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O60882 (MMP20_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-20

Short name=MMP-20
EC=3.4.24.-
Alternative name(s):
Enamel metalloproteinase
Enamelysin
Gene names
Name:MMP20
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit. Ref.6

Binds 2 calcium ions per subunit. Ref.6

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Expressed specifically in the enamel organ.

Developmental stage

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

Domain

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.

Post-translational modification

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

Involvement in disease

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. Ref.5

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 10785 By similarity
PRO_0000028833
Chain108 – 483376Matrix metalloproteinase-20
PRO_0000028834

Regions

Repeat293 – 34351Hemopexin 1
Repeat344 – 38946Hemopexin 2
Repeat391 – 43949Hemopexin 3
Repeat440 – 48344Hemopexin 4
Motif98 – 1058Cysteine switch By similarity

Sites

Active site2271 By similarity
Metal binding1001Zinc 1; in inhibited form By similarity
Metal binding1641Calcium 1
Metal binding1651Calcium 1; via carbonyl oxygen
Metal binding1661Calcium 1; via carbonyl oxygen
Metal binding1761Zinc 2
Metal binding1781Zinc 2
Metal binding1831Calcium 2
Metal binding1841Calcium 2; via carbonyl oxygen
Metal binding1861Calcium 2; via carbonyl oxygen
Metal binding1881Calcium 2; via carbonyl oxygen
Metal binding1911Zinc 2
Metal binding1971Calcium 1; via carbonyl oxygen
Metal binding1981Calcium 1; via carbonyl oxygen
Metal binding2001Calcium 1; via carbonyl oxygen
Metal binding2021Calcium 1
Metal binding2041Zinc 2
Metal binding2061Calcium 2
Metal binding2091Calcium 2
Metal binding2261Zinc 1; catalytic
Metal binding2301Zinc 1; catalytic
Metal binding2361Zinc 1; catalytic

Amino acid modifications

Disulfide bond296 ↔ 483 Potential

Natural variations

Natural variant181K → T. Ref.2
Corresponds to variant rs2245803 [ dbSNP | Ensembl ].
VAR_020511
Natural variant1391D → N. Ref.2
Corresponds to variant rs17099014 [ dbSNP | Ensembl ].
VAR_020512
Natural variant1691I → L. Ref.2
Corresponds to variant rs17099008 [ dbSNP | Ensembl ].
VAR_020513
Natural variant2751V → A. Ref.2
Corresponds to variant rs1784423 [ dbSNP | Ensembl ].
VAR_020514
Natural variant2811T → N. Ref.2
Corresponds to variant rs1784424 [ dbSNP | Ensembl ].
VAR_057802

Experimental info

Sequence conflict2081A → P in CAA73317. Ref.1

Secondary structure

.............................. 483
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O60882 [UniParc].

Last modified February 8, 2011. Version 3.
Checksum: 561B0A03E0BB0399

FASTA48354,387
        10         20         30         40         50         60 
MKVLPASGLA VFLIMALKFS TAAPSLVAAS PRTWRNNYRL AQAYLDKYYT NKEGHQIGEM 

        70         80         90        100        110        120 
VARGSNSMIR KIKELQAFFG LQVTGKLDQT TMNVIKKPRC GVPDVANYRL FPGEPKWKKN 

       130        140        150        160        170        180 
TLTYRISKYT PSMSSVEVDK AVEMALQAWS SAVPLSFVRI NSGEADIMIS FENGDHGDSY 

       190        200        210        220        230        240 
PFDGPRGTLA HAFAPGEGLG GDTHFDNAEK WTMGTNGFNL FTVAAHEFGH ALGLAHSTDP 

       250        260        270        280        290        300 
SALMYPTYKY KNPYGFHLPK DDVKGIQALY GPRKVFLGKP TLPHAPHHKP SIPDLCDSSS 

       310        320        330        340        350        360 
SFDAVTMLGK ELLLFKDRIF WRRQVHLRTG IRPSTITSSF PQLMSNVDAA YEVAERGTAY 

       370        380        390        400        410        420 
FFKGPHYWIT RGFQMQGPPR TIYDFGFPRH VQQIDAAVYL REPQKTLFFV GDEYYSYDER 

       430        440        450        460        470        480 
KRKMEKDYPK NTEEEFSGVN GQIDAAVELN GYIYFFSGPK TYKYDTEKED VVSVVKSSSW 


IGC 

« Hide

References

« Hide 'large scale' references
[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]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y12779 mRNA. Translation: CAA73317.1.
AY673603 Genomic DNA. Translation: AAT70722.1.
AP000851 Genomic DNA. No translation available.
CCDSCCDS8318.1.
RefSeqNP_004762.2. NM_004771.3.
UniGeneHs.591946.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JSDNMR-A113-272[»]
ProteinModelPortalO60882.
SMRO60882. Positions 40-483.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000260228.

Chemistry

BindingDBO60882.
ChEMBLCHEMBL1938226.

Protein family/group databases

MEROPSM10.019.

PTM databases

PhosphoSiteO60882.

Proteomic databases

PaxDbO60882.
PRIDEO60882.

Protocols and materials databases

DNASU9313.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260228; ENSP00000260228; ENSG00000137674.
GeneID9313.
KEGGhsa:9313.
UCSCuc001phc.3. human.

Organism-specific databases

CTD9313.
GeneCardsGC11M102481.
H-InvDBHIX0036038.
HGNCHGNC:7167. MMP20.
MIM604629. gene.
612529. phenotype.
neXtProtNX_O60882.
Orphanet100033. Hypomaturation amelogenesis imperfecta.
PharmGKBPA30878.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG328389.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidO60882.
KOK07999.
OMAPDVANYR.
OrthoDBEOG7XPZ57.
PhylomeDBO60882.
TreeFamTF315428.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

BgeeO60882.
CleanExHS_MMP20.
GenevestigatorO60882.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. 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]
PANTHERPTHR10201:SF125. PTHR10201:SF125. 1 hit.
PfamPF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO60882.
GeneWikiMMP20.
GenomeRNAi9313.
NextBio34887.
PROO60882.
SOURCESearch...

Entry information

Entry nameMMP20_HUMAN
AccessionPrimary (citable) accession number: O60882
Secondary accession number(s): Q6DKT9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 8, 2011
Last modified: July 9, 2014
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM