MMP1_BOVIN
ID MMP1_BOVIN Reviewed; 469 AA.
AC P28053;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Interstitial collagenase;
DE EC=3.4.24.7;
DE AltName: Full=Fibroblast collagenase;
DE AltName: Full=Matrix metalloproteinase-1;
DE Short=MMP-1;
DE Flags: Precursor;
GN Name=MMP1; Synonyms=CLG;
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].
RC TISSUE=Periodontium fibroblast;
RX PubMed=7894061; DOI=10.3109/10425179409039706;
RA Tamura M., Shimokawa H., Sasaki S.;
RT "Primary structure of bovine interstitial collagenase deduced from cDNA
RT sequence.";
RL DNA Seq. 5:63-66(1994).
RN [2]
RP PROTEIN SEQUENCE OF 19-39 AND 85-125.
RX PubMed=1311165; DOI=10.1016/0003-9861(92)90408-o;
RA Sudbeck B.D., Jeffrey J.J., Welgus H.G., Mecham R.P., McCourt D.,
RA Parks W.C.;
RT "Purification and characterization of bovine interstitial collagenase and
RT tissue inhibitor of metalloproteinases.";
RL Arch. Biochem. Biophys. 293:370-376(1992).
CC -!- FUNCTION: Cleaves collagens of types I, II, and III at one site in the
CC helical domain. Also cleaves collagens of types VII and X.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of the triple helix of collagen at about three-
CC quarters of the length of the molecule from the N-terminus, at 775-
CC Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates
CC and alpha-macroglobulins at bonds where P1' is a hydrophobic
CC residue.; EC=3.4.24.7;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 4 Ca(2+) ions per subunit. {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 -!- ACTIVITY REGULATION: Can be activated without removal of the activation
CC peptide.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
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: Tyrosine phosphorylated in platelets by PKDCC/VLK.
CC {ECO:0000250|UniProtKB:P03956}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; X58256; CAA41210.1; -; mRNA.
DR PIR; S14654; KCBOI.
DR RefSeq; NP_776537.1; NM_174112.1.
DR AlphaFoldDB; P28053; -.
DR SMR; P28053; -.
DR STRING; 9913.ENSBTAP00000021014; -.
DR MEROPS; M10.001; -.
DR PaxDb; P28053; -.
DR PRIDE; P28053; -.
DR GeneID; 281308; -.
DR KEGG; bta:281308; -.
DR CTD; 4312; -.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; P28053; -.
DR OrthoDB; 1075463at2759; -.
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:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071492; P:cellular response to UV-A; ISS:UniProtKB.
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; IPR018486; Hemopexin_CS.
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 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; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Collagen degradation; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Phosphoprotein; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:1311165"
FT PROPEP 19..99
FT /note="Activation peptide"
FT /id="PRO_0000028699"
FT CHAIN 100..469
FT /note="Interstitial collagenase"
FT /id="PRO_0000028700"
FT REPEAT 275..324
FT /note="Hemopexin 1"
FT REPEAT 325..371
FT /note="Hemopexin 2"
FT REPEAT 374..422
FT /note="Hemopexin 3"
FT REPEAT 423..466
FT /note="Hemopexin 4"
FT MOTIF 90..97
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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="3"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT MOD_RES 360
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 278..466
FT /evidence="ECO:0000250"
FT CONFLICT 22..23
FT /note="AT -> FP (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="D -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 35..36
FT /note="KK -> LL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="N -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106..108
FT /note="KSC -> NPR (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 53354 MW; B4A5504CE24BD7B5 CRC64;
MPRLPLLLLL LWGTGSHGFP AATSETQEQD VETVKKYLEN YYNLNSNGKK VERQRNGGLI
TEKLKQMQKF FGLRVTGKPD AETLNVMKQP RCGVPDVAPF VLTPGKSCWE NTNLTYRIEN
YTPDLSRADV DQAIEKAFQL WSNVTPLTFT KVSEGQADIM ISFVRGDHRD NSPFDGPGGN
LAHAFQPGAG IGGDAHFDDD EWWTSNFQDY NLYRVAAHEF GHSLGLAHST DIGALMYPSY
TFSGDVQLSQ DDIDGIQAIY GPSQNPTQPV GPQTPEVCDS KLTFDAITTI RGEVMFFKDR
FYMRTNPLYP EVELNFISVF WPQLPNGLQA AYEVADRDEV RFFKGNKYWA VKGQDVLRGY
PRDIYRSFGF PRTVKSIDAA VSEEDTGKTY FFVANKCWRY DEYKQSMDAG YPKMIAEDFP
GIGNKVDAVF QKGGFFYFFH GRRQYKFDPQ TKRILTLLKA NSWFNCRKN
