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O60882

- MMP20_HUMAN

UniProt

O60882 - MMP20_HUMAN

Protein

Matrix metalloproteinase-20

Gene

MMP20

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (08 Feb 2011)
      Previous versions | rss
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    Functioni

    Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation.2 Publications

    Catalytic activityi

    Cleaves aggrecan at the 360-Asn-|-Phe-361 site.

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi100 – 1001Zinc 1; in inhibited formBy similarity
    Metal bindingi164 – 1641Calcium 1
    Metal bindingi165 – 1651Calcium 1; via carbonyl oxygen
    Metal bindingi166 – 1661Calcium 1; via carbonyl oxygen
    Metal bindingi176 – 1761Zinc 2
    Metal bindingi178 – 1781Zinc 2
    Metal bindingi183 – 1831Calcium 2
    Metal bindingi184 – 1841Calcium 2; via carbonyl oxygen
    Metal bindingi186 – 1861Calcium 2; via carbonyl oxygen
    Metal bindingi188 – 1881Calcium 2; via carbonyl oxygen
    Metal bindingi191 – 1911Zinc 2
    Metal bindingi197 – 1971Calcium 1; via carbonyl oxygen
    Metal bindingi198 – 1981Calcium 1; via carbonyl oxygen
    Metal bindingi200 – 2001Calcium 1; via carbonyl oxygen
    Metal bindingi202 – 2021Calcium 1
    Metal bindingi204 – 2041Zinc 2
    Metal bindingi206 – 2061Calcium 2
    Metal bindingi209 – 2091Calcium 2
    Metal bindingi226 – 2261Zinc 1; catalytic
    Active sitei227 – 2271PROSITE-ProRule annotation
    Metal bindingi230 – 2301Zinc 1; catalytic
    Metal bindingi236 – 2361Zinc 1; catalytic

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: ProtInc
    3. protein binding Source: BHF-UCL
    4. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. amelogenesis Source: Ensembl
    2. collagen catabolic process Source: Reactome
    3. extracellular matrix disassembly Source: Reactome
    4. extracellular matrix organization Source: Reactome
    5. proteolysis Source: ProtInc
    6. regulation of enamel mineralization Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.019.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-20 (EC:3.4.24.-)
    Short name:
    MMP-20
    Alternative name(s):
    Enamel metalloproteinase
    Enamelysin
    Gene namesi
    Name:MMP20
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:7167. MMP20.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: ProtInc
    3. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Amelogenesis imperfecta, hypomaturation type, 2A2 (AI2A2) [MIM:612529]: A defect of enamel formation. The disorder involves both primary and secondary dentitions. The teeth have a shiny agar jelly appearance and the enamel is softer than normal. Brown pigment is present in middle layers of enamel.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Amelogenesis imperfecta

    Organism-specific databases

    MIMi612529. phenotype.
    Orphaneti100033. Hypomaturation amelogenesis imperfecta.
    PharmGKBiPA30878.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 10785By similarityPRO_0000028833Add
    BLAST
    Chaini108 – 483376Matrix metalloproteinase-20PRO_0000028834Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi296 ↔ 483Sequence Analysis

    Post-translational modificationi

    Autoactivates at least at the 107-Asn-|-Tyr-108 site.By similarity

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiO60882.
    PRIDEiO60882.

    PTM databases

    PhosphoSiteiO60882.

    Expressioni

    Tissue specificityi

    Expressed specifically in the enamel organ.

    Developmental stagei

    Expression initiates prior to the onset of dentin mineralization and continues throughout the secretory stage of amelogenesis.

    Gene expression databases

    BgeeiO60882.
    CleanExiHS_MMP20.
    GenevestigatoriO60882.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000260228.

    Structurei

    Secondary structure

    1
    483
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi120 – 1267
    Beta strandi131 – 1333
    Helixi135 – 15218
    Beta strandi156 – 1594
    Beta strandi161 – 1633
    Beta strandi166 – 1727
    Beta strandi176 – 1805
    Beta strandi184 – 1874
    Beta strandi189 – 1924
    Beta strandi195 – 1995
    Beta strandi203 – 2064
    Beta strandi211 – 2199
    Helixi220 – 23213
    Turni253 – 2553
    Helixi261 – 27010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JSDNMR-A113-272[»]
    ProteinModelPortaliO60882.
    SMRiO60882. Positions 40-483.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60882.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati293 – 34351Hemopexin 1Add
    BLAST
    Repeati344 – 38946Hemopexin 2Add
    BLAST
    Repeati391 – 43949Hemopexin 3Add
    BLAST
    Repeati440 – 48344Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi98 – 1058Cysteine 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

    eggNOGiNOG328389.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiO60882.
    KOiK07999.
    OMAiPDVANYR.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiO60882.
    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.
    IPR024079. MetalloPept_cat_dom.
    IPR028716. MMP20.
    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:SF125. PTHR10201:SF125. 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.
    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.

    O60882-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVLPASGLA VFLIMALKFS TAAPSLVAAS PRTWRNNYRL AQAYLDKYYT    50
    NKEGHQIGEM VARGSNSMIR KIKELQAFFG LQVTGKLDQT TMNVIKKPRC 100
    GVPDVANYRL FPGEPKWKKN TLTYRISKYT PSMSSVEVDK AVEMALQAWS 150
    SAVPLSFVRI NSGEADIMIS FENGDHGDSY PFDGPRGTLA HAFAPGEGLG 200
    GDTHFDNAEK WTMGTNGFNL FTVAAHEFGH ALGLAHSTDP SALMYPTYKY 250
    KNPYGFHLPK DDVKGIQALY GPRKVFLGKP TLPHAPHHKP SIPDLCDSSS 300
    SFDAVTMLGK ELLLFKDRIF WRRQVHLRTG IRPSTITSSF PQLMSNVDAA 350
    YEVAERGTAY FFKGPHYWIT RGFQMQGPPR TIYDFGFPRH VQQIDAAVYL 400
    REPQKTLFFV GDEYYSYDER KRKMEKDYPK NTEEEFSGVN GQIDAAVELN 450
    GYIYFFSGPK TYKYDTEKED VVSVVKSSSW IGC 483
    Length:483
    Mass (Da):54,387
    Last modified:February 8, 2011 - v3
    Checksum:i561B0A03E0BB0399
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti208 – 2081A → P in CAA73317. (PubMed:9398237)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181K → T.1 Publication
    Corresponds to variant rs2245803 [ dbSNP | Ensembl ].
    VAR_020511
    Natural varianti139 – 1391D → N.1 Publication
    Corresponds to variant rs17099014 [ dbSNP | Ensembl ].
    VAR_020512
    Natural varianti169 – 1691I → L.1 Publication
    Corresponds to variant rs17099008 [ dbSNP | Ensembl ].
    VAR_020513
    Natural varianti275 – 2751V → A.1 Publication
    Corresponds to variant rs1784423 [ dbSNP | Ensembl ].
    VAR_020514
    Natural varianti281 – 2811T → N.1 Publication
    Corresponds to variant rs1784424 [ dbSNP | Ensembl ].
    VAR_057802

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12779 mRNA. Translation: CAA73317.1.
    AY673603 Genomic DNA. Translation: AAT70722.1.
    AP000851 Genomic DNA. No translation available.
    CCDSiCCDS8318.1.
    RefSeqiNP_004762.2. NM_004771.3.
    UniGeneiHs.591946.

    Genome annotation databases

    EnsembliENST00000260228; ENSP00000260228; ENSG00000137674.
    GeneIDi9313.
    KEGGihsa:9313.
    UCSCiuc001phc.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12779 mRNA. Translation: CAA73317.1 .
    AY673603 Genomic DNA. Translation: AAT70722.1 .
    AP000851 Genomic DNA. No translation available.
    CCDSi CCDS8318.1.
    RefSeqi NP_004762.2. NM_004771.3.
    UniGenei Hs.591946.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JSD NMR - A 113-272 [» ]
    ProteinModelPortali O60882.
    SMRi O60882. Positions 40-483.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000260228.

    Chemistry

    BindingDBi O60882.
    ChEMBLi CHEMBL1938226.

    Protein family/group databases

    MEROPSi M10.019.

    PTM databases

    PhosphoSitei O60882.

    Proteomic databases

    PaxDbi O60882.
    PRIDEi O60882.

    Protocols and materials databases

    DNASUi 9313.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260228 ; ENSP00000260228 ; ENSG00000137674 .
    GeneIDi 9313.
    KEGGi hsa:9313.
    UCSCi uc001phc.3. human.

    Organism-specific databases

    CTDi 9313.
    GeneCardsi GC11M102481.
    H-InvDB HIX0036038.
    HGNCi HGNC:7167. MMP20.
    MIMi 604629. gene.
    612529. phenotype.
    neXtProti NX_O60882.
    Orphaneti 100033. Hypomaturation amelogenesis imperfecta.
    PharmGKBi PA30878.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG328389.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi O60882.
    KOi K07999.
    OMAi PDVANYR.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi O60882.
    TreeFami TF315428.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.

    Miscellaneous databases

    EvolutionaryTracei O60882.
    GeneWikii MMP20.
    GenomeRNAii 9313.
    NextBioi 34887.
    PROi O60882.
    SOURCEi Search...

    Gene expression databases

    Bgeei O60882.
    CleanExi HS_MMP20.
    Genevestigatori O60882.

    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.
    IPR024079. MetalloPept_cat_dom.
    IPR028716. MMP20.
    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:SF125. PTHR10201:SF125. 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.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and structural and functional characterization of human enamelysin (MMP-20)."
      Llano E., Pendas A.M., Knaeuper V., Sorsa T., Salo T., Salido E., Murphy G., Simmer J.P., Bartlett J.D., Lopez-Otin C.
      Biochemistry 36:15101-15108(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Odontoblast.
    2. NIEHS SNPs program
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-18; ASN-139; LEU-169; ALA-275 AND ASN-281.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)."
      Stracke J.O., Fosang A.J., Last K., Mercuri F.A., Pendas A.M., Llano E., Perris R., Di Cesare P.E., Murphy G., Knaeuper V.
      FEBS Lett. 478:52-56(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "MMP-20 mutation in autosomal recessive pigmented hypomaturation amelogenesis imperfecta."
      Kim J.-W., Simmer J.P., Hart T.C., Hart P.S., Ramaswami M.D., Bartlett J.D., Hu J.C.-C.
      J. Med. Genet. 42:271-275(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN AI2A2.
    6. "Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase."
      Arendt Y., Banci L., Bertini I., Cantini F., Cozzi R., Del Conte R., Gonnelli L.
      FEBS Lett. 581:4723-4726(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 113-272 IN COMPLEX WITH INHIBITOR, COFACTOR, ZINC-BINDING SITES, CALCIUM-BINDING SITES.

    Entry informationi

    Entry nameiMMP20_HUMAN
    AccessioniPrimary (citable) accession number: O60882
    Secondary accession number(s): Q6DKT9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 142 of the entry and version 3 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, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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