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Protein

Matrix metalloproteinase-20

Gene

MMP20

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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. Cleaves aggrecan at the '360-Asn-|-Phe-361' site.2 Publications

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

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

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000137674.3
HGNCiHGNC:7167 MMP20
MIMi604629 gene
neXtProtiNX_O60882

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
DB08271 N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID

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
PeptideAtlasiO60882
PRIDEiO60882
ProteomicsDBi49648

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 Expressed in 34 organ(s), highest expression level in testis
CleanExiHS_MMP20
GenevisibleiO60882 HS

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

3D structure databases

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

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

Family and domain databases

CDDicd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.110.10.10, 1 hit
3.40.390.10, 2 hits
InterProiView protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028716 MMP20
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
IPR036366 PGBDSf
PANTHERiPTHR10201:SF125 PTHR10201:SF125, 1 hit
PfamiView protein in Pfam
PF00045 Hemopexin, 3 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
PROSITEiView protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

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 → T1 PublicationCorresponds to variant dbSNP:rs2245803EnsemblClinVar.1
Natural variantiVAR_020512139D → N1 PublicationCorresponds to variant dbSNP:rs17099014EnsemblClinVar.1
Natural variantiVAR_020513169I → L1 PublicationCorresponds to variant dbSNP:rs17099008EnsemblClinVar.1
Natural variantiVAR_020514275V → A1 PublicationCorresponds to variant dbSNP:rs1784423EnsemblClinVar.1
Natural variantiVAR_057802281T → N1 PublicationCorresponds to variant dbSNP:rs1784424EnsemblClinVar.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

Similar proteinsi

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
DB08271 N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID

Protein family/group databases

MEROPSiM10.019

PTM databases

iPTMnetiO60882
PhosphoSitePlusiO60882

Polymorphism and mutation databases

BioMutaiMMP20

Proteomic databases

PaxDbiO60882
PeptideAtlasiO60882
PRIDEiO60882
ProteomicsDBi49648

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
EuPathDBiHostDB:ENSG00000137674.3
GeneCardsiMMP20
H-InvDBiHIX0036038
HGNCiHGNC:7167 MMP20
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
OMAiGDTHFDN
OrthoDBiEOG091G03DP
PhylomeDBiO60882
TreeFamiTF315428

Enzyme and pathway databases

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
PROiPR:O60882
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137674 Expressed in 34 organ(s), highest expression level in testis
CleanExiHS_MMP20
GenevisibleiO60882 HS

Family and domain databases

CDDicd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.110.10.10, 1 hit
3.40.390.10, 2 hits
InterProiView protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028716 MMP20
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
IPR036366 PGBDSf
PANTHERiPTHR10201:SF125 PTHR10201:SF125, 1 hit
PfamiView protein in Pfam
PF00045 Hemopexin, 3 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
PROSITEiView protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMMP20_HUMAN
AccessioniPrimary (citable) accession number: O60882
Secondary accession number(s): Q6DKT9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 8, 2011
Last modified: September 12, 2018
This is version 169 of the entry and version 3 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
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