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O88766

- MMP8_RAT

UniProt

O88766 - MMP8_RAT

Protein

Neutrophil collagenase

Gene

Mmp8

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Can degrade fibrillar type I, II, and III collagens.

    Catalytic activityi

    Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.

    Cofactori

    Binds 3 calcium ions per subunit.By similarity
    Binds 2 zinc ions per subunit.By similarity

    Enzyme regulationi

    Cannot be activated without removal of the activation peptide.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi92 – 921Zinc 2; in inhibited formBy similarity
    Metal bindingi158 – 1581Calcium 1By similarity
    Metal bindingi168 – 1681Zinc 1By similarity
    Metal bindingi170 – 1701Zinc 1By similarity
    Metal bindingi175 – 1751Calcium 2By similarity
    Metal bindingi176 – 1761Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi178 – 1781Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi180 – 1801Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi183 – 1831Zinc 1By similarity
    Metal bindingi190 – 1901Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi192 – 1921Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi194 – 1941Calcium 1By similarity
    Metal bindingi196 – 1961Zinc 1By similarity
    Metal bindingi198 – 1981Calcium 2By similarity
    Metal bindingi201 – 2011Calcium 2By similarity
    Metal bindingi218 – 2181Zinc 2; catalyticBy similarity
    Active sitei219 – 2191PROSITE-ProRule annotation
    Metal bindingi222 – 2221Zinc 2; catalyticBy similarity
    Metal bindingi228 – 2281Zinc 2; catalyticBy similarity
    Metal bindingi287 – 2871Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi379 – 3791Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi426 – 4261Calcium 3; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: RGD
    2. metalloendopeptidase activity Source: InterPro
    3. metallopeptidase activity Source: RGD
    4. serine-type endopeptidase activity Source: UniProtKB
    5. zinc ion binding Source: RGD

    GO - Biological processi

    1. collagen catabolic process Source: UniProtKB-KW
    2. ossification Source: RGD
    3. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM10.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neutrophil collagenase (EC:3.4.24.34)
    Alternative name(s):
    Matrix metalloproteinase-8
    Short name:
    MMP-8
    Gene namesi
    Name:Mmp8
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi631408. Mmp8.

    Subcellular locationi

    Cytoplasmic granule. Secretedextracellular spaceextracellular matrix By similarity
    Note: Stored in intracellular granules.

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020By similarityAdd
    BLAST
    Propeptidei21 – 10181Activation peptideBy similarityPRO_0000028748Add
    BLAST
    Chaini102 – 466365Neutrophil collagenasePRO_0000028749Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi56 – 561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi280 ↔ 465Curated

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiO88766.
    PRIDEiO88766.

    Expressioni

    Gene expression databases

    GenevestigatoriO88766.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000013936.

    Structurei

    3D structure databases

    ProteinModelPortaliO88766.
    SMRiO88766. Positions 100-263.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati277 – 32650Hemopexin 1Add
    BLAST
    Repeati327 – 37347Hemopexin 2Add
    BLAST
    Repeati375 – 42147Hemopexin 3Add
    BLAST
    Repeati422 – 46544Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi90 – 978Cysteine switchBy similarity

    Domaini

    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

    Sequence similaritiesi

    Belongs to the peptidase M10A family.Curated
    Contains 4 hemopexin repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG258253.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiO88766.
    KOiK01402.
    PhylomeDBiO88766.

    Family and domain databases

    Gene3Di2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR028709. MMP8.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF137. PTHR10201:SF137. 1 hit.
    PfamiPF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSiPR00138. MATRIXIN.
    SMARTiSM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O88766-1 [UniParc]FASTAAdd to Basket

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    MLHLKTLPFL FFFHTQLATA LPVPPEHLEE KNMKTAENYL RKFYHLPSNQ    50
    FRSARNATMI AEKLKEMQRF FGLPETGKPD AATIEIMEKP RCGVPDSGDF 100
    LLTPGSPKWT HTNLTYRIIN HTPQMSKAEV KTEIEKAFKI WSVPSTLTFT 150
    ETLEGEADIN IAFVSRDHGD NSPFDGPNGI LAHAFQPGRG IGGDAHFDSE 200
    ETWTQDSKNY NLFLVAAHEF GHSLGLSHST DPGALMYPNY AYREPSTYSL 250
    PQDDINGIQT IYGPSDNPVQ PTGPSTPTAC DPHLRFDAAT TLRGEIYFFK 300
    DKYFWRRHPQ LRTVDLNFIS LFWPFLPNGL QAAYEDFDRD LVFLFKGRQY 350
    WALSAYDLQQ GYPRDISNYG FPRSVQAIDA AVSYNGKTYF FVNNQCWRYD 400
    NQRRSMDPGY PTSIASVFPG INCRIDAVFQ QDSFFLFFSG PQYFAFNLVS 450
    RRVTRVARSN LWLNCP 466
    Length:466
    Mass (Da):53,277
    Last modified:November 1, 1998 - v1
    Checksum:i8B9DE97576E76C90
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007288 mRNA. Translation: CAA07432.1.
    RefSeqiNP_071557.1. NM_022221.1.
    UniGeneiRn.44474.

    Genome annotation databases

    GeneIDi63849.
    KEGGirno:63849.
    UCSCiRGD:631408. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007288 mRNA. Translation: CAA07432.1 .
    RefSeqi NP_071557.1. NM_022221.1.
    UniGenei Rn.44474.

    3D structure databases

    ProteinModelPortali O88766.
    SMRi O88766. Positions 100-263.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000013936.

    Chemistry

    BindingDBi O88766.
    ChEMBLi CHEMBL2312.

    Protein family/group databases

    MEROPSi M10.002.

    Proteomic databases

    PaxDbi O88766.
    PRIDEi O88766.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 63849.
    KEGGi rno:63849.
    UCSCi RGD:631408. rat.

    Organism-specific databases

    CTDi 4317.
    RGDi 631408. Mmp8.

    Phylogenomic databases

    eggNOGi NOG258253.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi O88766.
    KOi K01402.
    PhylomeDBi O88766.

    Miscellaneous databases

    NextBioi 612456.
    PROi O88766.

    Gene expression databases

    Genevestigatori O88766.

    Family and domain databases

    Gene3Di 2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR028709. MMP8.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF137. PTHR10201:SF137. 1 hit.
    Pfami PF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSi PR00138. MATRIXIN.
    SMARTi SM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, characterization and activation properties of rat neutrophil collagenase (MMP-8)."
      Overall C.M., Lowne D., Wells G., Burel S., Clements J.M.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Lewis.

    Entry informationi

    Entry nameiMMP8_RAT
    AccessioniPrimary (citable) accession number: O88766
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 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

    External Data

    Dasty 3