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MMP2_BOVIN
ID   MMP2_BOVIN              Reviewed;         661 AA.
AC   Q9GLE5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=72 kDa type IV collagenase;
DE            EC=3.4.24.24 {ECO:0000250|UniProtKB:P08253};
DE   AltName: Full=72 kDa gelatinase;
DE   AltName: Full=Matrix metalloproteinase-2;
DE            Short=MMP-2;
DE   Contains:
DE     RecName: Full=PEX;
DE   Flags: Precursor;
GN   Name=MMP2;
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].
RA   Yan L., Zhang B., Tsang P., Fang J., Yu Y., Ingber D.E., Moses M.A.;
RT   "Molecular cloning and biological characterization of bovine matrix
RT   metalloprotease 2 (bMMP-2).";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ubiquitinous metalloproteinase that is involved in diverse
CC       functions such as remodeling of the vasculature, angiogenesis, tissue
CC       repair, tumor invasion, inflammation, and atherosclerotic plaque
CC       rupture. As well as degrading extracellular matrix proteins, can also
CC       act on several nonmatrix proteins such as big endothelial 1 and beta-
CC       type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu
CC       bond. Appears to have a role in myocardial cell death pathways.
CC       Contributes to myocardial oxidative stress by regulating the activity
CC       of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of
CC       the fibrovascular tissues (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: PEX, the C-terminal non-catalytic fragment of MMP2, posseses
CC       anti-angiogenic and anti-tumor properties and inhibits cell migration
CC       and cell adhesion to FGF2 and vitronectin. Ligand for integrin alpha-
CC       v/beta-3 on the surface of blood vessels (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of gelatin type I and collagen types IV, V, VII, X.
CC         Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.;
CC         EC=3.4.24.24; Evidence={ECO:0000250|UniProtKB:P08253};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P08253};
CC       Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P08253};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P08253};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P08253};
CC   -!- SUBUNIT: Interacts (via the C-terminal hemopexin-like domains-
CC       containing region) with the integrin alpha-V/beta-3; the interaction
CC       promotes vascular invasion in angiogenic vessels and melamoma cells.
CC       Interacts (via the C-terminal PEX domain) with TIMP2 (via the C-
CC       terminal); the interaction inhibits the degradation activity. Interacts
CC       with GSK3B (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}. Membrane {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Colocalizes with integrin alphaV/beta3 at the membrane surface in
CC       angiogenic blood vessels and melanomas. Found in mitochondria, along
CC       microfibrils, and in nuclei of cardiomyocytes (By similarity).
CC       {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: Phosphorylation on multiple sites modulates enzymatic activity.
CC       Phosphorylated by PKC in vitro (By similarity). {ECO:0000250}.
CC   -!- PTM: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-
CC       MMP3). Autocatalytic cleavage in the C-terminal produces the anti-
CC       angiogenic peptide, PEX. This processing appears to be facilitated by
CC       binding integrinv/beta3 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR   EMBL; AF290428; AAG28169.1; -; mRNA.
DR   RefSeq; NP_777170.1; NM_174745.2.
DR   AlphaFoldDB; Q9GLE5; -.
DR   SMR; Q9GLE5; -.
DR   STRING; 9913.ENSBTAP00000025657; -.
DR   MEROPS; M10.003; -.
DR   PaxDb; Q9GLE5; -.
DR   PRIDE; Q9GLE5; -.
DR   GeneID; 282872; -.
DR   KEGG; bta:282872; -.
DR   CTD; 4313; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   InParanoid; Q9GLE5; -.
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:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0071492; P:cellular response to UV-A; ISS:UniProtKB.
DR   GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00062; FN2; 3.
DR   CDD; cd00094; HX; 1.
DR   CDD; cd04278; ZnMc_MMP; 1.
DR   Gene3D; 2.10.10.10; -; 2.
DR   Gene3D; 2.110.10.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 2.
DR   InterPro; IPR028708; 72kDa_collagenase.
DR   InterPro; IPR000562; FN_type2_dom.
DR   InterPro; IPR036943; FN_type2_sf.
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; IPR013806; Kringle-like.
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   PANTHER; PTHR10201:SF29; PTHR10201:SF29; 1.
DR   Pfam; PF00040; fn2; 3.
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; SM00059; FN2; 3.
DR   SMART; SM00120; HX; 4.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF47090; SSF47090; 1.
DR   SUPFAM; SSF50923; SSF50923; 1.
DR   SUPFAM; SSF57440; SSF57440; 3.
DR   PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR   PROSITE; PS00023; FN2_1; 3.
DR   PROSITE; PS51092; FN2_2; 3.
DR   PROSITE; PS00024; HEMOPEXIN; 1.
DR   PROSITE; PS51642; HEMOPEXIN_2; 4.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Angiogenesis; Calcium; Collagen degradation; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW   Repeat; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000250|UniProtKB:P33436"
FT   PROPEP          31..110
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000244644"
FT   CHAIN           111..661
FT                   /note="72 kDa type IV collagenase"
FT                   /id="PRO_0000244645"
FT   CHAIN           446..661
FT                   /note="PEX"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000391625"
FT   DOMAIN          229..277
FT                   /note="Fibronectin type-II 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          287..335
FT                   /note="Fibronectin type-II 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          345..393
FT                   /note="Fibronectin type-II 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   REPEAT          469..517
FT                   /note="Hemopexin 1"
FT   REPEAT          518..564
FT                   /note="Hemopexin 2"
FT   REPEAT          566..614
FT                   /note="Hemopexin 3"
FT   REPEAT          615..661
FT                   /note="Hemopexin 4"
FT   REGION          111..222
FT                   /note="Collagenase-like 1"
FT   REGION          223..397
FT                   /note="Collagen-binding"
FT   REGION          398..466
FT                   /note="Collagenase-like 2"
FT   REGION          415..661
FT                   /note="Required for inhibitor TIMP2 binding"
FT                   /evidence="ECO:0000250"
FT   MOTIF           101..108
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        405
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         103
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|UniProtKB:P08253"
FT   BINDING         135
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         169
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         186
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         187
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         201
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         203
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         205
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         209
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         212
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         212
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         404
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         408
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         414
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         477
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         522
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         570
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   BINDING         619
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:P08253"
FT   CARBOHYD        574
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        643
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        234..260
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        248..275
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        292..318
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        306..333
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        350..376
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        364..391
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        470..661
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
SQ   SEQUENCE   661 AA;  73777 MW;  90545F7645E5F84D CRC64;
     MTEARVSRGA LAALLRALCA LGCLLGRAAA APSPIIKFPG DVAPKTDKEL AVQYLNTFYG
     CPKESCNLFV LKDTLKKMQK FFGLPQTGEL DQSTIETMRK PRCGNPDVAN YNFFPRKPKW
     DKNQITYRII GYTPDLDPQT VDDAFARAFQ VWSDVTPLRF SRIHDGEADI MINFGRWEHG
     DGYPFDGKDG LLAHAFAPGP GVGGDSHFDD DELRTLGEGQ VVRVKYGNAD GEYCKFPFRF
     NGKEYTSCTD TGRSDGFLWC STTYNFDKDG KYGFCPHEAL FTMGGNADGQ PCKFPFRFQG
     TSYDSCTTEG RTDGYRWCGT TEDYDRDKEY GFCPETAMST VGGNSEGAPC VLPFTFLGNK
     HESCTSAGRS DGKLWCATTS NYDDDRKWGF CPDQGYSLFL VAAHEFGHAM GLEHSQDPGA
     LMAPIYTYTK NFRLSHDDIQ GIQELYGASP DIDTGTGPTP TLGPVTPELC KQDIVFDGIS
     QIRGEIFFFK DRFIWRTVTP RDKPTGPLLV ATFWPELPEK IDAVYEDPQE EKAVFFAGNE
     YWVYSASTLE RGYPKPLTSL GLPPGVQKVD AAFNWSKNKK TYIFAGDKFW RYNEVKKKMD
     PGFPKLIADA WNAIPDNLDA VVDLQGGGHS YFFKGAYYLK LENQSLKSVK FGSIKSDWLG
     C
 
 
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