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Protein

Matrix metalloproteinase-20

Gene

MMP20

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi100Zinc 1; in inhibited formBy similarity1
Metal bindingi164Calcium 11
Metal bindingi165Calcium 1; via carbonyl oxygen1
Metal bindingi166Calcium 1; via carbonyl oxygen1
Metal bindingi176Zinc 21
Metal bindingi178Zinc 21
Metal bindingi183Calcium 21
Metal bindingi184Calcium 2; via carbonyl oxygen1
Metal bindingi186Calcium 2; via carbonyl oxygen1
Metal bindingi188Calcium 2; via carbonyl oxygen1
Metal bindingi191Zinc 21
Metal bindingi197Calcium 1; via carbonyl oxygen1
Metal bindingi198Calcium 1; via carbonyl oxygen1
Metal bindingi200Calcium 1; via carbonyl oxygen1
Metal bindingi202Calcium 11
Metal bindingi204Zinc 21
Metal bindingi206Calcium 21
Metal bindingi209Calcium 21
Metal bindingi226Zinc 1; catalytic1
Active sitei227PROSITE-ProRule annotation1
Metal bindingi230Zinc 1; catalytic1
Metal bindingi236Zinc 1; catalytic1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • metalloendopeptidase activity Source: CACAO
  • serine-type endopeptidase activity Source: Reactome
  • zinc ion binding Source: ProtInc

GO - Biological processi

  • amelogenesis Source: Ensembl
  • collagen catabolic process Source: Reactome
  • extracellular matrix disassembly Source: Ensembl
  • protein catabolic process Source: Ensembl
  • proteolysis Source: ProtInc
  • 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

BioCyciZFISH:ENSG00000137674-MONOMER.
BRENDAi3.4.24.B6. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7167. MMP20.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
  • 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)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:612529

Keywords - Diseasei

Amelogenesis imperfecta

Organism-specific databases

DisGeNETi9313.
MalaCardsiMMP20.
MIMi612529. phenotype.
OpenTargetsiENSG00000137674.
Orphaneti100033. Hypomaturation amelogenesis imperfecta.
PharmGKBiPA30878.

Chemistry databases

ChEMBLiCHEMBL1938226.
DrugBankiDB00786. Marimastat.

Polymorphism and mutation databases

BioMutaiMMP20.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000002883323 – 107By similarityAdd BLAST85
ChainiPRO_0000028834108 – 483Matrix metalloproteinase-20Add BLAST376

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

iPTMnetiO60882.
PhosphoSitePlusiO60882.

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

BgeeiENSG00000137674.
CleanExiHS_MMP20.
GenevisibleiO60882. HS.

Organism-specific databases

HPAiCAB011500.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000260228.

Chemistry databases

BindingDBiO60882.

Structurei

Secondary structure

1483
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi120 – 126Combined sources7
Beta strandi131 – 133Combined sources3
Helixi135 – 152Combined sources18
Beta strandi156 – 159Combined sources4
Beta strandi161 – 163Combined sources3
Beta strandi166 – 172Combined sources7
Beta strandi176 – 180Combined sources5
Beta strandi184 – 187Combined sources4
Beta strandi189 – 192Combined sources4
Beta strandi195 – 199Combined sources5
Beta strandi203 – 206Combined sources4
Beta strandi211 – 219Combined sources9
Helixi220 – 232Combined sources13
Turni253 – 255Combined sources3
Helixi261 – 270Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JSDNMR-A113-272[»]
ProteinModelPortaliO60882.
SMRiO60882.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60882.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati293 – 343Hemopexin 1Add BLAST51
Repeati344 – 389Hemopexin 2Add BLAST46
Repeati391 – 439Hemopexin 3Add BLAST49
Repeati440 – 483Hemopexin 4Add BLAST44

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi98 – 105Cysteine switchBy similarity8

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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiO60882.
KOiK07999.
OMAiYSYDERK.
OrthoDBiEOG091G03DP.
PhylomeDBiO60882.
TreeFamiTF315428.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR033739. M10A_MMP.
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

        10         20         30         40         50
MKVLPASGLA VFLIMALKFS TAAPSLVAAS PRTWRNNYRL AQAYLDKYYT
60 70 80 90 100
NKEGHQIGEM VARGSNSMIR KIKELQAFFG LQVTGKLDQT TMNVIKKPRC
110 120 130 140 150
GVPDVANYRL FPGEPKWKKN TLTYRISKYT PSMSSVEVDK AVEMALQAWS
160 170 180 190 200
SAVPLSFVRI NSGEADIMIS FENGDHGDSY PFDGPRGTLA HAFAPGEGLG
210 220 230 240 250
GDTHFDNAEK WTMGTNGFNL FTVAAHEFGH ALGLAHSTDP SALMYPTYKY
260 270 280 290 300
KNPYGFHLPK DDVKGIQALY GPRKVFLGKP TLPHAPHHKP SIPDLCDSSS
310 320 330 340 350
SFDAVTMLGK ELLLFKDRIF WRRQVHLRTG IRPSTITSSF PQLMSNVDAA
360 370 380 390 400
YEVAERGTAY FFKGPHYWIT RGFQMQGPPR TIYDFGFPRH VQQIDAAVYL
410 420 430 440 450
REPQKTLFFV GDEYYSYDER KRKMEKDYPK NTEEEFSGVN GQIDAAVELN
460 470 480
GYIYFFSGPK TYKYDTEKED VVSVVKSSSW IGC
Length:483
Mass (Da):54,387
Last modified:February 8, 2011 - v3
Checksum:i561B0A03E0BB0399
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti208A → P in CAA73317 (PubMed:9398237).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02051118K → T.1 PublicationCorresponds to variant rs2245803dbSNPEnsembl.1
Natural variantiVAR_020512139D → N.1 PublicationCorresponds to variant rs17099014dbSNPEnsembl.1
Natural variantiVAR_020513169I → L.1 PublicationCorresponds to variant rs17099008dbSNPEnsembl.1
Natural variantiVAR_020514275V → A.1 PublicationCorresponds to variant rs1784423dbSNPEnsembl.1
Natural variantiVAR_057802281T → N.1 PublicationCorresponds to variant rs1784424dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JSDNMR-A113-272[»]
ProteinModelPortaliO60882.
SMRiO60882.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000260228.

Chemistry databases

BindingDBiO60882.
ChEMBLiCHEMBL1938226.
DrugBankiDB00786. Marimastat.

Protein family/group databases

MEROPSiM10.019.

PTM databases

iPTMnetiO60882.
PhosphoSitePlusiO60882.

Polymorphism and mutation databases

BioMutaiMMP20.

Proteomic databases

PaxDbiO60882.
PRIDEiO60882.

Protocols and materials databases

DNASUi9313.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9313.
DisGeNETi9313.
GeneCardsiMMP20.
H-InvDBHIX0036038.
HGNCiHGNC:7167. MMP20.
HPAiCAB011500.
MalaCardsiMMP20.
MIMi604629. gene.
612529. phenotype.
neXtProtiNX_O60882.
OpenTargetsiENSG00000137674.
Orphaneti100033. Hypomaturation amelogenesis imperfecta.
PharmGKBiPA30878.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiO60882.
KOiK07999.
OMAiYSYDERK.
OrthoDBiEOG091G03DP.
PhylomeDBiO60882.
TreeFamiTF315428.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137674-MONOMER.
BRENDAi3.4.24.B6. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.

Miscellaneous databases

EvolutionaryTraceiO60882.
GeneWikiiMMP20.
GenomeRNAii9313.
PROiO60882.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137674.
CleanExiHS_MMP20.
GenevisibleiO60882. HS.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR033739. M10A_MMP.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 158 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.