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Q9UBR2 (CATZ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cathepsin Z

EC=3.4.18.1
Alternative name(s):
Cathepsin P
Cathepsin X
Gene names
Name:CTSZ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 6138Activation peptide
PRO_0000026285
Chain62 – 303242Cathepsin Z
PRO_0000026286

Sites

Active site921
Active site2411
Active site2611

Amino acid modifications

Glycosylation1841N-linked (GlcNAc...) Ref.11
Glycosylation2241N-linked (GlcNAc...) Potential
Disulfide bond89 ↔ 132
Disulfide bond126 ↔ 164
Disulfide bond154 ↔ 170
Disulfide bond173 ↔ 179
Disulfide bond214 ↔ 296

Natural variations

Natural variant361P → S. Ref.1
VAR_010254
Natural variant1291A → R Requires 2 nucleotide substitutions. Ref.1
VAR_010255
Natural variant2861A → T.
Corresponds to variant rs34069356 [ dbSNP | Ensembl ].
VAR_033719

Experimental info

Sequence conflict481S → T in AAC39839. Ref.2
Sequence conflict1501P → S in AAC61477. Ref.1

Secondary structure

................................................. 303
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UBR2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6274FD1974D0EBDC

FASTA30333,868
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
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.
RefSeqNP_001327.2. NM_001336.3.
UniGeneHs.252549.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEUX-ray1.70A/B27-303[»]
1EF7X-ray2.67A/B62-303[»]
ProteinModelPortalQ9UBR2.
SMRQ9UBR2. Positions 29-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107902. 2 interactions.
IntActQ9UBR2. 1 interaction.
MINTMINT-3079312.
STRING9606.ENSP00000217131.

Chemistry

BindingDBQ9UBR2.
ChEMBLCHEMBL4160.

Protein family/group databases

MEROPSC01.013.

Polymorphism databases

DMDM12643324.

Proteomic databases

PaxDbQ9UBR2.
PeptideAtlasQ9UBR2.
PRIDEQ9UBR2.

Protocols and materials databases

DNASU1522.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217131; ENSP00000217131; ENSG00000101160.
GeneID1522.
KEGGhsa:1522.
UCSCuc002yai.2. human.

Organism-specific databases

CTD1522.
GeneCardsGC20M057570.
HGNCHGNC:2547. CTSZ.
HPACAB025114.
HPA049876.
MIM603169. gene.
neXtProtNX_Q9UBR2.
PharmGKBPA27043.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4870.
HOGENOMHOG000264454.
HOVERGENHBG004456.
InParanoidQ9UBR2.
KOK08568.
OMAQCGTCTE.
OrthoDBEOG751NFZ.
PhylomeDBQ9UBR2.
TreeFamTF313225.

Enzyme and pathway databases

BRENDA3.4.18.1. 2681.
ReactomeREACT_11123. Membrane Trafficking.
REACT_17015. Metabolism of proteins.

Gene expression databases

BgeeQ9UBR2.
CleanExHS_CTSZ.
GenevestigatorQ9UBR2.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTSZ. human.
EvolutionaryTraceQ9UBR2.
GeneWikiCathepsin_Z.
GenomeRNAi1522.
NextBio6299.
PROQ9UBR2.
SOURCESearch...

Entry information

Entry nameCATZ_HUMAN
AccessionPrimary (citable) accession number: Q9UBR2
Secondary accession number(s): B2RC40 expand/collapse secondary AC list , O75331, Q9UQV5, Q9UQV6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM