CATZ_MOUSE
ID CATZ_MOUSE Reviewed; 306 AA.
AC Q9WUU7;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cathepsin Z;
DE EC=3.4.18.1 {ECO:0000250|UniProtKB:Q9UBR2};
DE Flags: Precursor;
GN Name=Ctsz;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Santamaria I.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Fetus;
RX PubMed=10760573; DOI=10.1016/s0167-4781(00)00021-x;
RA Deussing J., von Olshausen I., Peters C.;
RT "Murine and human cathepsin Z: cDNA-cloning, characterization of the genes
RT and chromosomal localization.";
RL Biochim. Biophys. Acta 1491:93-106(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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-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 -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10090}.
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DR EMBL; AJ242663; CAB44494.1; -; mRNA.
DR EMBL; AF136277; AAF13143.1; -; mRNA.
DR EMBL; AF136278; AAF13144.1; -; Genomic_DNA.
DR EMBL; BC008619; AAH08619.1; -; mRNA.
DR CCDS; CCDS17152.1; -.
DR RefSeq; NP_071720.1; NM_022325.5.
DR AlphaFoldDB; Q9WUU7; -.
DR SMR; Q9WUU7; -.
DR BioGRID; 211031; 11.
DR IntAct; Q9WUU7; 1.
DR STRING; 10090.ENSMUSP00000016400; -.
DR MEROPS; C01.013; -.
DR GlyConnect; 2193; 4 N-Linked glycans (1 site).
DR GlyGen; Q9WUU7; 2 sites, 4 N-linked glycans (1 site).
DR PhosphoSitePlus; Q9WUU7; -.
DR SwissPalm; Q9WUU7; -.
DR CPTAC; non-CPTAC-3774; -.
DR EPD; Q9WUU7; -.
DR jPOST; Q9WUU7; -.
DR MaxQB; Q9WUU7; -.
DR PaxDb; Q9WUU7; -.
DR PRIDE; Q9WUU7; -.
DR ProteomicsDB; 279925; -.
DR Antibodypedia; 35172; 388 antibodies from 28 providers.
DR DNASU; 64138; -.
DR Ensembl; ENSMUST00000016400; ENSMUSP00000016400; ENSMUSG00000016256.
DR GeneID; 64138; -.
DR KEGG; mmu:64138; -.
DR UCSC; uc008ofd.1; mouse.
DR CTD; 1522; -.
DR MGI; MGI:1891190; Ctsz.
DR VEuPathDB; HostDB:ENSMUSG00000016256; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000155569; -.
DR HOGENOM; CLU_012184_2_1_1; -.
DR InParanoid; Q9WUU7; -.
DR OMA; ECHTIQN; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9WUU7; -.
DR TreeFam; TF313225; -.
DR BRENDA; 3.4.18.1; 3474.
DR Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 64138; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ctsz; mouse.
DR PRO; PR:Q9WUU7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9WUU7; protein.
DR Bgee; ENSMUSG00000016256; Expressed in stroma of bone marrow and 251 other tissues.
DR ExpressionAtlas; Q9WUU7; baseline and differential.
DR Genevisible; Q9WUU7; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0004180; F:carboxypeptidase activity; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEP:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:1901214; P:regulation of neuron death; ISO:MGI.
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; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..63
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026287"
FT CHAIN 64..306
FT /note="Cathepsin Z"
FT /id="PRO_0000026288"
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; 33996 MW; 1B94045C3D0A7CFB CRC64;
MASSGSVQQL PLVLLMLLLA SAARARLYFR SGQTCYHPIR GDQLALLGRR TYPRPHEYLS
PADLPKNWDW RNVNGVNYAS VTRNQHIPQY CGSCWAHGST SAMADRINIK RKGAWPSILL
SVQNVIDCGN AGSCEGGNDL PVWEYAHKHG IPDETCNNYQ AKDQDCDKFN QCGTCTEFKE
CHTIQNYTLW RVGDYGSLSG REKMMAEIYA NGPISCGIMA TEMMSNYTGG IYAEHQDQAV
INHIISVAGW GVSNDGIEYW IVRNSWGEPW GEKGWMRIVT STYKGGTGDS YNLAIESACT
FGDPIV
