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O60882

- MMP20_HUMAN

UniProt

O60882 - MMP20_HUMAN

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Protein

Matrix metalloproteinase-20

Gene
MMP20
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 form By 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 – 2271 By similarity
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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

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 – 2222 Reviewed predictionAdd
BLAST
Propeptidei23 – 10785 By similarityPRO_0000028833Add
BLAST
Chaini108 – 483376Matrix metalloproteinase-20PRO_0000028834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi296 ↔ 483 Reviewed prediction

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.

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 switch By 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.
Contains 4 hemopexin repeats.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081A → P in CAA73317. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 141 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

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