MMP1B_MOUSE
ID MMP1B_MOUSE Reviewed; 463 AA.
AC Q9EPL6;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Interstitial collagenase B;
DE EC=3.4.24.7;
DE AltName: Full=Matrix metalloproteinase-1b;
DE Short=MMP-1b;
DE AltName: Full=Mcol-B;
DE Flags: Precursor;
GN Name=Mmp1b; Synonyms=McolB;
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 [MRNA].
RX PubMed=11113146; DOI=10.1074/jbc.m009586200;
RA Balbin M., Fueyo A., Knauper V., Lopez J.M., Alvarez J., Sanchez L.M.,
RA Quesada V., Bordallo J., Murphy G., Lopez-Otin C.;
RT "Identification and enzymatic characterization of two diverging murine
RT counterparts of human interstitial collagenase (MMP-1) expressed at sites
RT of embryo implantation.";
RL J. Biol. Chem. 276:10253-10262(2001).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
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 -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; AJ278461; CAC18879.1; -; mRNA.
DR CCDS; CCDS22805.1; -.
DR AlphaFoldDB; Q9EPL6; -.
DR SMR; Q9EPL6; -.
DR STRING; 10090.ENSMUSP00000047261; -.
DR MEROPS; M10.034; -.
DR GlyGen; Q9EPL6; 1 site.
DR iPTMnet; Q9EPL6; -.
DR PhosphoSitePlus; Q9EPL6; -.
DR PaxDb; Q9EPL6; -.
DR PRIDE; Q9EPL6; -.
DR MGI; MGI:1933847; Mmp1b.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; Q9EPL6; -.
DR PhylomeDB; Q9EPL6; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-MMU-210991; Basigin interactions.
DR PRO; PR:Q9EPL6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9EPL6; protein.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
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; ISO:MGI.
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:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
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; 2.
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 2: Evidence at transcript level;
KW Autocatalytic cleavage; Calcium; Collagen degradation; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Zinc; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..96
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042647"
FT CHAIN 97..463
FT /note="Interstitial collagenase B"
FT /id="PRO_0000042648"
FT REPEAT 278..321
FT /note="Hemopexin 1"
FT REPEAT 322..368
FT /note="Hemopexin 2"
FT REPEAT 371..419
FT /note="Hemopexin 3"
FT REPEAT 420..463
FT /note="Hemopexin 4"
FT REGION 95..273
FT /note="Metalloprotease"
FT /evidence="ECO:0000250"
FT MOTIF 87..94
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 89
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 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 275..463
FT /evidence="ECO:0000250"
SQ SEQUENCE 463 AA; 53492 MW; 46013AB9D106C3F1 CRC64;
MPSLPLLLRL WAASSYSFPV IQDGLQKNVK TVWKYLENYY NLGKNMQAKN VNGKEVMAEK
LRQMQQLFGL KVTGNSDPET LRAMKKPRCG VPDVAPYAIT HNNPRWTKTH LTYSILNYTP
YLSKAVVEDA IARAFRVWSD VTPLTFQRVF EEEGDIVLSF HRGDHGDLYT FDGSKYHFAH
AFLPGLGLGG NVHYDLDQKW TDNNEDFNLF YVTAHELGHS LGLSHSNDEE ALMFPSYTWS
NKDFVLNQDD INRIQALYGP SPNPIQLTDA TLDPCNSGLT FDAIITYRGE VIFFKDRFYI
RVISFLPEPL IDVIDLTWPN LPGKFDAAYE VSGVDELRFF KGSKVWAVQE QNVLEGFPMD
IQSFFGFPSN VTNIDAAVCE EETGKTYFFV DHMYWRYDEN TRSMDPGYPR LIAEDFPGID
YKVDDVIQKE DNFYFFHQSI QYRFNLKTRR IDDSSDINTW FNC
