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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
 
 
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