MMP20_PIG
ID MMP20_PIG Reviewed; 483 AA.
AC P79287;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Enamel organ;
RX PubMed=8996096; DOI=10.1016/s0378-1119(96)00525-2;
RA Bartlett J.D., Simmer J.P., Xue J., Margolis H.C., Moreno E.C.;
RT "Molecular cloning and mRNA tissue distribution of a novel matrix
RT metalloproteinase isolated from porcine enamel organ.";
RL Gene 183:123-128(1996).
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 (By similarity). {ECO:0000250}.
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 107-Asn-|-Tyr-108 site.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; U54825; AAB41396.1; -; mRNA.
DR PIR; JC5743; JC5743.
DR RefSeq; NP_999070.1; NM_213905.1.
DR AlphaFoldDB; P79287; -.
DR SMR; P79287; -.
DR STRING; 9823.ENSSSCP00000015906; -.
DR MEROPS; M10.019; -.
DR PaxDb; P79287; -.
DR PRIDE; P79287; -.
DR Ensembl; ENSSSCT00000016345; ENSSSCP00000015906; ENSSSCG00000014983.
DR Ensembl; ENSSSCT00005015959; ENSSSCP00005009532; ENSSSCG00005010198.
DR Ensembl; ENSSSCT00015072836; ENSSSCP00015029214; ENSSSCG00015054527.
DR Ensembl; ENSSSCT00025075029; ENSSSCP00025032524; ENSSSCG00025054778.
DR Ensembl; ENSSSCT00030101397; ENSSSCP00030046770; ENSSSCG00030072387.
DR Ensembl; ENSSSCT00035102700; ENSSSCP00035043845; ENSSSCG00035075536.
DR Ensembl; ENSSSCT00040074983; ENSSSCP00040032172; ENSSSCG00040055321.
DR Ensembl; ENSSSCT00045061917; ENSSSCP00045043541; ENSSSCG00045035908.
DR Ensembl; ENSSSCT00050062859; ENSSSCP00050026989; ENSSSCG00050046196.
DR Ensembl; ENSSSCT00055015360; ENSSSCP00055012073; ENSSSCG00055007859.
DR Ensembl; ENSSSCT00060068286; ENSSSCP00060029329; ENSSSCG00060050229.
DR Ensembl; ENSSSCT00065007938; ENSSSCP00065003342; ENSSSCG00065005915.
DR GeneID; 396939; -.
DR KEGG; ssc:396939; -.
DR CTD; 9313; -.
DR VGNC; VGNC:90275; MMP20.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000161277; -.
DR HOGENOM; CLU_015489_6_0_1; -.
DR InParanoid; P79287; -.
DR OMA; HYWVTRG; -.
DR OrthoDB; 1075463at2759; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.B6; 6170.
DR Reactome; R-SSC-1442490; Collagen degradation.
DR Reactome; R-SSC-1474228; Degradation of the extracellular matrix.
DR Reactome; R-SSC-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Proteomes; UP000008227; Chromosome 9.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000014983; Expressed in immune organ and 2 other tissues.
DR ExpressionAtlas; P79287; baseline.
DR Genevisible; P79287; SS.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0097186; P:amelogenesis; IBA:GO_Central.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0022617; P:extracellular matrix disassembly; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
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..22
FT /evidence="ECO:0000255"
FT PROPEP 23..107
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000028837"
FT CHAIN 108..483
FT /note="Matrix metalloproteinase-20"
FT /id="PRO_0000028838"
FT REPEAT 293..343
FT /note="Hemopexin 1"
FT REPEAT 344..389
FT /note="Hemopexin 2"
FT REPEAT 391..439
FT /note="Hemopexin 3"
FT REPEAT 440..483
FT /note="Hemopexin 4"
FT MOTIF 98..105
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 100
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 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 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 296..483
FT /evidence="ECO:0000250"
SQ SEQUENCE 483 AA; 54085 MW; 1235DAAAEF1A20B4 CRC64;
MKVLPASGLA VLLVTALKFS AAAPSLFAAT PRTSRNNYHL AQAYLDKYYT KKGGHQVGEM
VAKGGNSMVK KIKELQAFFG LRVTGKLDRT TMDVIKRPRC GVPDVANYRL FPGEPKWKKN
TLTYRISKYT PSMTPAEVDK AMEMALQAWS SAVPLSFVRV NAGEADIMIS FETGDHGDSY
PFDGPRGTLA HAFAPGEGLG GDTHFDNAEK WTMGMNGFNL FTVAAHEFGH ALGLAHSTDP
SALMYPTYKY QNPYGFHLPK DDVKGIQALY GPRKTFTGKP TVPHGPPHNP SLPDICDSSS
SFDAVTMLGK ELLFFRDRIF WRRQVHLMSG IRPSTITSSF PQLMSNVDAA YEVADRGMAY
FFKGPHYWIT RGFQMQGPPR TIYDFGFPRY VQRIDAAVHL KDTQKTLFFV GDEYYSYDER
KRKMDKDYPK NTEEEFSGVN GQIDAAVELN GYIYFFSGPK AYKYDTEKED VVSVLKSNSW
IGC
