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

 MMP2_RABIT              Reviewed;         662 AA.
P50757;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=72 kDa type IV collagenase;
EC=3.4.24.24;
AltName: Full=72 kDa gelatinase;
AltName: Full=Gelatinase A;
AltName: Full=Matrix metalloproteinase-2;
Short=MMP-2;
Contains:
RecName: Full=PEX;
Flags: Precursor;
Name=MMP2;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Japanese white; TISSUE=Synovial cell;
PubMed=8679695; DOI=10.1016/0167-4781(96)00050-4;
Matsumoto S., Katoh M., Watanabe T., Masuho Y.;
"Molecular cloning of rabbit matrix metalloproteinase-2 and its broad
expression at several tissues.";
Biochim. Biophys. Acta 1307:137-139(1996).
-!- 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: Cleavage of gelatin type I and collagen types
IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-
Ile-Ala-Gly-Gln.
-!- 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) (By similarity). 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; D63579; BAA09796.1; -; mRNA.
PIR; S70365; S70365.
RefSeq; NP_001075678.1; NM_001082209.1.
UniGene; Ocu.6274; -.
ProteinModelPortal; P50757; -.
SMR; P50757; -.
STRING; 9986.ENSOCUP00000005803; -.
MEROPS; M10.003; -.
PRIDE; P50757; -.
GeneID; 100009000; -.
KEGG; ocu:100009000; -.
CTD; 4313; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
HOGENOM; HOG000217926; -.
HOVERGEN; HBG052484; -.
InParanoid; P50757; -.
KO; K01398; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
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.
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; 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; Autocatalytic cleavage; 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 29 {ECO:0000250|UniProtKB:P33436}.
PROPEP 30 109 Activation peptide.
/FTId=PRO_0000028718.
CHAIN 110 662 72 kDa type IV collagenase.
/FTId=PRO_0000028719.
CHAIN 445 662 PEX. {ECO:0000250}.
/FTId=PRO_0000391628.
DOMAIN 228 276 Fibronectin type-II 1.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 286 334 Fibronectin type-II 2.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 344 392 Fibronectin type-II 3.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
REPEAT 474 518 Hemopexin 1.
REPEAT 519 565 Hemopexin 2.
REPEAT 567 615 Hemopexin 3.
REPEAT 616 662 Hemopexin 4.
REGION 110 221 Collagenase-like 1.
REGION 222 396 Collagen-binding.
REGION 397 467 Collagenase-like 2.
REGION 414 662 Required for inhibitor TIMP2 binding.
{ECO:0000250}.
MOTIF 100 107 Cysteine switch. {ECO:0000250}.
ACT_SITE 404 404 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 102 102 Zinc 2; in inhibited form. {ECO:0000250}.
METAL 134 134 Calcium 1. {ECO:0000250}.
METAL 168 168 Calcium 2. {ECO:0000250}.
METAL 178 178 Zinc 1. {ECO:0000250}.
METAL 180 180 Zinc 1. {ECO:0000250}.
METAL 185 185 Calcium 3. {ECO:0000250}.
METAL 186 186 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 193 193 Zinc 1. {ECO:0000250}.
METAL 200 200 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 202 202 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 204 204 Calcium 2. {ECO:0000250}.
METAL 206 206 Zinc 1. {ECO:0000250}.
METAL 208 208 Calcium 3. {ECO:0000250}.
METAL 209 209 Calcium 1. {ECO:0000250}.
METAL 211 211 Calcium 3. {ECO:0000250}.
METAL 403 403 Zinc 2; catalytic. {ECO:0000250}.
METAL 407 407 Zinc 2; catalytic. {ECO:0000250}.
METAL 413 413 Zinc 2; catalytic. {ECO:0000250}.
METAL 478 478 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 523 523 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 571 571 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 620 620 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
CARBOHYD 575 575 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 644 644 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 233 259 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 247 274 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 291 317 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 305 332 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 349 375 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 363 390 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 471 662 {ECO:0000255|PROSITE-ProRule:PRU00479}.
SEQUENCE 662 AA; 73803 MW; 1CC246B270E440C8 CRC64;
MEALGARGAL AGFLRALCVL GCLLGRATAP PSPVIKFPGD VAPKTDKELA VQYLNTFYGC
PKDSCNLFVL KDTLKKMQKF FGLPQTGELD QSTIETMRKP RCGNPDVANY NFFPRKPKWD
KNQITYRIIG YTPDLDPETV DDAFARAFQV WSNVTPLRFS RIHDGEADIM INFGRWEHGD
GYPFDGKDGL LAHAFAPGTG VGGDSHFDDD ELWTLGEGQV VRVKYGNADG EYCKFPFLFN
GKEYTSCTDT GRSDGFLWCS TTYNFEKDGK YGFCPHEALF TMGGNADGQP CKFPFRFQGT
SYSSCTTEGR TDGYRWCGTT EDYDRDKKYG FCPETAMSTI GGNSEGAPCV FPFTFLGNKY
ESCTSAGRSD GKMWCATSTN YDDDRKWGFC PDQGYSLFLV AAHEFGHAMG LEHSQDPGAL
MAPIYTYTKN FRLSQDDIKG IQELYGASPD AGTDAGTGPT PTLGPVTPEI CTQDIVFDGI
AQIRGEIFFF KDRFIWRTVT PGDKPMGPLL VATFWPELPE KIDAVYEAPQ EEKAVFFAGN
EYWVYSASTL ERGYPKPLTS LGLPPDVQRV DAAFNWSKNK KTYIFAGDKF WRYNEVKKKM
DPGFPRLIAD AWNAIPDHLD AVVDLQGSGH SYFFKGTYYL KLENQSLKSV KVGSIKTDWL
GC


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