MMP20_BOVIN
ID MMP20_BOVIN Reviewed; 481 AA.
AC O18767;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF N-TERMINUS.
RC TISSUE=Enamel organ;
RX PubMed=9541246; DOI=10.1111/j.1600-0722.1998.tb02196.x;
RA DenBesten P.K., Punzi J.S., Li W.;
RT "Purification and sequencing of a 21 kDa and 25 kDa bovine enamel
RT metalloproteinase.";
RL Eur. J. Oral Sci. 106 Suppl. 1:345-349(1998).
RN [2]
RP CHARACTERIZATION.
RX PubMed=10515200; DOI=10.1046/j.0909-8836.1999.eos107506.x;
RA Li W., Machule D., Gao C., DenBesten P.K.;
RT "Activation of recombinant bovine matrix metalloproteinase-20 and its
RT hydrolysis of two amelogenin oligopeptides.";
RL Eur. J. Oral Sci. 107:352-359(1999).
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-Ser-|-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.
CC -!- TISSUE SPECIFICITY: Expressed 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 105-Asn-|-Tyr-106 site.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; AF009922; AAB66599.1; -; mRNA.
DR RefSeq; NP_776816.1; NM_174391.2.
DR AlphaFoldDB; O18767; -.
DR SMR; O18767; -.
DR STRING; 9913.ENSBTAP00000018936; -.
DR MEROPS; M10.019; -.
DR PaxDb; O18767; -.
DR GeneID; 281916; -.
DR KEGG; bta:281916; -.
DR CTD; 9313; -.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; O18767; -.
DR OrthoDB; 1075463at2759; -.
DR BRENDA; 3.4.24.B6; 908.
DR Proteomes; UP000009136; Unplaced.
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:0030198; P:extracellular matrix organization; IBA:GO_Central.
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; 3.
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 1: Evidence at protein level;
KW Autocatalytic cleavage; Calcium; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..105
FT /evidence="ECO:0000250"
FT /id="PRO_0000028831"
FT CHAIN 106..481
FT /note="Matrix metalloproteinase-20"
FT /id="PRO_0000028832"
FT REPEAT 291..341
FT /note="Hemopexin 1"
FT REPEAT 342..387
FT /note="Hemopexin 2"
FT REPEAT 389..437
FT /note="Hemopexin 3"
FT REPEAT 438..481
FT /note="Hemopexin 4"
FT MOTIF 96..103
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 98
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 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 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 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 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="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 294..481
FT /evidence="ECO:0000250"
FT CONFLICT 115
FT /note="W -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 53781 MW; 0E72FC5AFE5A719E CRC64;
MLPASGLAVL LVTALKFSTA APSLPAASPR TSRNNYRLAQ AYLDKYYTKK GGPQIGEMVA
RGGNSTVKKI KELQEFFGLR VTGKLDRATM DVIKRPRCGV PDVANYRLFP GEPKWKKNTL
TYRISKYTPS MTPAEVDRAM EMALRAWSSA VPLNFVRINA GEADIMISFE TGDHGDSYPF
DGPRGTLAHA FAPGEGLGGD THFDNAEKWT MGTNGFNLFT VAAHEFGHAL GLAHSTDPSA
LMFPTYKYQN PYGFRLPKDD VKGIQALYGP RRAFSGKPTA PHGPPHNPSI PDLCDSNLSF
DAVTMLGKEL LLFRDRIFWR RQVHLMSGIR PSTITSSFPQ LMSNVDAAYE VAERGTAYFF
KGPHYWITRG FQMQGPPRTI YDFGFPRYVQ RIDAAVYLKD AQKTLFFVGD EYYSYDERKR
KMEKDYPKST EEEFSGVNGQ IDAAVELNGY IYFFSGPKAY KSDTEKEDVV SELKSSSWIG
C
