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Protein

Matrix metalloproteinase-20

Gene

MMP20

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity
  • Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi98 – 981Zinc 1; in inhibited formBy similarity
Metal bindingi162 – 1621Calcium 1By similarity
Metal bindingi163 – 1631Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi164 – 1641Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi174 – 1741Zinc 2By similarity
Metal bindingi176 – 1761Zinc 2By similarity
Metal bindingi181 – 1811Calcium 2By similarity
Metal bindingi182 – 1821Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi184 – 1841Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi186 – 1861Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi189 – 1891Zinc 2By similarity
Metal bindingi195 – 1951Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi196 – 1961Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi198 – 1981Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi200 – 2001Calcium 1By similarity
Metal bindingi202 – 2021Zinc 2By similarity
Metal bindingi204 – 2041Calcium 2By similarity
Metal bindingi207 – 2071Calcium 2By similarity
Metal bindingi224 – 2241Zinc 1; catalyticBy similarity
Active sitei225 – 2251PROSITE-ProRule annotation
Metal bindingi228 – 2281Zinc 1; catalyticBy similarity
Metal bindingi234 – 2341Zinc 1; catalyticBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.B6. 908.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 10585By similarityPRO_0000028831Add
BLAST
Chaini106 – 481376Matrix metalloproteinase-20PRO_0000028832Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence analysis
Disulfide bondi294 ↔ 481By similarity
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Autoactivates at least at the 105-Asn-|-Tyr-106 site.By similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiO18767.
PRIDEiO18767.

Expressioni

Tissue specificityi

Expressed in the enamel organ.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000018936.

Structurei

3D structure databases

ProteinModelPortaliO18767.
SMRiO18767. Positions 111-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati291 – 34151Hemopexin 1Add
BLAST
Repeati342 – 38746Hemopexin 2Add
BLAST
Repeati389 – 43749Hemopexin 3Add
BLAST
Repeati438 – 48144Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi96 – 1038Cysteine switchBy 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.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiO18767.
KOiK07999.

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.

O18767-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPASGLAVL LVTALKFSTA APSLPAASPR TSRNNYRLAQ AYLDKYYTKK
60 70 80 90 100
GGPQIGEMVA RGGNSTVKKI KELQEFFGLR VTGKLDRATM DVIKRPRCGV
110 120 130 140 150
PDVANYRLFP GEPKWKKNTL TYRISKYTPS MTPAEVDRAM EMALRAWSSA
160 170 180 190 200
VPLNFVRINA GEADIMISFE TGDHGDSYPF DGPRGTLAHA FAPGEGLGGD
210 220 230 240 250
THFDNAEKWT MGTNGFNLFT VAAHEFGHAL GLAHSTDPSA LMFPTYKYQN
260 270 280 290 300
PYGFRLPKDD VKGIQALYGP RRAFSGKPTA PHGPPHNPSI PDLCDSNLSF
310 320 330 340 350
DAVTMLGKEL LLFRDRIFWR RQVHLMSGIR PSTITSSFPQ LMSNVDAAYE
360 370 380 390 400
VAERGTAYFF KGPHYWITRG FQMQGPPRTI YDFGFPRYVQ RIDAAVYLKD
410 420 430 440 450
AQKTLFFVGD EYYSYDERKR KMEKDYPKST EEEFSGVNGQ IDAAVELNGY
460 470 480
IYFFSGPKAY KSDTEKEDVV SELKSSSWIG C
Length:481
Mass (Da):53,781
Last modified:January 1, 1998 - v1
Checksum:i0E72FC5AFE5A719E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151W → K AA sequence (PubMed:9541246).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009922 mRNA. Translation: AAB66599.1.
RefSeqiNP_776816.1. NM_174391.2.
UniGeneiBt.597.

Genome annotation databases

GeneIDi281916.
KEGGibta:281916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009922 mRNA. Translation: AAB66599.1.
RefSeqiNP_776816.1. NM_174391.2.
UniGeneiBt.597.

3D structure databases

ProteinModelPortaliO18767.
SMRiO18767. Positions 111-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000018936.

Protein family/group databases

MEROPSiM10.019.

Proteomic databases

PaxDbiO18767.
PRIDEiO18767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281916.
KEGGibta:281916.

Organism-specific databases

CTDi9313.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiO18767.
KOiK07999.

Enzyme and pathway databases

BRENDAi3.4.24.B6. 908.

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]
ProtoNetiSearch...

Publicationsi

  1. "Purification and sequencing of a 21 kDa and 25 kDa bovine enamel metalloproteinase."
    DenBesten P.K., Punzi J.S., Li W.
    Eur. J. Oral Sci. 106 Suppl. 1:345-349(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS.
    Tissue: Enamel organ.
  2. "Activation of recombinant bovine matrix metalloproteinase-20 and its hydrolysis of two amelogenin oligopeptides."
    Li W., Machule D., Gao C., DenBesten P.K.
    Eur. J. Oral Sci. 107:352-359(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiMMP20_BOVIN
AccessioniPrimary (citable) accession number: O18767
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.