MMP20_MOUSE
ID MMP20_MOUSE Reviewed; 482 AA.
AC P57748; A7MCV5;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Matrix metalloproteinase-20;
DE Short=MMP-20;
DE EC=3.4.24.-;
DE AltName: Full=Enamel metalloproteinase;
DE AltName: Full=Enamelysin;
DE Flags: Precursor;
GN Name=Mmp20;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ;
RX PubMed=10610728; DOI=10.1006/geno.1999.5990;
RA Caterina J., Shi J., Krakora S., Bartlett J.D., Engler J.A., Kozak C.A.,
RA Birkedal-Hansen H.;
RT "Isolation, characterization, and chromosomal location of the mouse
RT enamelysin gene.";
RL Genomics 62:308-311(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Degrades amelogenin, the major protein component of the
CC enamel matrix and two of the macromolecules characterizing the
CC cartilage extracellular matrix: aggrecan and the cartilage oligomeric
CC matrix protein (COMP). May play a central role in tooth enamel
CC formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site.
CC {ECO:0000250|UniProtKB:O60882}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 Calcium ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the enamel organ.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: Autoactivates at least at the 106-Asn-|-Tyr-107 site.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; AF156956; AAF28472.1; -; Genomic_DNA.
DR EMBL; AF156947; AAF28472.1; JOINED; Genomic_DNA.
DR EMBL; AF156948; AAF28472.1; JOINED; Genomic_DNA.
DR EMBL; AF156949; AAF28472.1; JOINED; Genomic_DNA.
DR EMBL; AF156950; AAF28472.1; JOINED; Genomic_DNA.
DR EMBL; AF156951; AAF28472.1; JOINED; Genomic_DNA.
DR EMBL; AF156952; AAF28472.1; JOINED; Genomic_DNA.
DR EMBL; AF156953; AAF28472.1; JOINED; Genomic_DNA.
DR EMBL; AF156954; AAF28472.1; JOINED; Genomic_DNA.
DR EMBL; AF156955; AAF28472.1; JOINED; Genomic_DNA.
DR EMBL; AF155933; AAF28470.1; -; mRNA.
DR EMBL; BC152335; AAI52336.1; -; mRNA.
DR EMBL; BC152336; AAI52337.1; -; mRNA.
DR CCDS; CCDS22809.1; -.
DR RefSeq; NP_038931.1; NM_013903.2.
DR AlphaFoldDB; P57748; -.
DR SMR; P57748; -.
DR STRING; 10090.ENSMUSP00000034487; -.
DR MEROPS; M10.019; -.
DR PhosphoSitePlus; P57748; -.
DR PaxDb; P57748; -.
DR PRIDE; P57748; -.
DR ProteomicsDB; 295687; -.
DR Antibodypedia; 31760; 281 antibodies from 28 providers.
DR DNASU; 30800; -.
DR Ensembl; ENSMUST00000034487; ENSMUSP00000034487; ENSMUSG00000018620.
DR GeneID; 30800; -.
DR KEGG; mmu:30800; -.
DR UCSC; uc009ocu.1; mouse.
DR CTD; 9313; -.
DR MGI; MGI:1353466; Mmp20.
DR VEuPathDB; HostDB:ENSMUSG00000018620; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000161277; -.
DR HOGENOM; CLU_015489_6_0_1; -.
DR InParanoid; P57748; -.
DR OMA; HYWVTRG; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; P57748; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.B6; 3474.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR BioGRID-ORCS; 30800; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Mmp25; mouse.
DR PRO; PR:P57748; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P57748; protein.
DR Bgee; ENSMUSG00000018620; Expressed in molar tooth and 7 other tissues.
DR Genevisible; P57748; MM.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0097186; P:amelogenesis; IMP:MGI.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0022617; P:extracellular matrix disassembly; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.110.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR028716; MMP20.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR021158; Pept_M10A_Zn_BS.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR PANTHER; PTHR10201:SF125; PTHR10201:SF125; 1.
DR Pfam; PF00045; Hemopexin; 4.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Autocatalytic cleavage; Calcium; Disulfide bond; Extracellular matrix;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..106
FT /evidence="ECO:0000250"
FT /id="PRO_0000028835"
FT CHAIN 107..482
FT /note="Matrix metalloproteinase-20"
FT /id="PRO_0000028836"
FT REPEAT 292..342
FT /note="Hemopexin 1"
FT REPEAT 343..388
FT /note="Hemopexin 2"
FT REPEAT 390..438
FT /note="Hemopexin 3"
FT REPEAT 439..482
FT /note="Hemopexin 4"
FT MOTIF 97..104
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 295..482
FT /evidence="ECO:0000250"
SQ 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
