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72 kDa type IV collagenase (EC 3.4.24.24) (72 kDa gelatinase) (Matrix metalloproteinase-2) (MMP-2) [Cleaved into: PEX]

 MMP2_BOVIN              Reviewed;         661 AA.
Q9GLE5;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-DEC-2018, entry version 101.
RecName: Full=72 kDa type IV collagenase;
EC=3.4.24.24;
AltName: Full=72 kDa gelatinase;
AltName: Full=Matrix metalloproteinase-2;
Short=MMP-2;
Contains:
RecName: Full=PEX;
Flags: Precursor;
Name=MMP2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Yan L., Zhang B., Tsang P., Fang J., Yu Y., Ingber D.E., Moses M.A.;
"Molecular cloning and biological characterization of bovine matrix
metalloprotease 2 (bMMP-2).";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Ubiquitinous metalloproteinase that is involved in
diverse functions such as remodeling of the vasculature,
angiogenesis, tissue repair, tumor invasion, inflammation, and
atherosclerotic plaque rupture. As well as degrading extracellular
matrix proteins, can also act on several nonmatrix proteins such
as big endothelial 1 and beta-type CGRP promoting
vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears
to have a role in myocardial cell death pathways. Contributes to
myocardial oxidative stress by regulating the activity of
GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of
the fibrovascular tissues (By similarity). {ECO:0000250}.
-!- FUNCTION: PEX, the C-terminal non-catalytic fragment of MMP2,
posseses anti-angiogenic and anti-tumor properties and inhibits
cell migration and cell adhesion to FGF2 and vitronectin. Ligand
for integrin alpha-v/beta-3 on the surface of blood vessels (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=Cleavage of gelatin type I and collagen types IV, V, VII,
X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-
Gln.; EC=3.4.24.24;
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- SUBUNIT: Interacts (via the C-terminal hemopexin-like domains-
containing region) with the integrin alpha-V/beta-3; the
interaction promotes vascular invasion in angiogenic vessels and
melamoma cells. Interacts (via the C-terminal PEX domain) with
TIMP2 (via the C-terminal); the interaction inhibits the
degradation activity. Interacts with GSK3B (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}. Membrane {ECO:0000250}. Nucleus
{ECO:0000250}. Note=Colocalizes with integrin alphaV/beta3 at the
membrane surface in angiogenic blood vessels and melanomas. Found
in mitochondria, along microfibrils, and in nuclei of
cardiomyocytes (By similarity). {ECO:0000250}.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: Phosphorylation on multiple sites modulates enzymatic
activity. Phosphorylated by PKC in vitro (By similarity).
{ECO:0000250}.
-!- PTM: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-
MMP3). Autocatalytic cleavage in the C-terminal produces the anti-
angiogenic peptide, PEX. This processing appears to be facilitated
by binding integrinv/beta3 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF290428; AAG28169.1; -; mRNA.
RefSeq; NP_777170.1; NM_174745.2.
UniGene; Bt.5313; -.
ProteinModelPortal; Q9GLE5; -.
SMR; Q9GLE5; -.
STRING; 9913.ENSBTAP00000025657; -.
MEROPS; M10.003; -.
PaxDb; Q9GLE5; -.
PRIDE; Q9GLE5; -.
GeneID; 282872; -.
KEGG; bta:282872; -.
CTD; 4313; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
HOGENOM; HOG000217926; -.
HOVERGEN; HBG052484; -.
InParanoid; Q9GLE5; -.
KO; K01398; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
CDD; cd00062; FN2; 3.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 1.10.101.10; -; 1.
Gene3D; 2.10.10.10; -; 3.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR028708; 72kDa_collagenase.
InterPro; IPR000562; FN_type2_dom.
InterPro; IPR036943; FN_type2_sf.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR013806; Kringle-like.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
InterPro; IPR036366; PGBDSf.
PANTHER; PTHR10201:SF29; PTHR10201:SF29; 4.
Pfam; PF00040; fn2; 3.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00059; FN2; 3.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
SUPFAM; SSF57440; SSF57440; 3.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00023; FN2_1; 3.
PROSITE; PS51092; FN2_2; 3.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Angiogenesis; Calcium; Collagen degradation; Complete proteome;
Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase;
Membrane; Metal-binding; Metalloprotease; Nucleus; Phosphoprotein;
Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 30 {ECO:0000250|UniProtKB:P33436}.
PROPEP 31 110 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000244644.
CHAIN 111 661 72 kDa type IV collagenase.
/FTId=PRO_0000244645.
CHAIN 446 661 PEX. {ECO:0000250}.
/FTId=PRO_0000391625.
DOMAIN 229 277 Fibronectin type-II 1.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 287 335 Fibronectin type-II 2.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 345 393 Fibronectin type-II 3.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
REPEAT 469 517 Hemopexin 1.
REPEAT 518 564 Hemopexin 2.
REPEAT 566 614 Hemopexin 3.
REPEAT 615 661 Hemopexin 4.
REGION 111 222 Collagenase-like 1.
REGION 223 397 Collagen-binding.
REGION 398 466 Collagenase-like 2.
REGION 415 661 Required for inhibitor TIMP2 binding.
{ECO:0000250}.
MOTIF 101 108 Cysteine switch. {ECO:0000250}.
ACT_SITE 405 405 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 103 103 Zinc 2; in inhibited form. {ECO:0000250}.
METAL 135 135 Calcium 1. {ECO:0000250}.
METAL 169 169 Calcium 2. {ECO:0000250}.
METAL 179 179 Zinc 1. {ECO:0000250}.
METAL 181 181 Zinc 1. {ECO:0000250}.
METAL 186 186 Calcium 3. {ECO:0000250}.
METAL 187 187 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 194 194 Zinc 1. {ECO:0000250}.
METAL 201 201 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 203 203 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 205 205 Calcium 2. {ECO:0000250}.
METAL 207 207 Zinc 1. {ECO:0000250}.
METAL 209 209 Calcium 3. {ECO:0000250}.
METAL 210 210 Calcium 1. {ECO:0000250}.
METAL 212 212 Calcium 3. {ECO:0000250}.
METAL 404 404 Zinc 2; catalytic. {ECO:0000250}.
METAL 408 408 Zinc 2; catalytic. {ECO:0000250}.
METAL 414 414 Zinc 2; catalytic. {ECO:0000250}.
METAL 477 477 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 522 522 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 570 570 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 619 619 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
CARBOHYD 574 574 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 643 643 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 234 260 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 248 275 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 292 318 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 306 333 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 350 376 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 364 391 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 470 661 {ECO:0000255|PROSITE-ProRule:PRU00479}.
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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