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 24-JAN-2024, entry version 172. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000034487; -. DR ProteomicsDB; 295687; -. DR Antibodypedia; 31760; 310 antibodies from 29 providers. DR DNASU; 30800; -. DR Ensembl; ENSMUST00000034487.4; ENSMUSP00000034487.3; ENSMUSG00000018620.4. DR GeneID; 30800; -. DR KEGG; mmu:30800; -. DR UCSC; uc009ocu.1; mouse. DR AGR; MGI:1353466; -. 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; YPTYKYK; -. DR OrthoDB; 391167at2759; -. 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 77 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 cell types or tissues. DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. 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; 3.40.390.10; Collagenase (Catalytic Domain); 1. DR Gene3D; 2.110.10.10; Hemopexin-like domain; 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; 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; MATRIX METALLOPROTEINASE; 1. DR PANTHER; PTHR10201:SF125; MATRIX METALLOPROTEINASE-20; 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; SSF50923; Hemopexin-like domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR SUPFAM; SSF47090; PGBD-like; 1. DR PROSITE; PS00546; CYSTEINE_SWITCH; 1. DR PROSITE; PS51642; HEMOPEXIN_2; 4. DR PROSITE; PS00142; ZINC_PROTEASE; 1. DR Genevisible; P57748; MM. 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 //