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Protein

Cathepsin Z

Gene

Ctsz

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Capable of producing kinin potentiating peptides.

Catalytic activityi

Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity.

Kineticsi

  1. KM=6.6 µM for the synthetic substrate Z-Phe-Arg-NMec

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei94 – 941PROSITE-ProRule annotation
    Active sitei243 – 2431PROSITE-ProRule annotation
    Active sitei264 – 2641PROSITE-ProRule annotation

    GO - Molecular functioni

    • cysteine-type endopeptidase activity Source: RGD

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    ReactomeiR-RNO-2022377. Metabolism of Angiotensinogen to Angiotensins.
    R-RNO-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
    R-RNO-432720. Lysosome Vesicle Biogenesis.
    R-RNO-5694530. Cargo concentration in the ER.

    Protein family/group databases

    MEROPSiC01.125.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cathepsin Z (EC:3.4.18.1)
    Alternative name(s):
    Cathepsin Y
    Gene namesi
    Name:Ctsz
    Synonyms:Ctsy
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 3

    Organism-specific databases

    RGDi708479. Ctsz.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence analysisAdd
    BLAST
    Propeptidei26 – 6338Activation peptideBy similarityPRO_0000026289Add
    BLAST
    Chaini64 – 306243Cathepsin ZPRO_0000026290Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi91 ↔ 134By similarity
    Disulfide bondi128 ↔ 166By similarity
    Disulfide bondi156 ↔ 172By similarity
    Disulfide bondi175 ↔ 181By similarity
    Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence analysis
    Disulfide bondi216 ↔ 299By similarity
    Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ9R1T3.
    PRIDEiQ9R1T3.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    GenevisibleiQ9R1T3. RN.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000066523.

    Chemistry

    BindingDBiQ9R1T3.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R1T3.
    SMRiQ9R1T3. Positions 32-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG1543. Eukaryota.
    COG4870. LUCA.
    GeneTreeiENSGT00780000121937.
    HOVERGENiHBG004456.
    InParanoidiQ9R1T3.
    KOiK08568.
    OMAiQCGTCTE.
    OrthoDBiEOG751NFZ.
    PhylomeDBiQ9R1T3.

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR000668. Peptidase_C1A_C.
    [Graphical view]
    PfamiPF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9R1T3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASSGSVQQL RLVLLMLLLA GAARASLYFR PGQTCYRPLH RDHLALLGRR
    60 70 80 90 100
    TYPRPHEYLS PADLPKNWDW RNVNGVNYAS VTRNQHIPQY CGSCWAHGST
    110 120 130 140 150
    SALADRINIK RKGAWPSTLL SVQNVIDCGN AGSCEGGNDL PVWEYAHKHG
    160 170 180 190 200
    IPDETCNNYQ AKDQECDKFN QCGTCTEFKE CHTIQNYTLW RVGDYGSLSG
    210 220 230 240 250
    REKMMAEIYA NGPISCGIMA TERMSNYTGG IYTEYQNQAI INHIISVAGW
    260 270 280 290 300
    GVSNDGIEYW IVRNSWGEPW GERGWMRIVT STYKGGTGSS YNLAIEEACT

    FGDPIV
    Length:306
    Mass (Da):34,194
    Last modified:September 19, 2003 - v2
    Checksum:iA4B3C6646087BCB5
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB023781 mRNA. Translation: BAA82844.2.
    BC091110 mRNA. Translation: AAH91110.1.
    RefSeqiNP_899159.1. NM_183330.1.
    UniGeneiRn.1475.

    Genome annotation databases

    EnsembliENSRNOT00000072069; ENSRNOP00000066523; ENSRNOG00000050697.
    GeneIDi252929.
    KEGGirno:252929.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB023781 mRNA. Translation: BAA82844.2.
    BC091110 mRNA. Translation: AAH91110.1.
    RefSeqiNP_899159.1. NM_183330.1.
    UniGeneiRn.1475.

    3D structure databases

    ProteinModelPortaliQ9R1T3.
    SMRiQ9R1T3. Positions 32-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000066523.

    Chemistry

    BindingDBiQ9R1T3.

    Protein family/group databases

    MEROPSiC01.125.

    Proteomic databases

    PaxDbiQ9R1T3.
    PRIDEiQ9R1T3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000072069; ENSRNOP00000066523; ENSRNOG00000050697.
    GeneIDi252929.
    KEGGirno:252929.

    Organism-specific databases

    CTDi1522.
    RGDi708479. Ctsz.

    Phylogenomic databases

    eggNOGiKOG1543. Eukaryota.
    COG4870. LUCA.
    GeneTreeiENSGT00780000121937.
    HOVERGENiHBG004456.
    InParanoidiQ9R1T3.
    KOiK08568.
    OMAiQCGTCTE.
    OrthoDBiEOG751NFZ.
    PhylomeDBiQ9R1T3.

    Enzyme and pathway databases

    ReactomeiR-RNO-2022377. Metabolism of Angiotensinogen to Angiotensins.
    R-RNO-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
    R-RNO-432720. Lysosome Vesicle Biogenesis.
    R-RNO-5694530. Cargo concentration in the ER.

    Miscellaneous databases

    PROiQ9R1T3.

    Gene expression databases

    GenevisibleiQ9R1T3. RN.

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR000668. Peptidase_C1A_C.
    [Graphical view]
    PfamiPF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Determination of the mRNA sequence of cathepsin Y, a cysteine endopeptidase from rat spleen, and confirmation of its ubiquitous expression."
      Nakazono E., Kamata Y., Yamafuji K.
      Biol. Chem. 383:1971-1975(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CHARACTERIZATION.
      Strain: Wistar.
      Tissue: Spleen.
    2. "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: Thymus.
    3. "Cathepsin Y (a novel thiol enzyme) produces kinin potentiating peptide from the component protein of rat plasma."
      Sakamoto E., Sakao Y., Taniguchi Y., Yamafuji K.
      Immunopharmacology 45:207-214(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE OF 64-306.
      Strain: Wistar.
      Tissue: Spleen.

    Entry informationi

    Entry nameiCATZ_RAT
    AccessioniPrimary (citable) accession number: Q9R1T3
    Secondary accession number(s): Q5BKD9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: September 19, 2003
    Last modified: July 6, 2016
    This is version 103 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.