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Protein

Cathepsin G

Gene

CTSG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine protease with trypsin- and chymotrypsin-like specificity. Cleaves complement C3. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, antibacterial activity is inhibited by LPS from P.aeruginosa, Z-Gly-Leu-Phe-CH2Cl and phenylmethylsulfonyl fluoride.3 Publications

Catalytic activityi

Specificity similar to chymotrypsin C.

Enzyme regulationi

Inhibited by soybean trypsin inhibitor, benzamidine, the synthetic peptide R13K, Z-Gly-Leu-Phe-CH2Cl, phenylmethylsulfonyl fluoride, 3,4-dichloroisocoumarin, DFP, SBTI and alpha-1-antitrypsin. Inhibited by LPS from P.aeruginosa but not by LPS from S.minnesota. Not inhibited by elastinal, CMK, TLCK and ETDA.3 Publications

Kineticsi

  1. KM=1.15 mM for Z-Lys-SBzl1 Publication
  2. KM=0.26 mM for Suc-Ala-Ala-Pro-Phe-SBzl1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei64 – 641Charge relay system
    Active sitei108 – 1081Charge relay system
    Active sitei201 – 2011Charge relay system

    GO - Molecular functioni

    • heparin binding Source: MGI
    • peptidase activity Source: MGI
    • serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    BRENDAi3.4.21.20. 2681.
    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
    SABIO-RKP08311.

    Protein family/group databases

    MEROPSiS01.133.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cathepsin G (EC:3.4.21.20)
    Short name:
    CG
    Gene namesi
    Name:CTSG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:2532. CTSG.

    Subcellular locationi

    GO - Cellular componenti

    • cell surface Source: UniProtKB-SubCell
    • cytoplasm Source: GO_Central
    • extracellular exosome Source: UniProtKB
    • extracellular region Source: Reactome
    • extracellular space Source: BHF-UCL
    • nucleus Source: UniProtKB
    • plasma membrane Source: UniProtKB
    • secretory granule Source: MGI
    Complete GO annotation...

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27032.

    Polymorphism and mutation databases

    BioMutaiCTSG.
    DMDMi115725.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Add
    BLAST
    Propeptidei19 – 202Activation peptide5 PublicationsPRO_0000027512
    Chaini21 – 255235Cathepsin GPRO_0000027513Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi49 ↔ 65
    Glycosylationi71 – 711N-linked (GlcNAc...)
    Disulfide bondi142 ↔ 207
    Disulfide bondi172 ↔ 186

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP08311.
    PaxDbiP08311.
    PeptideAtlasiP08311.
    PRIDEiP08311.

    PTM databases

    PhosphoSiteiP08311.

    Miscellaneous databases

    PMAP-CutDBP08311.

    Expressioni

    Gene expression databases

    BgeeiP08311.
    CleanExiHS_CTSG.
    GenevisibleiP08311. HS.

    Organism-specific databases

    HPAiCAB000110.
    HPA047737.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KRT31Q153233EBI-5462635,EBI-948001
    NOTCH2NLQ7Z3S93EBI-5462635,EBI-945833

    Protein-protein interaction databases

    BioGridi107891. 16 interactions.
    IntActiP08311. 4 interactions.
    MINTiMINT-4054534.
    STRINGi9606.ENSP00000216336.

    Structurei

    Secondary structure

    1
    255
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 417Combined sources
    Turni42 – 454Combined sources
    Beta strandi48 – 558Combined sources
    Beta strandi58 – 614Combined sources
    Helixi63 – 653Combined sources
    Beta strandi68 – 758Combined sources
    Beta strandi87 – 9610Combined sources
    Turni102 – 1054Combined sources
    Beta strandi110 – 1167Combined sources
    Beta strandi141 – 1477Combined sources
    Beta strandi150 – 1534Combined sources
    Beta strandi160 – 1667Combined sources
    Helixi169 – 1757Combined sources
    Turni181 – 1833Combined sources
    Beta strandi184 – 1874Combined sources
    Beta strandi204 – 2074Combined sources
    Beta strandi210 – 2178Combined sources
    Beta strandi226 – 2305Combined sources
    Helixi231 – 2344Combined sources
    Helixi235 – 2439Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AU8X-ray1.90A21-244[»]
    1CGHX-ray1.80A21-244[»]
    1KYNX-ray3.50A/B21-255[»]
    1T32X-ray1.85A21-239[»]
    ProteinModelPortaliP08311.
    SMRiP08311. Positions 21-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08311.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 243223Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00760000118895.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiP08311.
    KOiK01319.
    OMAiLCNNVAH.
    OrthoDBiEOG7RRF7Z.
    PhylomeDBiP08311.
    TreeFamiTF333630.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P08311-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQPLLLLLAF LLPTGAEAGE IIGGRESRPH SRPYMAYLQI QSPAGQSRCG
    60 70 80 90 100
    GFLVREDFVL TAAHCWGSNI NVTLGAHNIQ RRENTQQHIT ARRAIRHPQY
    110 120 130 140 150
    NQRTIQNDIM LLQLSRRVRR NRNVNPVALP RAQEGLRPGT LCTVAGWGRV
    160 170 180 190 200
    SMRRGTDTLR EVQLRVQRDR QCLRIFGSYD PRRQICVGDR RERKAAFKGD
    210 220 230 240 250
    SGGPLLCNNV AHGIVSYGKS SGVPPEVFTR VSSFLPWIRT TMRSFKLLDQ

    METPL
    Length:255
    Mass (Da):28,837
    Last modified:January 1, 1990 - v2
    Checksum:i6228E741E6A43889
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti125 – 1251N → S.1 Publication
    Corresponds to variant rs45567233 [ dbSNP | Ensembl ].
    VAR_006491

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M16117 mRNA. Translation: AAA52126.1.
    J04990 Genomic DNA. Translation: AAA51919.1.
    CR456807 mRNA. Translation: CAG33088.1.
    CR541704 mRNA. Translation: CAG46505.1.
    CH471078 Genomic DNA. Translation: EAW66006.1.
    BC014460 mRNA. Translation: AAH14460.1.
    CCDSiCCDS9631.1.
    PIRiA32627. A27122.
    RefSeqiNP_001902.1. NM_001911.2.
    UniGeneiHs.421724.

    Genome annotation databases

    EnsembliENST00000216336; ENSP00000216336; ENSG00000100448.
    GeneIDi1511.
    KEGGihsa:1511.
    UCSCiuc001wpq.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M16117 mRNA. Translation: AAA52126.1.
    J04990 Genomic DNA. Translation: AAA51919.1.
    CR456807 mRNA. Translation: CAG33088.1.
    CR541704 mRNA. Translation: CAG46505.1.
    CH471078 Genomic DNA. Translation: EAW66006.1.
    BC014460 mRNA. Translation: AAH14460.1.
    CCDSiCCDS9631.1.
    PIRiA32627. A27122.
    RefSeqiNP_001902.1. NM_001911.2.
    UniGeneiHs.421724.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AU8X-ray1.90A21-244[»]
    1CGHX-ray1.80A21-244[»]
    1KYNX-ray3.50A/B21-255[»]
    1T32X-ray1.85A21-239[»]
    ProteinModelPortaliP08311.
    SMRiP08311. Positions 21-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107891. 16 interactions.
    IntActiP08311. 4 interactions.
    MINTiMINT-4054534.
    STRINGi9606.ENSP00000216336.

    Chemistry

    BindingDBiP08311.
    ChEMBLiCHEMBL4071.
    GuidetoPHARMACOLOGYi2348.

    Protein family/group databases

    MEROPSiS01.133.

    PTM databases

    PhosphoSiteiP08311.

    Polymorphism and mutation databases

    BioMutaiCTSG.
    DMDMi115725.

    Proteomic databases

    MaxQBiP08311.
    PaxDbiP08311.
    PeptideAtlasiP08311.
    PRIDEiP08311.

    Protocols and materials databases

    DNASUi1511.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000216336; ENSP00000216336; ENSG00000100448.
    GeneIDi1511.
    KEGGihsa:1511.
    UCSCiuc001wpq.3. human.

    Organism-specific databases

    CTDi1511.
    GeneCardsiGC14M025042.
    HGNCiHGNC:2532. CTSG.
    HPAiCAB000110.
    HPA047737.
    MIMi116830. gene.
    neXtProtiNX_P08311.
    PharmGKBiPA27032.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00760000118895.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiP08311.
    KOiK01319.
    OMAiLCNNVAH.
    OrthoDBiEOG7RRF7Z.
    PhylomeDBiP08311.
    TreeFamiTF333630.

    Enzyme and pathway databases

    BRENDAi3.4.21.20. 2681.
    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
    SABIO-RKP08311.

    Miscellaneous databases

    EvolutionaryTraceiP08311.
    GeneWikiiCathepsin_G.
    GenomeRNAii1511.
    NextBioi6257.
    PMAP-CutDBP08311.
    PROiP08311.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP08311.
    CleanExiHS_CTSG.
    GenevisibleiP08311. HS.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases."
      Salvesen G., Farley D., Shuman J., Przybyla A., Reilly C., Travis J.
      Biochemistry 26:2289-2293(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Genomic organization and chromosomal localization of the human cathepsin G gene."
      Hohn P.A., Popescu N.C., Hanson R.D., Salvesen G., Ley T.J.
      J. Biol. Chem. 264:13412-13419(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Skin.
    6. "Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G."
      Avril L.E., Di Martino-Ferrer M., Pignede G., Seman M., Gauthier F.
      FEBS Lett. 345:81-86(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-52, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
      Tissue: Monocyte.
    7. "Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors."
      Heck L.W., Rostand K.S., Hunter F.A., Bhown A.
      Anal. Biochem. 158:217-227(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-45.
    8. Cited for: PROTEIN SEQUENCE OF 21-36.
    9. "Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G."
      Maison C.M., Villiers C.L., Colomb M.G.
      J. Immunol. 147:921-926(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-30, FUNCTION, ENZYME REGULATION.
      Tissue: Monocyte.
    10. "Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis."
      Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D.
      J. Immunol. Methods 180:25-33(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-30.
      Tissue: Neutrophil.
    11. "Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa."
      Wasiluk K.R., Skubitz K.M., Gray B.H.
      Infect. Immun. 59:4193-4200(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A MICROBICIDE, ENZYME REGULATION.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities."
      Hof P., Mayr I., Huber R., Korzus E., Potempa J., Travis J., Powers J.C., Bode W.
      EMBO J. 15:5481-5491(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    14. Medrano F.J., Bode W., Banbula A., Potempa J.
      Submitted (SEP-1997) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    15. "Sequence variant of the human cathepsin G gene."
      Luedecke B., Poller W., Olek K., Bartholome K.
      Hum. Genet. 91:83-84(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-125.

    Entry informationi

    Entry nameiCATG_HUMAN
    AccessioniPrimary (citable) accession number: P08311
    Secondary accession number(s): Q6IBJ6, Q9UCA5, Q9UCU6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 1, 1990
    Last modified: July 22, 2015
    This is version 159 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.