Q9UBR2 (CATZ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cathepsin Z
EC=3.4.18.1

Alternative name(s):
Cathepsin P
Cathepsin X

Gene names

Name:

CTSZ

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity.
Catalytic activity	Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity. Ref.9
Subcellular location	Lysosome.
Tissue specificity	Widely expressed. Ref.10
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	epithelial tube branching involved in lung morphogenesis Inferred from electronic annotation. Source: Compara proteolysis Traceable author statement Ref.2. Source: ProtInc
Cellular_component	endoplasmic reticulum Inferred from direct assay. Source: LIFEdb extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cysteine-type peptidase activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Potential

Propeptide

24 – 61

38

Activation peptide

PRO_0000026285

Chain

62 – 303

242

Cathepsin Z

PRO_0000026286

Sites

Active site

92

1

Active site

241

1

Active site

261

1

Amino acid modifications

Glycosylation

184

1

N-linked (GlcNAc...) Ref.11

Glycosylation

224

1

N-linked (GlcNAc...) Potential

Disulfide bond

89 ↔ 132

Disulfide bond

126 ↔ 164

Disulfide bond

154 ↔ 170

Disulfide bond

173 ↔ 179

Disulfide bond

214 ↔ 296

Natural variations

Natural variant

36

1

P → S. Ref.1

VAR_010254

Natural variant

129

1

A → R Requires 2 nucleotide substitutions. Ref.1

VAR_010255

Natural variant

286

1

A → T.
Corresponds to variant rs34069356 [ dbSNP | Ensembl ].

VAR_033719

Experimental info

Sequence conflict

48

1

S → T in AAC39839. Ref.2

Sequence conflict

150

1

P → S in AAC61477. Ref.1

Secondary structure

1

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303

Helix Strand Turn

Details...

Beta strand

40 – 42

3

Helix

59 – 61

3

Beta strand

85 – 87

3

Helix

92 – 108

17

Turn

109 – 111

3

Helix

120 – 126

7

Beta strand

127 – 131

5

Beta strand

133 – 135

3

Helix

137 – 146

10

Beta strand

149 – 151

3

Helix

152 – 154

3

Helix

166 – 169

4

Beta strand

170 – 175

6

Beta strand

178 – 181

4

Beta strand

190 – 196

7

Helix

199 – 209

11

Beta strand

212 – 216

5

Helix

220 – 223

4

Beta strand

227 – 230

4

Beta strand

241 – 251

11

Beta strand

254 – 260

7

Beta strand

272 – 276

5

Helix

280 – 283

4

Helix

285 – 287

3

Turn

290 – 293

4

Beta strand

296 – 301

6

Sequences

	Sequence		Length	Mass (Da)
	Q9UBR2 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6274FD1974D0EBDC	FASTA	303	33,868
	10 20 30 40 50 60 MARRGPGWRP LLLLVLLAGA AQGGLYFRRG QTCYRPLRGD GLAPLGRSTY PRPHEYLSPA 70 80 90 100 110 120 DLPKSWDWRN VDGVNYASIT RNQHIPQYCG SCWAHASTSA MADRINIKRK GAWPSTLLSV 130 140 150 160 170 180 QNVIDCGNAG SCEGGNDLSV WDYAHQHGIP DETCNNYQAK DQECDKFNQC GTCNEFKECH 190 200 210 220 230 240 AIRNYTLWRV GDYGSLSGRE KMMAEIYANG PISCGIMATE RLANYTGGIY AEYQDTTYIN 250 260 270 280 290 300 HVVSVAGWGI SDGTEYWIVR NSWGEPWGER GWLRIVTSTY KDGKGARYNL AIEEHCTFGD PIV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions." Naegler D.K., Menard R. FEBS Lett. 434:135-139(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-36 AND ARG-129. Tissue: Ovary.
[2]	"Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location." Santamaria I., Velasco G., Pendas A.M., Fueyo A., Lopez-Otin C. J. Biol. Chem. 273:16816-16823(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Prostate.
[3]	"Murine and human cathepsin Z: cDNA-cloning, characterization of the genes and chromosomal localization." Deussing J., von Olshausen I., Peters C. Biochim. Biophys. Acta 1491:93-106(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Blood and Colon tumor.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[5]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[8]	"Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family." Pungercar J., Ivanovski G. Pflugers Arch. 439:R116-R118(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 11-303. Tissue: Ileum.
[9]	"Human cathepsin X: a cysteine protease with unique carboxypeptidase activity." Naegler D.K., Zhang R., Tam W., Sulea T., Purisima E.O., Menard R. Biochemistry 38:12648-12654(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, CHARACTERIZATION.
[10]	"Tissue expression and immunolocalization of a novel human cathepsin P." Pungercar J., Viyjak A., Ivanovski G., Krizaj I. Pflugers Arch. 439:R119-R121(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[11]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184, MASS SPECTROMETRY. Tissue: Liver.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease." Guncar G., Klemencic I., Turk B., Turk V., Karaoglanovic-Carmona A., Juliano L., Turk D. Structure 8:305-313(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF073890 mRNA. Translation: AAC61477.1.
AF032906 mRNA. Translation: AAC39839.1.
AF136273 mRNA. Translation: AAF13145.1.
AF136276, AF136274, AF136275 Genomic DNA. Translation: AAF13148.1.
AK314931 mRNA. Translation: BAG37437.1.
AL109840 Genomic DNA. Translation: CAC09370.1.
CH471077 Genomic DNA. Translation: EAW75448.1.
BC042168 mRNA. Translation: AAH42168.1.
AF009923 mRNA. Translation: AAC63141.1.

IPI

IPI00002745.

RefSeq

NP_001327.2. NM_001336.3.

UniGene

Hs.252549.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DEU	X-ray	1.70	A/B	27-303	[»]
1EF7	X-ray	2.67	A/B	62-303	[»]

ProteinModelPortal

Q9UBR2.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000217131.

Protein family/group databases

MEROPS

C01.013.

Polymorphism databases

DMDM

12643324.

Proteomic databases

PaxDb

Q9UBR2.

PeptideAtlas

Q9UBR2.

PRIDE

Q9UBR2.

Protocols and materials databases

DNASU

1522.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000217131; ENSP00000217131; ENSG00000101160.

GeneID

1522.

KEGG

hsa:1522.

UCSC

uc002yai.2. human.

Organism-specific databases

CTD

1522.

GeneCards

GC20M057570.

HGNC

HGNC:2547. CTSZ.

HPA

CAB025114.

MIM

603169. gene.

neXtProt

NX_Q9UBR2.

PharmGKB

PA27043.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4870.

HOGENOM

HOG000264454.

HOVERGEN

HBG004456.

InParanoid

Q9UBR2.

KO

K08568.

OMA

QCGTCTE.

OrthoDB

EOG42Z4QN.

PhylomeDB

Q9UBR2.

Enzyme and pathway databases

BRENDA

3.4.18.1. 2681.

Reactome

REACT_11123. Membrane Trafficking.
REACT_17015. Metabolism of proteins.

Gene expression databases

Bgee

Q9UBR2.

CleanEx

HS_CTSZ.

Genevestigator

Q9UBR2.

GermOnline

ENSG00000101160. Homo sapiens.

Family and domain databases

InterPro

IPR025661. Pept_asp_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]

PANTHER

PTHR12411. PTHR12411. 1 hit.

Pfam

PF00112. Peptidase_C1. 1 hit.
[Graphical view]

PRINTS

PR00705. PAPAIN.

SMART

SM00645. Pept_C1. 1 hit.
[Graphical view]

PROSITE

PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. False negative.
PS00639. THIOL_PROTEASE_HIS. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9UBR2.

ChEMBL

CHEMBL4160.

ChiTaRS

CTSZ. human.

EvolutionaryTrace

Q9UBR2.

GenomeRNAi

1522.

NextBio

6299.

SOURCE

Search...

Entry information

Entry name

CATZ_HUMAN

Accession

Primary (citable) accession number: Q9UBR2
Secondary accession number(s): B2RC40 , O75331, Q9UQV5, Q9UQV6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.