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P57748 (MMP20_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Binds 2 Calcium ions per subunit By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Expressed specifically in the enamel organ.

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 106-Asn-|-Tyr-107 site By similarity.

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 – 2121 Potential
Propeptide22 – 10685 By similarity
PRO_0000028835
Chain107 – 482376Matrix metalloproteinase-20
PRO_0000028836

Regions

Repeat292 – 34251Hemopexin 1
Repeat343 – 38846Hemopexin 2
Repeat390 – 43849Hemopexin 3
Repeat439 – 48244Hemopexin 4
Motif97 – 1048Cysteine switch By similarity

Sites

Active site2261 By similarity
Metal binding991Zinc 1; in inhibited form By similarity
Metal binding1631Calcium 1 By similarity
Metal binding1641Calcium 1; via carbonyl oxygen By similarity
Metal binding1651Calcium 1; via carbonyl oxygen By similarity
Metal binding1751Zinc 2 By similarity
Metal binding1771Zinc 2 By similarity
Metal binding1821Calcium 2 By similarity
Metal binding1831Calcium 2; via carbonyl oxygen By similarity
Metal binding1851Calcium 2; via carbonyl oxygen By similarity
Metal binding1871Calcium 2; via carbonyl oxygen By similarity
Metal binding1901Zinc 2 By similarity
Metal binding1961Calcium 1; via carbonyl oxygen By similarity
Metal binding1971Calcium 1; via carbonyl oxygen By similarity
Metal binding1991Calcium 1; via carbonyl oxygen By similarity
Metal binding2011Calcium 1 By similarity
Metal binding2031Zinc 2 By similarity
Metal binding2051Calcium 2 By similarity
Metal binding2081Calcium 2 By similarity
Metal binding2251Zinc 1; catalytic By similarity
Metal binding2291Zinc 1; catalytic By similarity
Metal binding2351Zinc 1; catalytic By similarity

Amino acid modifications

Disulfide bond295 ↔ 482 By similarity

Sequences

Sequence LengthMass (Da)Tools
P57748 [UniParc].

Last modified January 24, 2001. Version 1.
Checksum: 366149FAF2BDC8BB

FASTA48254,373
        10         20         30         40         50         60 
MKVLPASGLA VLVTALKFAT ADPNLLAATP RTFRSNYHLA QAYLDKYYTK KGGPQAGEMV 

        70         80         90        100        110        120 
ARESNPMIRR IKELQIFFGL KVTGKLDQNT MNVIKKPRCG VPDVANYRLF PGEPKWKKNI 

       130        140        150        160        170        180 
LTYRISKYTP SMSPTEVDKA IQMALHAWST AVPLNFVRIN SGEADIMISF ETGDHGDSYP 

       190        200        210        220        230        240 
FDGPRGTLAH AFAPGEGLGG DTHFDNAEKW TMGTNGFNLF TVAAHEFGHA LGLGHSTDPS 

       250        260        270        280        290        300 
ALMYPTYKYQ NPYRFHLPKD DVKGIQALYG PRKIFPGKPT MPHIPPHKPS IPDLCDSSSS 

       310        320        330        340        350        360 
FDAVTMLGKE LLFFKDRIFW RRQVHLPTGI RPSTITSSFP QLMSNVDAAY EVAERGIAFF 

       370        380        390        400        410        420 
FKGPHYWVTR GFHMQGPPRT IYDFGFPRHV QRIDAAVYLK EPQKTLFFVG EEYYSYDERK 

       430        440        450        460        470        480 
KKMEKDYPKN TEEEFSGVSG HIDAAVELNG YIYFFSGRKT FKYDTEKEDV VSVVKSSSWI 


GC 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, characterization, and chromosomal location of the mouse enamelysin gene."
Caterina J., Shi J., Krakora S., Bartlett J.D., Engler J.A., Kozak C.A., Birkedal-Hansen H.
Genomics 62:308-311(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/SvJ.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF156956 expand/collapse EMBL AC list , AF156947, AF156948, AF156949, AF156950, AF156951, AF156952, AF156953, AF156954, AF156955 Genomic DNA. Translation: AAF28472.1.
AF155933 mRNA. Translation: AAF28470.1.
BC152335 mRNA. Translation: AAI52336.1.
BC152336 mRNA. Translation: AAI52337.1.
CCDSCCDS22809.1.
RefSeqNP_038931.1. NM_013903.2.
UniGeneMm.390121.

3D structure databases

ProteinModelPortalP57748.
SMRP57748. Positions 39-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000034487.

Protein family/group databases

MEROPSM10.019.

PTM databases

PhosphoSiteP57748.

Proteomic databases

PRIDEP57748.

Protocols and materials databases

DNASU30800.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034487; ENSMUSP00000034487; ENSMUSG00000018620.
GeneID30800.
KEGGmmu:30800.
UCSCuc009ocu.1. mouse.

Organism-specific databases

CTD9313.
MGIMGI:1353466. Mmp20.

Phylogenomic databases

eggNOGNOG328389.
GeneTreeENSGT00750000117336.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidA7MCV5.
KOK07999.
OMAPDVANYR.
OrthoDBEOG7XPZ57.
PhylomeDBP57748.
TreeFamTF315428.

Enzyme and pathway databases

ReactomeREACT_206066. Extracellular matrix organization.

Gene expression databases

BgeeP57748.
CleanExMM_MMP20.
GenevestigatorP57748.

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. 4 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

NextBio307218.
PROP57748.
SOURCESearch...

Entry information

Entry nameMMP20_MOUSE
AccessionPrimary (citable) accession number: P57748
Secondary accession number(s): A7MCV5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot