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Q02853

- MMP11_MOUSE

UniProt

Q02853 - MMP11_MOUSE

Protein

Stromelysin-3

Gene

Mmp11

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    May play an important role in the progression of epithelial malignancies.

    Cofactori

    Binds 1 calcium ion per subunit.
    Binds 2 zinc ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi84 – 841Zinc 2; in inhibited formBy similarity
    Metal bindingi168 – 1681Zinc 1
    Metal bindingi170 – 1701Zinc 1
    Metal bindingi175 – 1751Calcium
    Metal bindingi176 – 1761Calcium; via carbonyl oxygen
    Metal bindingi178 – 1781Calcium; via carbonyl oxygen
    Metal bindingi180 – 1801Calcium; via carbonyl oxygen
    Metal bindingi183 – 1831Zinc 1
    Metal bindingi196 – 1961Zinc 1
    Metal bindingi219 – 2191Zinc 2; catalytic
    Active sitei220 – 2201
    Metal bindingi223 – 2231Zinc 2; catalytic
    Metal bindingi229 – 2291Zinc 2; catalytic

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: InterPro
    3. metallopeptidase activity Source: MGI
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. basement membrane organization Source: MGI
    2. collagen catabolic process Source: MGI
    3. collagen fibril organization Source: MGI
    4. extracellular matrix organization Source: MGI
    5. multicellular organismal development Source: InterPro
    6. negative regulation of fat cell differentiation Source: MGI

    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_199055. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stromelysin-3 (EC:3.4.24.-)
    Short name:
    SL-3
    Short name:
    ST3
    Alternative name(s):
    Matrix metalloproteinase-11
    Short name:
    MMP-11
    Gene namesi
    Name:Mmp11
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:97008. Mmp11.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular matrix Source: MGI
    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 – 3535Sequence AnalysisAdd
    BLAST
    Propeptidei36 – 10166Activation peptideBy similarityPRO_0000028772Add
    BLAST
    Chaini102 – 492391Stromelysin-3PRO_0000028773Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi298 ↔ 484By similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Zymogen

    Proteomic databases

    MaxQBiQ02853.
    PRIDEiQ02853.

    PTM databases

    PhosphoSiteiQ02853.

    Miscellaneous databases

    PMAP-CutDBQ02853.

    Expressioni

    Tissue specificityi

    Specifically expressed in the mammary gland during apoptosis.

    Gene expression databases

    ArrayExpressiQ02853.
    BgeeiQ02853.
    CleanExiMM_MMP11.
    GenevestigatoriQ02853.

    Interactioni

    Structurei

    Secondary structure

    1
    492
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi102 – 1054
    Beta strandi108 – 1114
    Beta strandi113 – 1186
    Helixi127 – 14216
    Beta strandi148 – 1514
    Beta strandi153 – 1564
    Beta strandi158 – 1647
    Beta strandi168 – 1714
    Beta strandi176 – 1794
    Beta strandi182 – 1854
    Beta strandi190 – 1989
    Beta strandi203 – 2064
    Beta strandi208 – 2125
    Helixi213 – 22412
    Helixi251 – 26010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HV5X-ray2.60A/B/C/D/E/F102-265[»]
    ProteinModelPortaliQ02853.
    SMRiQ02853. Positions 102-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02853.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati295 – 34349Hemopexin 1Add
    BLAST
    Repeati344 – 38643Hemopexin 2Add
    BLAST
    Repeati388 – 43649Hemopexin 3Add
    BLAST
    Repeati437 – 48448Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi82 – 898Cysteine 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

    eggNOGiNOG236137.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiQ02853.
    KOiK07993.
    OMAiVDTNEIA.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiQ02853.
    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.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR028705. Stromelysin-3.
    [Graphical view]
    PANTHERiPTHR10201:SF20. PTHR10201:SF20. 1 hit.
    PfamiPF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSiPR00138. MATRIXIN.
    SMARTiSM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50923. SSF50923. 1 hit.
    PROSITEiPS00024. 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.

    Q02853-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARAACLLRA ISRVLLLPLP LLLLLLLLLP SPLMARARPP ESHRHHPVKK    50
    GPRLLHAALP NTLTSVPASH WVPSPAGSSR PLRCGVPDLP DVLNARNRQK 100
    RFVLSGGRWE KTDLTYRILR FPWQLVREQV RQTVAEALQV WSEVTPLTFT 150
    EVHEGRADIM IDFARYWHGD NLPFDGPGGI LAHAFFPKTH REGDVHFDYD 200
    ETWTIGDNQG TDLLQVAAHE FGHVLGLQHT TAAKALMSPF YTFRYPLSLS 250
    PDDRRGIQHL YGRPQMAPTS PAPTLSSQAG TDTNEIALLE PETPPDVCET 300
    SFDAVSTIRG ELFFFKAGFV WRLRSGRLQP GYPALASRHW QGLPSPVDAA 350
    FEDAQGQIWF FQGAQYWVYD GEKPVLGPAP LSKLGLQGSP VHAALVWGPE 400
    KNKIYFFRGG DYWRFHPRTQ RVDNPVPRRS TDWRGVPSEI DAAFQDAEGY 450
    AYFLRGHLYW KFDPVKVKVL EGFPRPVGPD FFDCAEPANT FR 492
    Length:492
    Mass (Da):55,441
    Last modified:February 1, 1996 - v2
    Checksum:iB54E260E4AB3D7C3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z12604 mRNA. Translation: CAA78248.1.
    CCDSiCCDS23937.1.
    PIRiA44399.
    RefSeqiNP_032632.1. NM_008606.2.
    XP_006513381.1. XM_006513318.1.
    UniGeneiMm.4561.

    Genome annotation databases

    EnsembliENSMUST00000000924; ENSMUSP00000000924; ENSMUSG00000000901.
    ENSMUST00000120281; ENSMUSP00000112940; ENSMUSG00000000901.
    GeneIDi17385.
    KEGGimmu:17385.
    UCSCiuc007fto.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z12604 mRNA. Translation: CAA78248.1 .
    CCDSi CCDS23937.1.
    PIRi A44399.
    RefSeqi NP_032632.1. NM_008606.2.
    XP_006513381.1. XM_006513318.1.
    UniGenei Mm.4561.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HV5 X-ray 2.60 A/B/C/D/E/F 102-265 [» ]
    ProteinModelPortali Q02853.
    SMRi Q02853. Positions 102-463.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi Q02853.
    ChEMBLi CHEMBL3412.

    Protein family/group databases

    MEROPSi M10.007.

    PTM databases

    PhosphoSitei Q02853.

    Proteomic databases

    MaxQBi Q02853.
    PRIDEi Q02853.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000924 ; ENSMUSP00000000924 ; ENSMUSG00000000901 .
    ENSMUST00000120281 ; ENSMUSP00000112940 ; ENSMUSG00000000901 .
    GeneIDi 17385.
    KEGGi mmu:17385.
    UCSCi uc007fto.1. mouse.

    Organism-specific databases

    CTDi 4320.
    MGIi MGI:97008. Mmp11.

    Phylogenomic databases

    eggNOGi NOG236137.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi Q02853.
    KOi K07993.
    OMAi VDTNEIA.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi Q02853.
    TreeFami TF315428.

    Enzyme and pathway databases

    Reactomei REACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199055. Collagen degradation.

    Miscellaneous databases

    EvolutionaryTracei Q02853.
    NextBioi 291992.
    PMAP-CutDB Q02853.
    PROi Q02853.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02853.
    Bgeei Q02853.
    CleanExi MM_MMP11.
    Genevestigatori Q02853.

    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.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR028705. Stromelysin-3.
    [Graphical view ]
    PANTHERi PTHR10201:SF20. PTHR10201:SF20. 1 hit.
    Pfami PF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 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 SSF50923. SSF50923. 1 hit.
    PROSITEi PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The breast cancer-associated stromelysin-3 gene is expressed during mouse mammary gland apoptosis."
      Lefebvre O., Wolf C., Limacher J.-M., Hutin P., Wendling C., Lemeur M., Basset P., Rio M.C.
      J. Cell Biol. 119:997-1002(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Lefebvre O.
      Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Crystal structure of the stromelysin-3 (MMP-11) catalytic domain complexed with a phosphinic inhibitor mimicking the transition-state."
      Gall A.-L., Ruff M., Kannan R., Cuniasse P., Yiotakis A., Dive V., Rio M.-C., Basset P., Moras D.
      J. Mol. Biol. 307:577-586(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 102-265.

    Entry informationi

    Entry nameiMMP11_MOUSE
    AccessioniPrimary (citable) accession number: Q02853
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 140 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3