CATZ_HUMAN
ID CATZ_HUMAN Reviewed; 303 AA.
AC Q9UBR2; B2RC40; O75331; Q9UQV5; Q9UQV6;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Cathepsin Z;
DE EC=3.4.18.1 {ECO:0000269|PubMed:10504234};
DE AltName: Full=Cathepsin P;
DE AltName: Full=Cathepsin X;
DE Flags: Precursor;
GN Name=CTSZ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-36 AND ARG-129.
RC TISSUE=Ovary;
RX PubMed=9738465; DOI=10.1016/s0014-5793(98)00964-8;
RA Naegler D.K., Menard R.;
RT "Human cathepsin X: a novel cysteine protease of the papain family with a
RT very short proregion and unique insertions.";
RL FEBS Lett. 434:135-139(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Prostate;
RX PubMed=9642240; DOI=10.1074/jbc.273.27.16816;
RA Santamaria I., Velasco G., Pendas A.M., Fueyo A., Lopez-Otin C.;
RT "Cathepsin Z, a novel human cysteine proteinase with a short propeptide
RT domain and a unique chromosomal location.";
RL J. Biol. Chem. 273:16816-16823(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Blood, and Colon tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [8]
RP NUCLEOTIDE SEQUENCE OF 11-303.
RC TISSUE=Ileum;
RX PubMed=10653162; DOI=10.1007/s004240000112;
RA Pungercar J., Ivanovski G.;
RT "Identification and molecular cloning of cathepsin P, a novel human
RT putative cysteine protease of the papain family.";
RL Pflugers Arch. 439:R116-R118(2000).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10504234; DOI=10.1021/bi991371z;
RA Naegler D.K., Zhang R., Tam W., Sulea T., Purisima E.O., Menard R.;
RT "Human cathepsin X: a cysteine protease with unique carboxypeptidase
RT activity.";
RL Biochemistry 38:12648-12654(1999).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=10653163; DOI=10.1007/s004240000113;
RA Pungercar J., Viyjak A., Ivanovski G., Krizaj I.;
RT "Tissue expression and immunolocalization of a novel human cathepsin P.";
RL Pflugers Arch. 439:R119-R121(2000).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15] {ECO:0007744|PDB:1DEU}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 27-303, ACTIVITY REGULATION,
RP DISULFIDE BONDS, AND ACTIVE SITE.
RX PubMed=10656802; DOI=10.1006/jmbi.1999.3410;
RA Sivaraman J., Nagler D.K., Zhang R., Menard R., Cygler M.;
RT "Crystal structure of human procathepsin X: a cysteine protease with the
RT proregion covalently linked to the active site cysteine.";
RL J. Mol. Biol. 295:939-951(2000).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS), DISULFIDE BONDS, AND ACTIVE SITE.
RX PubMed=10745011; DOI=10.1016/s0969-2126(00)00108-8;
RA Guncar G., Klemencic I., Turk B., Turk V., Karaoglanovic-Carmona A.,
RA Juliano L., Turk D.;
RT "Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows
RT carboxy-monopeptidase and carboxy-dipeptidase activity of the protease.";
RL Structure 8:305-313(2000).
CC -!- FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase
CC activity (PubMed:10504234). Capable of producing kinin potentiating
CC peptides (By similarity). {ECO:0000250|UniProtKB:Q9R1T3,
CC ECO:0000269|PubMed:10504234}.
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:10504234};
CC -!- ACTIVITY REGULATION: The disulfide bridge formed between Cys-33 in the
CC propeptide and the active site residue Cys-92 may prevent activation of
CC the zymogen through formation of a reversible covalent bond with the
CC active site residue. {ECO:0000305|PubMed:10656802}.
CC -!- INTERACTION:
CC Q9UBR2; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-8636823, EBI-1642333;
CC Q9UBR2; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-8636823, EBI-11524452;
CC Q9UBR2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-8636823, EBI-3867333;
CC Q9UBR2; Q5TD97: FHL5; NbExp=3; IntAct=EBI-8636823, EBI-750641;
CC Q9UBR2; O75031: HSF2BP; NbExp=3; IntAct=EBI-8636823, EBI-7116203;
CC Q9UBR2; Q92764: KRT35; NbExp=3; IntAct=EBI-8636823, EBI-1058674;
CC Q9UBR2; Q6A162: KRT40; NbExp=3; IntAct=EBI-8636823, EBI-10171697;
CC Q9UBR2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-8636823, EBI-11959885;
CC Q9UBR2; P60014: KRTAP10-10; NbExp=3; IntAct=EBI-8636823, EBI-11955579;
CC Q9UBR2; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-8636823, EBI-14065470;
CC Q9UBR2; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-8636823, EBI-3957694;
CC Q9UBR2; P26371: KRTAP5-9; NbExp=8; IntAct=EBI-8636823, EBI-3958099;
CC Q9UBR2; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-8636823, EBI-10172526;
CC Q9UBR2; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-8636823, EBI-742948;
CC Q9UBR2; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-8636823, EBI-945833;
CC Q9UBR2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-8636823, EBI-22310682;
CC Q9UBR2; O15162: PLSCR1; NbExp=3; IntAct=EBI-8636823, EBI-740019;
CC Q9UBR2; Q63HR2: TNS2; NbExp=3; IntAct=EBI-8636823, EBI-949753;
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10653163}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10090}.
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DR EMBL; AF073890; AAC61477.1; -; mRNA.
DR EMBL; AF032906; AAC39839.1; -; mRNA.
DR EMBL; AF136273; AAF13145.1; -; mRNA.
DR EMBL; AF136276; AAF13148.1; -; Genomic_DNA.
DR EMBL; AF136274; AAF13148.1; JOINED; Genomic_DNA.
DR EMBL; AF136275; AAF13148.1; JOINED; Genomic_DNA.
DR EMBL; AK314931; BAG37437.1; -; mRNA.
DR EMBL; AL109840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75448.1; -; Genomic_DNA.
DR EMBL; BC042168; AAH42168.1; -; mRNA.
DR EMBL; AF009923; AAC63141.1; -; mRNA.
DR CCDS; CCDS13474.1; -.
DR RefSeq; NP_001327.2; NM_001336.3.
DR PDB; 1DEU; X-ray; 1.70 A; A/B=27-303.
DR PDB; 1EF7; X-ray; 2.67 A; A/B=62-303.
DR PDBsum; 1DEU; -.
DR PDBsum; 1EF7; -.
DR AlphaFoldDB; Q9UBR2; -.
DR SASBDB; Q9UBR2; -.
DR SMR; Q9UBR2; -.
DR BioGRID; 107902; 41.
DR IntAct; Q9UBR2; 26.
DR MINT; Q9UBR2; -.
DR STRING; 9606.ENSP00000217131; -.
DR BindingDB; Q9UBR2; -.
DR ChEMBL; CHEMBL4160; -.
DR GuidetoPHARMACOLOGY; 2354; -.
DR MEROPS; C01.013; -.
DR GlyConnect; 1082; 7 N-Linked glycans (1 site).
DR GlyGen; Q9UBR2; 2 sites, 6 N-linked glycans (1 site).
DR iPTMnet; Q9UBR2; -.
DR PhosphoSitePlus; Q9UBR2; -.
DR SwissPalm; Q9UBR2; -.
DR BioMuta; CTSZ; -.
DR DMDM; 12643324; -.
DR CPTAC; CPTAC-53; -.
DR CPTAC; CPTAC-54; -.
DR EPD; Q9UBR2; -.
DR jPOST; Q9UBR2; -.
DR MassIVE; Q9UBR2; -.
DR MaxQB; Q9UBR2; -.
DR PaxDb; Q9UBR2; -.
DR PeptideAtlas; Q9UBR2; -.
DR PRIDE; Q9UBR2; -.
DR ProteomicsDB; 84036; -.
DR Antibodypedia; 35172; 388 antibodies from 28 providers.
DR DNASU; 1522; -.
DR Ensembl; ENST00000217131.6; ENSP00000217131.5; ENSG00000101160.15.
DR GeneID; 1522; -.
DR KEGG; hsa:1522; -.
DR MANE-Select; ENST00000217131.6; ENSP00000217131.5; NM_001336.4; NP_001327.2.
DR UCSC; uc002yai.3; human.
DR CTD; 1522; -.
DR DisGeNET; 1522; -.
DR GeneCards; CTSZ; -.
DR HGNC; HGNC:2547; CTSZ.
DR HPA; ENSG00000101160; Low tissue specificity.
DR MIM; 603169; gene.
DR neXtProt; NX_Q9UBR2; -.
DR OpenTargets; ENSG00000101160; -.
DR PharmGKB; PA27043; -.
DR VEuPathDB; HostDB:ENSG00000101160; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000155569; -.
DR HOGENOM; CLU_012184_2_1_1; -.
DR InParanoid; Q9UBR2; -.
DR OMA; ECHTIQN; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9UBR2; -.
DR TreeFam; TF313225; -.
DR BRENDA; 3.4.18.1; 2681.
DR PathwayCommons; Q9UBR2; -.
DR Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9UBR2; -.
DR BioGRID-ORCS; 1522; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; CTSZ; human.
DR EvolutionaryTrace; Q9UBR2; -.
DR GeneWiki; Cathepsin_Z; -.
DR GenomeRNAi; 1522; -.
DR Pharos; Q9UBR2; Tchem.
DR PRO; PR:Q9UBR2; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9UBR2; protein.
DR Bgee; ENSG00000101160; Expressed in monocyte and 165 other tissues.
DR Genevisible; Q9UBR2; HS.
DR GO; GO:0005938; C:cell cortex; IDA:CAFA.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; TAS:Reactome.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:CAFA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005764; C:lysosome; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0004180; F:carboxypeptidase activity; IMP:CAFA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; TAS:Reactome.
DR GO; GO:0002003; P:angiotensin maturation; TAS:Reactome.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; IMP:CAFA.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:CAFA.
DR GO; GO:0006508; P:proteolysis; IMP:CAFA.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:1901214; P:regulation of neuron death; IGI:CAFA.
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 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..61
FT /note="Activation peptide"
FT /id="PRO_0000026285"
FT CHAIN 62..303
FT /note="Cathepsin Z"
FT /id="PRO_0000026286"
FT ACT_SITE 92
FT /evidence="ECO:0000305|PubMed:10656802,
FT ECO:0000305|PubMed:10745011"
FT ACT_SITE 241
FT /evidence="ECO:0000305|PubMed:10656802,
FT ECO:0000305|PubMed:10745011"
FT ACT_SITE 261
FT /evidence="ECO:0000305|PubMed:10656802,
FT ECO:0000305|PubMed:10745011"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..92
FT /evidence="ECO:0000269|PubMed:10656802,
FT ECO:0007744|PDB:1DEU"
FT DISULFID 89..132
FT /evidence="ECO:0000269|PubMed:10656802,
FT ECO:0000269|PubMed:10745011, ECO:0007744|PDB:1DEU,
FT ECO:0007744|PDB:1EF7"
FT DISULFID 126..164
FT /evidence="ECO:0000269|PubMed:10656802,
FT ECO:0000269|PubMed:10745011, ECO:0007744|PDB:1DEU,
FT ECO:0007744|PDB:1EF7"
FT DISULFID 154..170
FT /evidence="ECO:0000269|PubMed:10656802,
FT ECO:0000269|PubMed:10745011, ECO:0007744|PDB:1DEU,
FT ECO:0007744|PDB:1EF7"
FT DISULFID 173..179
FT /evidence="ECO:0000269|PubMed:10656802,
FT ECO:0000269|PubMed:10745011, ECO:0007744|PDB:1DEU,
FT ECO:0007744|PDB:1EF7"
FT DISULFID 214..296
FT /evidence="ECO:0000269|PubMed:10656802,
FT ECO:0000269|PubMed:10745011, ECO:0007744|PDB:1DEU,
FT ECO:0007744|PDB:1EF7"
FT VARIANT 36
FT /note="P -> S (in dbSNP:rs778998634)"
FT /evidence="ECO:0000269|PubMed:9738465"
FT /id="VAR_010254"
FT VARIANT 129
FT /note="A -> R (requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:9738465"
FT /id="VAR_010255"
FT VARIANT 286
FT /note="A -> T (in dbSNP:rs34069356)"
FT /id="VAR_033719"
FT CONFLICT 48
FT /note="S -> T (in Ref. 2; AAC39839)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="P -> S (in Ref. 1; AAC61477)"
FT /evidence="ECO:0000305"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1DEU"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1EF7"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:1DEU"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1DEU"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1DEU"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1EF7"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1DEU"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:1DEU"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1DEU"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:1DEU"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:1DEU"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:1DEU"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:1DEU"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:1DEU"
SQ SEQUENCE 303 AA; 33868 MW; 6274FD1974D0EBDC CRC64;
MARRGPGWRP LLLLVLLAGA AQGGLYFRRG QTCYRPLRGD GLAPLGRSTY PRPHEYLSPA
DLPKSWDWRN VDGVNYASIT RNQHIPQYCG SCWAHASTSA MADRINIKRK GAWPSTLLSV
QNVIDCGNAG SCEGGNDLSV WDYAHQHGIP DETCNNYQAK DQECDKFNQC GTCNEFKECH
AIRNYTLWRV GDYGSLSGRE KMMAEIYANG PISCGIMATE RLANYTGGIY AEYQDTTYIN
HVVSVAGWGI SDGTEYWIVR NSWGEPWGER GWLRIVTSTY KDGKGARYNL AIEEHCTFGD
PIV
