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O70138

- MMP8_MOUSE

UniProt

O70138 - MMP8_MOUSE

Protein

Neutrophil collagenase

Gene

Mmp8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Can degrade fibrillar type I, II, and III collagens. May play a role in the degradation of collagen fibers during uterine involution.

    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. Activated by matrilysin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi91 – 911Zinc 2; in inhibited formBy similarity
    Metal bindingi157 – 1571Calcium 1By similarity
    Metal bindingi167 – 1671Zinc 1By similarity
    Metal bindingi169 – 1691Zinc 1By similarity
    Metal bindingi174 – 1741Calcium 2By similarity
    Metal bindingi175 – 1751Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi177 – 1771Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi179 – 1791Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi182 – 1821Zinc 1By similarity
    Metal bindingi189 – 1891Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi191 – 1911Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi193 – 1931Calcium 1By similarity
    Metal bindingi195 – 1951Zinc 1By similarity
    Metal bindingi197 – 1971Calcium 2By similarity
    Metal bindingi200 – 2001Calcium 2By similarity
    Metal bindingi217 – 2171Zinc 2; catalyticBy similarity
    Active sitei218 – 2181PROSITE-ProRule annotation
    Metal bindingi221 – 2211Zinc 2; catalyticBy similarity
    Metal bindingi227 – 2271Zinc 2; catalyticBy similarity
    Metal bindingi286 – 2861Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi378 – 3781Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi425 – 4251Calcium 3; via carbonyl oxygenBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neutrophil collagenase (EC:3.4.24.34)
    Alternative name(s):
    Collagenase 2
    Matrix metalloproteinase-8
    Short name:
    MMP-8
    Gene namesi
    Name:Mmp8
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1202395. Mmp8.

    Subcellular locationi

    Cytoplasmic granule. Secretedextracellular spaceextracellular matrix
    Note: Stored in intracellular granules and released during inflammatory conditions.

    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 – 10080Activation peptidePRO_0000028746Add
    BLAST
    Chaini101 – 465365Neutrophil collagenasePRO_0000028747Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi279 ↔ 464By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PRIDEiO70138.

    PTM databases

    PhosphoSiteiO70138.

    Expressioni

    Tissue specificityi

    Neutrophils. Expressed in uterus. Low levels in kidney and muscle.

    Developmental stagei

    Expressed in late embryogenesis and in the involuting postpartum uterus.

    Gene expression databases

    BgeeiO70138.
    CleanExiMM_MMP8.
    GenevestigatoriO70138.

    Structurei

    3D structure databases

    ProteinModelPortaliO70138.
    SMRiO70138. Positions 32-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati276 – 32550Hemopexin 1Add
    BLAST
    Repeati326 – 37247Hemopexin 2Add
    BLAST
    Repeati374 – 42047Hemopexin 3Add
    BLAST
    Repeati421 – 46444Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi89 – 968Cysteine 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.
    GeneTreeiENSGT00730000110530.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiQ6GTR5.
    KOiK01402.
    OMAiYAFREPS.
    OrthoDBiEOG7XPZ57.
    TreeFamiTF315428.

    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. 3 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.

    O70138-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFRLKTLPLL IFLHTQLANA FPVPEHLEEK NIKTAENYLR KFYNLPSNQF    50
    RSSRNATMVA EKLKEMQRFF SLAETGKLDA ATMGIMEMPR CGVPDSGDFL 100
    LTPGSPKWTH TNLTYRIINH TPQLSRAEVK TAIEKAFHVW SVASPLTFTE 150
    ILQGEADINI AFVSRDHGDN SPFDGPNGIL AHAFQPGQGI GGDAHFDSEE 200
    TWTQDSKNYN LFLVAAHEFG HSLGLSHSTD PGALMYPNYA YREPSTYSLP 250
    QDDINGIQTI YGPSDNPIQP TGPSTPKACD PHLRFDATTT LRGEIYFFKD 300
    KYFWRRHPQL RTVDLNFISL FWPFLPNGLQ AAYEDFDRDL VFLFKGRQYW 350
    ALSGYDLQQG YPRDISNYGF PRSVQAIDAA VSYNGKTYFF INNQCWRYDN 400
    QRRSMDPGYP KSIPSMFPGV NCRVDAVFLQ DSFFLFFSGP QYFAFNFVSH 450
    RVTRVARSNL WLNCS 465
    Length:465
    Mass (Da):53,126
    Last modified:July 27, 2011 - v2
    Checksum:i448AEC59639E9237
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti116 – 1161R → W in AAC12707. (PubMed:9516153)Curated
    Sequence conflicti300 – 3001D → E in AAC12707. (PubMed:9516153)Curated
    Sequence conflicti324 – 3241F → G in AAC12707. (PubMed:9516153)Curated
    Sequence conflicti401 – 4011Q → E in AAC12707. (PubMed:9516153)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96696 mRNA. Translation: AAC12707.1.
    Y13342 mRNA. Translation: CAA73786.1.
    AK089234 mRNA. Translation: BAC40805.1.
    AK137468 mRNA. Translation: BAE23365.1.
    AK154937 mRNA. Translation: BAE32938.1.
    CH466522 Genomic DNA. Translation: EDL24937.1.
    BC042742 mRNA. Translation: AAH42742.1.
    CCDSiCCDS22808.1.
    RefSeqiNP_032637.3. NM_008611.4.
    UniGeneiMm.16415.

    Genome annotation databases

    EnsembliENSMUST00000018765; ENSMUSP00000018765; ENSMUSG00000005800.
    GeneIDi17394.
    KEGGimmu:17394.
    UCSCiuc009ocr.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96696 mRNA. Translation: AAC12707.1 .
    Y13342 mRNA. Translation: CAA73786.1 .
    AK089234 mRNA. Translation: BAC40805.1 .
    AK137468 mRNA. Translation: BAE23365.1 .
    AK154937 mRNA. Translation: BAE32938.1 .
    CH466522 Genomic DNA. Translation: EDL24937.1 .
    BC042742 mRNA. Translation: AAH42742.1 .
    CCDSi CCDS22808.1.
    RefSeqi NP_032637.3. NM_008611.4.
    UniGenei Mm.16415.

    3D structure databases

    ProteinModelPortali O70138.
    SMRi O70138. Positions 32-464.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M10.002.

    PTM databases

    PhosphoSitei O70138.

    Proteomic databases

    PRIDEi O70138.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000018765 ; ENSMUSP00000018765 ; ENSMUSG00000005800 .
    GeneIDi 17394.
    KEGGi mmu:17394.
    UCSCi uc009ocr.2. mouse.

    Organism-specific databases

    CTDi 4317.
    MGIi MGI:1202395. Mmp8.

    Phylogenomic databases

    eggNOGi NOG258253.
    GeneTreei ENSGT00730000110530.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi Q6GTR5.
    KOi K01402.
    OMAi YAFREPS.
    OrthoDBi EOG7XPZ57.
    TreeFami TF315428.

    Enzyme and pathway databases

    Reactomei REACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.

    Miscellaneous databases

    ChiTaRSi MMP8. mouse.
    NextBioi 292028.
    PROi O70138.
    SOURCEi Search...

    Gene expression databases

    Bgeei O70138.
    CleanExi MM_MMP8.
    Genevestigatori O70138.

    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. 3 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. "Isolation and characterization of the cDNA for mouse neutrophil collagenase: demonstration of shared negative regulatory pathways for neutrophil secondary granule protein gene expression."
      Lawson N.D., Khanna-Gupta A., Berliner N.
      Blood 91:2517-2524(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Collagenase 2 (MMP-8) expression in murine tissue-remodelling processes. Analysis of its potential role in postpartum involution of the uterus."
      Balbin M., Fueyo A., Knaeuper V., Pendas A.M., Lopez J.M., Jimenez M.G., Murphy G., Lopez-Otin C.
      J. Biol. Chem. 273:23959-23968(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129/Sv.
      Tissue: Embryo.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Bone and Dendritic cell.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      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].
      Strain: 129.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiMMP8_MOUSE
    AccessioniPrimary (citable) accession number: O70138
    Secondary accession number(s): O88733, Q6GTR5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 130 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3