ID   MMP1_RAT                Reviewed;          15 AA.
AC   P81563;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 68.
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   AltName: Full=Myocardial collagenase;
DE   Flags: Fragment;
GN   Name=Mmp1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Heart;
RX   PubMed=8605638;
RA   Tyagi S.C., Cleutjens J.P.M.;
RT   "Myocardial collagenase: purification and structural characterization.";
RL   Can. J. Cardiol. 12:165-171(1996).
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. May play a
CC       role in the deterioration of the heart wall extracellular matrix
CC       proteins during the onset of dilated cardiomyopathy.
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   -!- PTM: The N-terminus is blocked.
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   BRENDA; 3.4.24.7; 5301.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Collagen degradation; Direct protein sequencing;
KW   Extracellular matrix; Hydrolase; Metalloprotease; Phosphoprotein; Protease;
KW   Reference proteome; Secreted; Zinc.
FT   CHAIN           <1..>15
FT                   /note="Interstitial collagenase"
FT                   /id="PRO_0000078182"
FT   NON_TER         1
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1787 MW;  15A57D24C0F6FD80 CRC64;
     DTLKSEKNAD FKDLY