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

 MMP20_MOUSE             Reviewed;         482 AA.
P57748; A7MCV5;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 1.
28-FEB-2018, entry version 142.
RecName: Full=Matrix metalloproteinase-20;
Short=MMP-20;
EC=3.4.24.-;
AltName: Full=Enamel metalloproteinase;
AltName: Full=Enamelysin;
Flags: Precursor;
Name=Mmp20;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/SvJ;
PubMed=10610728; DOI=10.1006/geno.1999.5990;
Caterina J., Shi J., Krakora S., Bartlett J.D., Engler J.A.,
Kozak C.A., Birkedal-Hansen H.;
"Isolation, characterization, and chromosomal location of the mouse
enamelysin gene.";
Genomics 62:308-311(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- 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:0000250|UniProtKB:O60882}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 2 Calcium ions per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- 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.
-!- PTM: Autoactivates at least at the 106-Asn-|-Tyr-107 site.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF156956; AAF28472.1; -; Genomic_DNA.
EMBL; AF156947; AAF28472.1; JOINED; Genomic_DNA.
EMBL; AF156948; AAF28472.1; JOINED; Genomic_DNA.
EMBL; AF156949; AAF28472.1; JOINED; Genomic_DNA.
EMBL; AF156950; AAF28472.1; JOINED; Genomic_DNA.
EMBL; AF156951; AAF28472.1; JOINED; Genomic_DNA.
EMBL; AF156952; AAF28472.1; JOINED; Genomic_DNA.
EMBL; AF156953; AAF28472.1; JOINED; Genomic_DNA.
EMBL; AF156954; AAF28472.1; JOINED; Genomic_DNA.
EMBL; AF156955; AAF28472.1; JOINED; Genomic_DNA.
EMBL; AF155933; AAF28470.1; -; mRNA.
EMBL; BC152335; AAI52336.1; -; mRNA.
EMBL; BC152336; AAI52337.1; -; mRNA.
CCDS; CCDS22809.1; -.
RefSeq; NP_038931.1; NM_013903.2.
UniGene; Mm.390121; -.
ProteinModelPortal; P57748; -.
STRING; 10090.ENSMUSP00000034487; -.
MEROPS; M10.019; -.
PhosphoSitePlus; P57748; -.
PaxDb; P57748; -.
PRIDE; P57748; -.
DNASU; 30800; -.
Ensembl; ENSMUST00000034487; ENSMUSP00000034487; ENSMUSG00000018620.
GeneID; 30800; -.
KEGG; mmu:30800; -.
UCSC; uc009ocu.1; mouse.
CTD; 9313; -.
MGI; MGI:1353466; Mmp20.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; P57748; -.
KO; K07999; -.
OMA; GDTHFDN; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; P57748; -.
TreeFam; TF315428; -.
BRENDA; 3.4.24.B6; 3474.
Reactome; R-MMU-1442490; Collagen degradation.
Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
PRO; PR:P57748; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000018620; -.
CleanEx; MM_MMP20; -.
Genevisible; P57748; MM.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0097186; P:amelogenesis; IMP:MGI.
GO; GO:0022617; P:extracellular matrix disassembly; IMP:MGI.
GO; GO:0030163; P:protein catabolic process; IMP:MGI.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
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.
PANTHER; PTHR10201:SF125; PTHR10201:SF125; 1.
Pfam; PF00045; Hemopexin; 4.
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.
2: Evidence at transcript level;
Autocatalytic cleavage; Calcium; Complete proteome; Disulfide bond;
Extracellular matrix; Hydrolase; Metal-binding; Metalloprotease;
Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 106 {ECO:0000250}.
/FTId=PRO_0000028835.
CHAIN 107 482 Matrix metalloproteinase-20.
/FTId=PRO_0000028836.
REPEAT 292 342 Hemopexin 1.
REPEAT 343 388 Hemopexin 2.
REPEAT 390 438 Hemopexin 3.
REPEAT 439 482 Hemopexin 4.
MOTIF 97 104 Cysteine switch. {ECO:0000250}.
ACT_SITE 226 226 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 99 99 Zinc 1; in inhibited form. {ECO:0000250}.
METAL 163 163 Calcium 1. {ECO:0000250}.
METAL 164 164 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 165 165 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 175 175 Zinc 2. {ECO:0000250}.
METAL 177 177 Zinc 2. {ECO:0000250}.
METAL 182 182 Calcium 2. {ECO:0000250}.
METAL 183 183 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 185 185 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 187 187 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 190 190 Zinc 2. {ECO:0000250}.
METAL 196 196 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 197 197 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 199 199 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 201 201 Calcium 1. {ECO:0000250}.
METAL 203 203 Zinc 2. {ECO:0000250}.
METAL 205 205 Calcium 2. {ECO:0000250}.
METAL 208 208 Calcium 2. {ECO:0000250}.
METAL 225 225 Zinc 1; catalytic. {ECO:0000250}.
METAL 229 229 Zinc 1; catalytic. {ECO:0000250}.
METAL 235 235 Zinc 1; catalytic. {ECO:0000250}.
DISULFID 295 482 {ECO:0000250}.
SEQUENCE 482 AA; 54373 MW; 366149FAF2BDC8BB CRC64;
MKVLPASGLA VLVTALKFAT ADPNLLAATP RTFRSNYHLA QAYLDKYYTK KGGPQAGEMV
ARESNPMIRR IKELQIFFGL KVTGKLDQNT MNVIKKPRCG VPDVANYRLF PGEPKWKKNI
LTYRISKYTP SMSPTEVDKA IQMALHAWST AVPLNFVRIN SGEADIMISF ETGDHGDSYP
FDGPRGTLAH AFAPGEGLGG DTHFDNAEKW TMGTNGFNLF TVAAHEFGHA LGLGHSTDPS
ALMYPTYKYQ NPYRFHLPKD DVKGIQALYG PRKIFPGKPT MPHIPPHKPS IPDLCDSSSS
FDAVTMLGKE LLFFKDRIFW RRQVHLPTGI RPSTITSSFP QLMSNVDAAY EVAERGIAFF
FKGPHYWVTR GFHMQGPPRT IYDFGFPRHV QRIDAAVYLK EPQKTLFFVG EEYYSYDERK
KKMEKDYPKN TEEEFSGVSG HIDAAVELNG YIYFFSGRKT FKYDTEKEDV VSVVKSSSWI
GC


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