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P08311

- CATG_HUMAN

UniProt

P08311 - CATG_HUMAN

Protein

Cathepsin G

Gene

CTSG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (01 Jan 1990)
      Previous versions | rss
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    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

    1. heparin binding Source: MGI
    2. peptidase activity Source: MGI
    3. serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. angiotensin maturation Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. defense response to fungus Source: Ensembl
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. immune response Source: ProtInc
    7. negative regulation of growth of symbiont in host Source: Ensembl
    8. neutrophil mediated killing of gram-positive bacterium Source: Ensembl
    9. positive regulation of immune response Source: Ensembl
    10. proteolysis Source: UniProtKB
    11. response to lipopolysaccharide Source: Ensembl

    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: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:2532. CTSG.

    Subcellular locationi

    Cell surface 1 Publication

    GO - Cellular componenti

    1. cell surface Source: UniProtKB-SubCell
    2. extracellular region Source: Reactome
    3. extracellular space Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProt
    5. nucleus Source: UniProt
    6. plasma membrane Source: UniProtKB
    7. secretory granule Source: MGI

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27032.

    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.
    GenevestigatoriP08311.

    Organism-specific databases

    HPAiCAB000110.
    HPA047737.

    Interactioni

    Protein-protein interaction databases

    BioGridi107891. 6 interactions.
    IntActiP08311. 2 interactions.
    MINTiMINT-4054534.
    STRINGi9606.ENSP00000216336.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiP08311.
    KOiK01319.
    OMAiQHITARR.
    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

    MQPLLLLLAF LLPTGAEAGE IIGGRESRPH SRPYMAYLQI QSPAGQSRCG    50
    GFLVREDFVL TAAHCWGSNI NVTLGAHNIQ RRENTQQHIT ARRAIRHPQY 100
    NQRTIQNDIM LLQLSRRVRR NRNVNPVALP RAQEGLRPGT LCTVAGWGRV 150
    SMRRGTDTLR EVQLRVQRDR QCLRIFGSYD PRRQICVGDR RERKAAFKGD 200
    SGGPLLCNNV AHGIVSYGKS SGVPPEVFTR VSSFLPWIRT TMRSFKLLDQ 250
    METPL 255
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi115725.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS9631.1.
    PIRi A32627. A27122.
    RefSeqi NP_001902.1. NM_001911.2.
    UniGenei Hs.421724.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AU8 X-ray 1.90 A 21-244 [» ]
    1CGH X-ray 1.80 A 21-244 [» ]
    1KYN X-ray 3.50 A/B 21-255 [» ]
    1T32 X-ray 1.85 A 21-239 [» ]
    ProteinModelPortali P08311.
    SMRi P08311. Positions 21-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107891. 6 interactions.
    IntActi P08311. 2 interactions.
    MINTi MINT-4054534.
    STRINGi 9606.ENSP00000216336.

    Chemistry

    BindingDBi P08311.
    ChEMBLi CHEMBL4071.
    GuidetoPHARMACOLOGYi 2348.

    Protein family/group databases

    MEROPSi S01.133.

    PTM databases

    PhosphoSitei P08311.

    Polymorphism databases

    DMDMi 115725.

    Proteomic databases

    MaxQBi P08311.
    PaxDbi P08311.
    PeptideAtlasi P08311.
    PRIDEi P08311.

    Protocols and materials databases

    DNASUi 1511.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216336 ; ENSP00000216336 ; ENSG00000100448 .
    GeneIDi 1511.
    KEGGi hsa:1511.
    UCSCi uc001wpq.3. human.

    Organism-specific databases

    CTDi 1511.
    GeneCardsi GC14M025042.
    HGNCi HGNC:2532. CTSG.
    HPAi CAB000110.
    HPA047737.
    MIMi 116830. gene.
    neXtProti NX_P08311.
    PharmGKBi PA27032.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251820.
    HOVERGENi HBG013304.
    InParanoidi P08311.
    KOi K01319.
    OMAi QHITARR.
    OrthoDBi EOG7RRF7Z.
    PhylomeDBi P08311.
    TreeFami TF333630.

    Enzyme and pathway databases

    BRENDAi 3.4.21.20. 2681.
    Reactomei REACT_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-RK P08311.

    Miscellaneous databases

    EvolutionaryTracei P08311.
    GeneWikii Cathepsin_G.
    GenomeRNAii 1511.
    NextBioi 6257.
    PMAP-CutDB P08311.
    PROi P08311.
    SOURCEi Search...

    Gene expression databases

    Bgeei P08311.
    CleanExi HS_CTSG.
    Genevestigatori P08311.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 150 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