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Matrix metalloproteinase-20 (MMP-20) (EC 3.4.24.-) (Enamel metalloproteinase) (Enamelysin)

 MMP20_HUMAN             Reviewed;         483 AA.
O60882; Q6DKT9;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 3.
12-SEP-2018, entry version 169.
RecName: Full=Matrix metalloproteinase-20;
Short=MMP-20;
EC=3.4.24.-;
AltName: Full=Enamel metalloproteinase;
AltName: Full=Enamelysin;
Flags: Precursor;
Name=MMP20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Odontoblast;
PubMed=9398237; DOI=10.1021/bi972120y;
Llano E., Pendas A.M., Knaeuper V., Sorsa T., Salo T., Salido E.,
Murphy G., Simmer J.P., Bartlett J.D., Lopez-Otin C.;
"Identification and structural and functional characterization of
human enamelysin (MMP-20).";
Biochemistry 36:15101-15108(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-18; ASN-139;
LEU-169; ALA-275 AND ASN-281.
NIEHS SNPs program;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
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., 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.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
FUNCTION.
PubMed=10922468; DOI=10.1016/S0014-5793(00)01819-6;
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.;
"Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage
oligomeric matrix protein (COMP).";
FEBS Lett. 478:52-56(2000).
[5]
INVOLVEMENT IN AI2A2.
PubMed=15744043; DOI=10.1136/jmg.2004.024505;
Kim J.-W., Simmer J.P., Hart T.C., Hart P.S., Ramaswami M.D.,
Bartlett J.D., Hu J.C.-C.;
"MMP-20 mutation in autosomal recessive pigmented hypomaturation
amelogenesis imperfecta.";
J. Med. Genet. 42:271-275(2005).
[6]
STRUCTURE BY NMR OF 113-272 IN COMPLEX WITH INHIBITOR, COFACTOR,
ZINC-BINDING SITES, AND CALCIUM-BINDING SITES.
PubMed=17869250; DOI=10.1016/j.febslet.2007.08.069;
Arendt Y., Banci L., Bertini I., Cantini F., Cozzi R., Del Conte R.,
Gonnelli L.;
"Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new
matrix metalloproteinase.";
FEBS Lett. 581:4723-4726(2007).
-!- 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. Cleaves aggrecan at the '360-Asn-|-Phe-361'
site. {ECO:0000269|PubMed:10922468, ECO:0000269|PubMed:9398237}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:17869250};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:17869250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:17869250};
Note=Binds 2 calcium ions per subunit.
{ECO:0000269|PubMed:17869250};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- 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.
-!- PTM: Autoactivates at least at the 107-Asn-|-Tyr-108 site.
{ECO:0000250}.
-!- 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.
{ECO:0000269|PubMed:15744043}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp20/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; Y12779; CAA73317.1; -; mRNA.
EMBL; AY673603; AAT70722.1; -; Genomic_DNA.
EMBL; AP000851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS8318.1; -.
RefSeq; NP_004762.2; NM_004771.3.
UniGene; Hs.591946; -.
PDB; 2JSD; NMR; -; A=113-272.
PDBsum; 2JSD; -.
ProteinModelPortal; O60882; -.
SMR; O60882; -.
STRING; 9606.ENSP00000260228; -.
BindingDB; O60882; -.
ChEMBL; CHEMBL1938226; -.
DrugBank; DB00786; Marimastat.
DrugBank; DB08271; N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID.
MEROPS; M10.019; -.
iPTMnet; O60882; -.
PhosphoSitePlus; O60882; -.
BioMuta; MMP20; -.
PaxDb; O60882; -.
PeptideAtlas; O60882; -.
PRIDE; O60882; -.
ProteomicsDB; 49648; -.
DNASU; 9313; -.
Ensembl; ENST00000260228; ENSP00000260228; ENSG00000137674.
GeneID; 9313; -.
KEGG; hsa:9313; -.
UCSC; uc001phc.3; human.
CTD; 9313; -.
DisGeNET; 9313; -.
EuPathDB; HostDB:ENSG00000137674.3; -.
GeneCards; MMP20; -.
H-InvDB; HIX0036038; -.
HGNC; HGNC:7167; MMP20.
MalaCards; MMP20; -.
MIM; 604629; gene.
MIM; 612529; phenotype.
neXtProt; NX_O60882; -.
OpenTargets; ENSG00000137674; -.
Orphanet; 100033; Hypomaturation amelogenesis imperfecta.
PharmGKB; PA30878; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; O60882; -.
KO; K07999; -.
OMA; GDTHFDN; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; O60882; -.
TreeFam; TF315428; -.
BRENDA; 3.4.24.B6; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
EvolutionaryTrace; O60882; -.
GeneWiki; MMP20; -.
GenomeRNAi; 9313; -.
PRO; PR:O60882; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000137674; Expressed in 34 organ(s), highest expression level in testis.
CleanEx; HS_MMP20; -.
Genevisible; O60882; HS.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:CACAO.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0097186; P:amelogenesis; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0022617; P:extracellular matrix disassembly; IEA:Ensembl.
GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0070173; P:regulation of enamel mineralization; TAS:BHF-UCL.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 1.10.101.10; -; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 2.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028716; MMP20.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
InterPro; IPR036366; PGBDSf.
PANTHER; PTHR10201:SF125; PTHR10201:SF125; 1.
Pfam; PF00045; Hemopexin; 3.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Amelogenesis imperfecta; Autocatalytic cleavage;
Calcium; Complete proteome; Disulfide bond; Extracellular matrix;
Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease;
Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 107 {ECO:0000250}.
/FTId=PRO_0000028833.
CHAIN 108 483 Matrix metalloproteinase-20.
/FTId=PRO_0000028834.
REPEAT 293 343 Hemopexin 1.
REPEAT 344 389 Hemopexin 2.
REPEAT 391 439 Hemopexin 3.
REPEAT 440 483 Hemopexin 4.
MOTIF 98 105 Cysteine switch. {ECO:0000250}.
ACT_SITE 227 227 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 100 100 Zinc 1; in inhibited form. {ECO:0000250}.
METAL 164 164 Calcium 1.
METAL 165 165 Calcium 1; via carbonyl oxygen.
METAL 166 166 Calcium 1; via carbonyl oxygen.
METAL 176 176 Zinc 2.
METAL 178 178 Zinc 2.
METAL 183 183 Calcium 2.
METAL 184 184 Calcium 2; via carbonyl oxygen.
METAL 186 186 Calcium 2; via carbonyl oxygen.
METAL 188 188 Calcium 2; via carbonyl oxygen.
METAL 191 191 Zinc 2.
METAL 197 197 Calcium 1; via carbonyl oxygen.
METAL 198 198 Calcium 1; via carbonyl oxygen.
METAL 200 200 Calcium 1; via carbonyl oxygen.
METAL 202 202 Calcium 1.
METAL 204 204 Zinc 2.
METAL 206 206 Calcium 2.
METAL 209 209 Calcium 2.
METAL 226 226 Zinc 1; catalytic.
METAL 230 230 Zinc 1; catalytic.
METAL 236 236 Zinc 1; catalytic.
DISULFID 296 483 {ECO:0000255}.
VARIANT 18 18 K -> T (in dbSNP:rs2245803).
{ECO:0000269|Ref.2}.
/FTId=VAR_020511.
VARIANT 139 139 D -> N (in dbSNP:rs17099014).
{ECO:0000269|Ref.2}.
/FTId=VAR_020512.
VARIANT 169 169 I -> L (in dbSNP:rs17099008).
{ECO:0000269|Ref.2}.
/FTId=VAR_020513.
VARIANT 275 275 V -> A (in dbSNP:rs1784423).
{ECO:0000269|Ref.2}.
/FTId=VAR_020514.
VARIANT 281 281 T -> N (in dbSNP:rs1784424).
{ECO:0000269|Ref.2}.
/FTId=VAR_057802.
CONFLICT 208 208 A -> P (in Ref. 1; CAA73317).
{ECO:0000305}.
STRAND 120 126 {ECO:0000244|PDB:2JSD}.
STRAND 131 133 {ECO:0000244|PDB:2JSD}.
HELIX 135 152 {ECO:0000244|PDB:2JSD}.
STRAND 156 159 {ECO:0000244|PDB:2JSD}.
STRAND 161 163 {ECO:0000244|PDB:2JSD}.
STRAND 166 172 {ECO:0000244|PDB:2JSD}.
STRAND 176 180 {ECO:0000244|PDB:2JSD}.
STRAND 184 187 {ECO:0000244|PDB:2JSD}.
STRAND 189 192 {ECO:0000244|PDB:2JSD}.
STRAND 195 199 {ECO:0000244|PDB:2JSD}.
STRAND 203 206 {ECO:0000244|PDB:2JSD}.
STRAND 211 219 {ECO:0000244|PDB:2JSD}.
HELIX 220 232 {ECO:0000244|PDB:2JSD}.
TURN 253 255 {ECO:0000244|PDB:2JSD}.
HELIX 261 270 {ECO:0000244|PDB:2JSD}.
SEQUENCE 483 AA; 54387 MW; 561B0A03E0BB0399 CRC64;
MKVLPASGLA VFLIMALKFS TAAPSLVAAS PRTWRNNYRL AQAYLDKYYT NKEGHQIGEM
VARGSNSMIR KIKELQAFFG LQVTGKLDQT TMNVIKKPRC GVPDVANYRL FPGEPKWKKN
TLTYRISKYT PSMSSVEVDK AVEMALQAWS SAVPLSFVRI NSGEADIMIS FENGDHGDSY
PFDGPRGTLA HAFAPGEGLG GDTHFDNAEK WTMGTNGFNL FTVAAHEFGH ALGLAHSTDP
SALMYPTYKY KNPYGFHLPK DDVKGIQALY GPRKVFLGKP TLPHAPHHKP SIPDLCDSSS
SFDAVTMLGK ELLLFKDRIF WRRQVHLRTG IRPSTITSSF PQLMSNVDAA YEVAERGTAY
FFKGPHYWIT RGFQMQGPPR TIYDFGFPRH VQQIDAAVYL REPQKTLFFV GDEYYSYDER
KRKMEKDYPK NTEEEFSGVN GQIDAAVELN GYIYFFSGPK TYKYDTEKED VVSVVKSSSW
IGC


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