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

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)DescriptionActionsGraphical viewLength
Metal bindingi98Zinc 1; in inhibited formBy similarity1
Metal bindingi162Calcium 1By similarity1
Metal bindingi163Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi164Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi174Zinc 2By similarity1
Metal bindingi176Zinc 2By similarity1
Metal bindingi181Calcium 2By similarity1
Metal bindingi182Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi184Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi186Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi189Zinc 2By similarity1
Metal bindingi195Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi196Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi198Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi200Calcium 1By similarity1
Metal bindingi202Zinc 2By similarity1
Metal bindingi204Calcium 2By similarity1
Metal bindingi207Calcium 2By similarity1
Metal bindingi224Zinc 1; catalyticBy similarity1
Active sitei225PROSITE-ProRule annotation1
Metal bindingi228Zinc 1; catalyticBy similarity1
Metal bindingi234Zinc 1; catalyticBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
LigandCalcium, 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

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000002883121 – 105By similarityAdd BLAST85
ChainiPRO_0000028832106 – 481Matrix metalloproteinase-20Add BLAST376

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi64N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi294 ↔ 481By similarity
Glycosylationi297N-linked (GlcNAc...) asparagineSequence analysis1

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati291 – 341Hemopexin 1Add BLAST51
Repeati342 – 387Hemopexin 2Add BLAST46
Repeati389 – 437Hemopexin 3Add BLAST49
Repeati438 – 481Hemopexin 4Add BLAST44

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi96 – 103Cysteine 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.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiO18767.
KOiK07999.

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.
InterProiView protein in InterPro
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR028716. MMP20.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
PANTHERiPTHR10201:SF176. PTHR10201:SF176. 1 hit.
PfamiView protein in Pfam
PF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti115W → K AA sequence (PubMed:9541246).Curated1

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.

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.

Entry informationi

Entry nameiMMP20_BOVIN
AccessioniPrimary (citable) accession number: O18767
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 1, 1998
Last modified: July 5, 2017
This is version 129 of the entry and version 1 of the sequence. See 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