ AKDQECDKFN QCGTCTEFKE
CHTIQNYTLW RVGDYGSLSG REKMMAEIYA NGPISCGIMA TERMSNYTGG IYTEYQNQAI
INHIISVAGW GVSNDGIEYW IVRNSWGEPW GERGWMRIVT STYKGGTGSS YNLAIEEACT
FGDPIV
