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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
(Microbial infection) Serine protease activity is inhibited by the M.tuberculosis protein Rv3364c, which leads to the suppression of downstream caspase-1-dependent apoptosis in macrophages.1 Publication

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)DescriptionActionsGraphical viewLength
    Active sitei64Charge relay system1
    Active sitei108Charge relay system1
    Active sitei201Charge relay system1

    GO - Molecular functioni

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

    GO - Biological processi

    • angiotensin maturation Source: Reactome
    • antibacterial humoral response Source: UniProtKB
    • antimicrobial humoral response Source: Reactome
    • cellular protein metabolic process Source: Reactome
    • cellular response to lipopolysaccharide Source: UniProtKB
    • defense response to fungus Source: GO_Central
    • defense response to Gram-negative bacterium Source: UniProtKB
    • extracellular matrix disassembly Source: Reactome
    • immune response Source: ProtInc
    • negative regulation of growth of symbiont in host Source: Ensembl
    • neutrophil degranulation Source: Reactome
    • neutrophil mediated killing of gram-positive bacterium Source: GO_Central
    • positive regulation of immune response Source: Ensembl
    • protein phosphorylation Source: CACAO
    • proteolysis Source: UniProtKB

    Keywordsi

    Molecular functionAntibiotic, Antimicrobial, Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    BRENDAi3.4.21.20. 2681.
    ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
    R-HSA-1592389. Activation of Matrix Metalloproteinases.
    R-HSA-2022377. Metabolism of Angiotensinogen to Angiotensins.
    R-HSA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
    R-HSA-6798695. Neutrophil degranulation.
    R-HSA-6803157. Antimicrobial peptides.
    SABIO-RKiP08311.

    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
    Proteomesi
    • UP000005640 Componenti: Chromosome 14

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000100448.3.
    HGNCiHGNC:2532. CTSG.

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Pathology & Biotechi

    Organism-specific databases

    DisGeNETi1511.
    OpenTargetsiENSG00000100448.
    PharmGKBiPA27032.

    Chemistry databases

    ChEMBLiCHEMBL4071.
    DrugBankiDB04016. 2-[3-({Methyl[1-(2-Naphthoyl)Piperidin-4-Yl]Amino}Carbonyl)-2-Naphthyl]-1-(1-Naphthyl)-2-Oxoethylphosphonic Acid.
    DB02360. Bis-Napthyl Beta-Ketophosphonic Acid.
    GuidetoPHARMACOLOGYi2348.

    Polymorphism and mutation databases

    BioMutaiCTSG.
    DMDMi115725.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 18Add BLAST18
    PropeptideiPRO_000002751219 – 20Activation peptide5 Publications2
    ChainiPRO_000002751321 – 255Cathepsin GAdd BLAST235

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi49 ↔ 65
    Glycosylationi71N-linked (GlcNAc...) asparagine1
    Disulfide bondi142 ↔ 207
    Disulfide bondi172 ↔ 186

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    EPDiP08311.
    MaxQBiP08311.
    PaxDbiP08311.
    PeptideAtlasiP08311.
    PRIDEiP08311.
    TopDownProteomicsiP08311.

    PTM databases

    iPTMnetiP08311.
    PhosphoSitePlusiP08311.

    Miscellaneous databases

    PMAP-CutDBiP08311.

    Expressioni

    Gene expression databases

    BgeeiENSG00000100448.
    CleanExiHS_CTSG.
    GenevisibleiP08311. HS.

    Organism-specific databases

    HPAiCAB000110.
    HPA047737.

    Interactioni

    Subunit structurei

    (Microbial infection) Interacts with M.tuberculosis protein Rv3364c.1 Publication

    Binary interactionsi

    Show more details

    Protein-protein interaction databases

    BioGridi107891. 17 interactors.
    CORUMiP08311.
    IntActiP08311. 6 interactors.
    MINTiMINT-4054534.
    STRINGi9606.ENSP00000216336.

    Chemistry databases

    BindingDBiP08311.

    Structurei

    Secondary structure

    1255
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi35 – 41Combined sources7
    Turni42 – 45Combined sources4
    Beta strandi48 – 55Combined sources8
    Beta strandi58 – 61Combined sources4
    Helixi63 – 65Combined sources3
    Beta strandi68 – 75Combined sources8
    Beta strandi87 – 96Combined sources10
    Turni102 – 105Combined sources4
    Beta strandi110 – 116Combined sources7
    Beta strandi141 – 147Combined sources7
    Beta strandi150 – 153Combined sources4
    Beta strandi160 – 166Combined sources7
    Helixi169 – 175Combined sources7
    Turni181 – 183Combined sources3
    Beta strandi184 – 187Combined sources4
    Beta strandi204 – 207Combined sources4
    Beta strandi210 – 217Combined sources8
    Beta strandi226 – 230Combined sources5
    Helixi231 – 234Combined sources4
    Helixi235 – 243Combined sources9

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP08311.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini21 – 243Peptidase S1PROSITE-ProRule annotationAdd BLAST223

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG3627. Eukaryota.
    COG5640. LUCA.
    GeneTreeiENSGT00760000118895.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiP08311.
    KOiK01319.
    OMAiICVGDRR.
    OrthoDBiEOG091G0G5F.
    PhylomeDBiP08311.
    TreeFamiTF333630.

    Family and domain databases

    CDDicd00190. Tryp_SPc. 1 hit.
    InterProiView protein in InterPro
    IPR009003. Peptidase_S1_PA.
    IPR001314. Peptidase_S1A.
    IPR001254. Trypsin_dom.
    IPR018114. TRYPSIN_HIS.
    IPR033116. TRYPSIN_SER.
    PfamiView protein in Pfam
    PF00089. Trypsin. 1 hit.
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiView protein in SMART
    SM00020. Tryp_SPc. 1 hit.
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiView protein in PROSITE
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.

    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)DescriptionActionsGraphical viewLength
    Natural variantiVAR_006491125N → S1 PublicationCorresponds to variant dbSNP:rs45567233Ensembl.1

    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.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Similar proteinsi

    Entry informationi

    Entry nameiCATG_HUMAN
    AccessioniPrimary (citable) accession number: P08311
    Secondary accession number(s): Q6IBJ6, Q9UCA5, Q9UCU6
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 1, 1990
    Last modified: November 22, 2017
    This is version 178 of the entry and version 2 of the sequence. See 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