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72 kDa type IV collagenase (EC 3.4.24.24) (72 kDa gelatinase) (Gelatinase A) (Matrix metalloproteinase-2) (MMP-2) (TBE-1) [Cleaved into: PEX]

 MMP2_HUMAN              Reviewed;         660 AA.
P08253; B2R6U1; B4DWH3; E9PE45; Q9UCJ8;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
27-SEP-2017, entry version 217.
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;
AltName: Full=TBE-1;
Contains:
RecName: Full=PEX;
Flags: Precursor;
Name=MMP2; Synonyms=CLG4A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2162831;
Huhtala P., Chow L.T., Tryggvason K.;
"Structure of the human type IV collagenase gene.";
J. Biol. Chem. 265:11077-11082(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1851724; DOI=10.1016/0888-7543(91)90408-7;
Collier I.E., Bruns G.A.P., Goldberg G.I., Gerhard D.S.;
"On the structure and chromosome location of the 72- and 92-kDa human
type IV collagenase genes.";
Genomics 9:429-434(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Teratocarcinoma, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-447 AND LEU-621.
NIEHS SNPs program;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
PubMed=2158484; DOI=10.1016/0888-7543(90)90486-E;
Huhtala P., Eddy R.L., Fan Y.S., Byers M.G., Shows T.B.,
Tryggvason K.;
"Completion of the primary structure of the human type IV collagenase
preproenzyme and assignment of the gene (CLG4) to the q21 region of
chromosome 16.";
Genomics 6:554-559(1990).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 19-660 (ISOFORM 1), AND PARTIAL PROTEIN
SEQUENCE.
PubMed=2834383;
Collier I.E., Wilhelm S.M., Eisen A.Z., Marmer B.L., Grant G.A.,
Seltzer J.L., Kronberger A., He C., Bauer E.A., Goldberg G.I.;
"H-ras oncogene-transformed human bronchial epithelial cells (TBE-1)
secrete a single metalloprotease capable of degrading basement
membrane collagen.";
J. Biol. Chem. 263:6579-6587(1988).
[9]
PROTEIN SEQUENCE OF 30-44.
TISSUE=Melanoma;
PubMed=1480041;
Stetler-Stevenson W.G., Krutzsch H.C., Liotta L.A.;
"TIMP-2: identification and characterization of a new member of the
metalloproteinase inhibitor family.";
Matrix Suppl. 1:299-306(1992).
[10]
INTERACTION WITH TIMP2.
PubMed=1655733;
Howard E.W., Banda M.J.;
"Binding of tissue inhibitor of metalloproteinases 2 to two distinct
sites on human 72-kDa gelatinase. Identification of a stabilization
site.";
J. Biol. Chem. 266:17972-17977(1991).
[11]
IDENTIFICATION OF RECEPTOR, AND SUBCELLULAR LOCATION.
PubMed=8646777; DOI=10.1016/S0092-8674(00)81235-0;
Brooks P.C., Stroemblad S., Sanders L.C., von Schalscha T.L.,
Aimes R.T., Stetler-Stevenson W.G., Quigley J.P., Cheresh D.A.;
"Localization of matrix metalloproteinase MMP-2 to the surface of
invasive cells by interaction with integrin alpha v beta 3.";
Cell 85:683-693(1996).
[12]
PROTEOLYTIC PROCESSING.
PubMed=9119036; DOI=10.1111/j.1432-1033.1997.t01-1-00653.x;
Butler G.S., Will H., Atkinson S.J., Murphy G.;
"Membrane-type-2 matrix metalloproteinase can initiate the processing
of progelatinase A and is regulated by the tissue inhibitors of
metalloproteinases.";
Eur. J. Biochem. 244:653-657(1997).
[13]
IDENTIFICATION OF RECEPTOR, AND FUNCTION.
PubMed=9476898; DOI=10.1016/S0092-8674(00)80931-9;
Brooks P.C., Silletti S., von Schalscha T.L., Friedlander M.,
Cheresh D.A.;
"Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase
fragment with integrin binding activity.";
Cell 92:391-400(1998).
[14]
FUNCTION.
PubMed=10559137; DOI=10.1161/01.RES.85.10.906;
Fernandez-Patron C., Radomski M.W., Davidge S.T.;
"Vascular matrix metalloproteinase-2 cleaves big endothelin-1 yielding
a novel vasoconstrictor.";
Circ. Res. 85:906-911(1999).
[15]
FUNCTION.
PubMed=11029402; DOI=10.1161/01.RES.87.8.670;
Fernandez-Patron C., Stewart K.G., Zhang Y., Koivunen E.,
Radomski M.W., Davidge S.T.;
"Vascular matrix metalloproteinase-2-dependent cleavage of calcitonin
gene-related peptide promotes vasoconstriction.";
Circ. Res. 87:670-676(2000).
[16]
FUNCTION OF PEX, TISSUE SPECIFICITY, AND INTERACTION WITH TIMP2.
PubMed=11751392;
Bello L., Lucini V., Carrabba G., Giussani C., Machluf M., Pluderi M.,
Nikas D., Zhang J., Tomei G., Villani R.M., Carroll R.S., Bikfalvi A.,
Black P.M.;
"Simultaneous inhibition of glioma angiogenesis, cell proliferation,
and invasion by a naturally occurring fragment of human
metalloproteinase-2.";
Cancer Res. 61:8730-8736(2001).
[17]
ENZYME REGULATION.
PubMed=11179305; DOI=10.1128/IAI.69.3.1402-1408.2001;
Gusman H., Travis J., Helmerhorst E.J., Potempa J., Troxler R.F.,
Oppenheim F.G.;
"Salivary histatin 5 is an inhibitor of both host and bacterial
enzymes implicated in periodontal disease.";
Infect. Immun. 69:1402-1408(2001).
[18]
IDENTIFICATION OF RECEPTOR, INTERACTION WITH TMP2, AND FUNCTION.
PubMed=11710594; DOI=10.1007/s004320100271;
Chattopadhyay N., Mitra A., Frei E., Chatterjee A.;
"Human cervical tumor cell (SiHa) surface alphavbeta3 integrin
receptor has associated matrix metalloproteinase (MMP-2) activity.";
J. Cancer Res. Clin. Oncol. 127:653-658(2001).
[19]
FUNCTION IN THE FORMATION OF THE FIBROVASCULAR TISSUES.
PubMed=12714657; DOI=10.1167/iovs.02-0662;
Noda K., Ishida S., Inoue M., Obata K., Oguchi Y., Okada Y., Ikeda E.;
"Production and activation of matrix metalloproteinase-2 in
proliferative diabetic retinopathy.";
Invest. Ophthalmol. Vis. Sci. 44:2163-2170(2003).
[20]
PROTEOLYTIC PROCESSING OF KISS1.
PubMed=12879005; DOI=10.1038/sj.onc.1206542;
Takino T., Koshikawa N., Miyamori H., Tanaka M., Sasaki T., Okada Y.,
Seiki M., Sato H.;
"Cleavage of metastasis suppressor gene product KiSS-1
protein/metastin by matrix metalloproteinases.";
Oncogene 22:4617-4626(2003).
[21]
SUBCELLULAR LOCATION.
PubMed=14766804; DOI=10.1096/fj.02-1202fje;
Kwan J.A., Schulze C.J., Wang W., Leon H., Sariahmetoglu M., Sung M.,
Sawicka J., Sims D.E., Sawicki G., Schulz R.;
"Matrix metalloproteinase-2 (MMP-2) is present in the nucleus of
cardiac myocytes and is capable of cleaving poly (ADP-ribose)
polymerase (PARP) in vitro.";
FASEB J. 18:690-692(2004).
[22]
PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17435175; DOI=10.1096/fj.06-7938com;
Sariahmetoglu M., Crawford B.D., Leon H., Sawicka J., Li L.,
Ballermann B.J., Holmes C., Berthiaume L.G., Holt A., Sawicki G.,
Schulz R.;
"Regulation of matrix metalloproteinase-2 (MMP-2) activity by
phosphorylation.";
FASEB J. 21:2486-2495(2007).
[23]
INTERACTION WITH GSK3B, AND FUNCTION.
PubMed=19493954; DOI=10.1093/cvr/cvp175;
Kandasamy A.D., Schulz R.;
"Glycogen synthase kinase-3beta is activated by matrix
metalloproteinase-2 mediated proteolysis in cardiomyoblasts.";
Cardiovasc. Res. 83:698-706(2009).
[24]
INDUCTION.
PubMed=18971601; DOI=10.1159/000166183;
Hua Y., Xue J., Sun F., Zhu L., Xie M.;
"Aspirin inhibits MMP-2 and MMP-9 expressions and activities through
upregulation of PPARalpha/gamma and TIMP gene expressions in ox-LDL-
stimulated macrophages derived from human monocytes.";
Pharmacology 83:18-25(2009).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[26]
ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22509276; DOI=10.1371/journal.pone.0034177;
Lovett D.H., Mahimkar R., Raffai R.L., Cape L., Maklashina E.,
Cecchini G., Karliner J.S.;
"A novel intracellular isoform of matrix metalloproteinase-2 induced
by oxidative stress activates innate immunity.";
PLoS ONE 7:E34177-E34177(2012).
[27]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 443-660.
PubMed=7583664; DOI=10.1038/nsb1195-938;
Libson A.M., Gittis A.G., Collier I.E., Marmer B.L., Goldberg G.I.,
Lattman E.E.;
"Crystal structure of the haemopexin-like C-terminal domain of
gelatinase A.";
Nat. Struct. Biol. 2:938-942(1995).
[28]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 458-660.
PubMed=8549817; DOI=10.1016/0014-5793(95)01435-7;
Gohlke U., Gomis-Rueth F.-X., Crabbe T., Murphy G., Docherty A.J.,
Bode W.;
"The C-terminal (haemopexin-like) domain structure of human gelatinase
A (MMP2): structural implications for its function.";
FEBS Lett. 378:126-130(1996).
[29]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-660 OF MUTANT ALA-404.
PubMed=10356396; DOI=10.1126/science.284.5420.1667;
Morgunova E., Tuuttila A., Bergmann U., Isupov M., Lindqvist Y.,
Schneider G., Tryggvason K.;
"Structure of human pro-matrix metalloproteinase-2: activation
mechanism revealed.";
Science 284:1667-1670(1999).
[30]
STRUCTURE BY NMR OF 278-336, AND DISULFIDE BONDS.
PubMed=10545322; DOI=10.1016/S0969-2126(00)80057-X;
Briknarova K., Grishaev A., Banyai L., Tordai H., Patthy L.,
Llinas M.;
"The second type II module from human matrix metalloproteinase 2:
structure, function and dynamics.";
Structure 7:1235-1245(1999).
[31]
STRUCTURE BY NMR OF 337-394 OF WILD TYPE AND IN COMPLEX WITH PPG
PEPTIDES.
PubMed=11320090; DOI=10.1074/jbc.M101105200;
Briknarova K., Gehrmann M., Banyai L., Tordai H., Patthy L.,
Llinas M.;
"Gelatin-binding region of human matrix metalloproteinase-2: solution
structure, dynamics, and function of the COL-23 two-domain
construct.";
J. Biol. Chem. 276:27613-27621(2001).
[32]
STRUCTURE BY NMR OF 110-446 IN COMPLEX WITH A HYDROXAMIC ACID
INHIBITOR.
PubMed=12147339; DOI=10.1016/S0167-4838(02)00307-2;
Feng Y., Likos J.J., Zhu L., Woodward H., Munie G., McDonald J.J.,
Stevens A.M., Howard C.P., De Crescenzo G.A., Welsch D., Shieh H.S.,
Stallings W.C.;
"Solution structure and backbone dynamics of the catalytic domain of
matrix metalloproteinase-2 complexed with a hydroxamic acid
inhibitor.";
Biochim. Biophys. Acta 1598:10-23(2002).
[33]
STRUCTURE BY NMR OF 223-282 OF WILD TYPE AND IN COMPLEX WITH A PPG
PEPTIDE.
PubMed=11928808; DOI=10.1515/BC.2002.014;
Gehrmann M., Briknarova K., Banyai L., Patthy L., Llinas M.;
"The col-1 module of human matrix metalloproteinase-2 (MMP-2):
structural/functional relatedness between gelatin-binding fibronectin
type II modules and lysine-binding kringle domains.";
Biol. Chem. 383:137-148(2002).
[34]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 30-660 IN COMPLEX WITH
INHIBITOR TIMP2.
PubMed=12032297; DOI=10.1073/pnas.102185399;
Morgunova E., Tuuttila A., Bergmann U., Tryggvason K.;
"Structural insight into the complex formation of latent matrix
metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.";
Proc. Natl. Acad. Sci. U.S.A. 99:7414-7419(2002).
[35]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 115-449.
PubMed=16392792; DOI=10.1021/jm050363f;
Pirard B., Matter H.;
"Matrix metalloproteinase target family landscape: a chemometrical
approach to ligand selectivity based on protein binding site
analysis.";
J. Med. Chem. 49:51-69(2006).
[36]
VARIANT MONA HIS-101, AND VARIANT TYR-210.
PubMed=11431697; DOI=10.1038/90100;
Martignetti J.A., Aqeel A.A., Sewairi W.A., Boumah C.E., Kambouris M.,
Mayouf S.A., Sheth K.V., Eid W.A., Dowling O., Harris J.,
Glucksman M.J., Bahabri S., Meyer B.F., Desnick R.J.;
"Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a
multicentric osteolysis and arthritis syndrome.";
Nat. Genet. 28:261-265(2001).
[37]
VARIANT MONA LYS-404.
PubMed=15691365; DOI=10.1111/j.1399-0004.2004.00402.x;
Zankl A., Bonafe L., Calcaterra V., Di Rocco M., Superti-Furga A.;
"Winchester syndrome caused by a homozygous mutation affecting the
active site of matrix metalloproteinase 2.";
Clin. Genet. 67:261-266(2005).
[38]
VARIANT MONA VAL-400 DEL.
PubMed=16542393; DOI=10.1111/j.1399-0004.2006.00584.x;
Rouzier C., Vanatka R., Bannwarth S., Philip N., Coussement A.,
Paquis-Flucklinger V., Lambert J.-C.;
"A novel homozygous MMP2 mutation in a family with Winchester
syndrome.";
Clin. Genet. 69:271-276(2006).
[39]
VARIANTS [LARGE SCALE ANALYSIS] THR-228; MET-498 AND ILE-644.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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 in association with MMP14.
-!- 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 integrinv/beta3 on the surface of blood vessels.
-!- FUNCTION: Isoform 2: Mediates the proteolysis of CHUK/IKKA and
initiates a primary innate immune response by inducing
mitochondrial-nuclear stress signaling with activation of the pro-
inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.
-!- 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;
Note=Binds 4 Ca(2+) ions per subunit.;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit.;
-!- ENZYME REGULATION: Inhibited by histatin-3 1/24 (histatin-5).
{ECO:0000269|PubMed:11179305}.
-!- 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.
{ECO:0000269|PubMed:11320090, ECO:0000269|PubMed:11710594,
ECO:0000269|PubMed:11751392, ECO:0000269|PubMed:11928808,
ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:12147339,
ECO:0000269|PubMed:1655733, ECO:0000269|PubMed:19493954}.
-!- INTERACTION:
Q8NBP7:PCSK9; NbExp=4; IntAct=EBI-1033518, EBI-7539251;
Q8IX30:SCUBE3; NbExp=2; IntAct=EBI-1033518, EBI-4479975;
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted, extracellular space,
extracellular matrix. Membrane. Nucleus. 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.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P08253-1; Sequence=Displayed;
Name=2;
IsoId=P08253-2; Sequence=VSP_044631;
Note=Induced by oxidative stress.;
Name=3;
IsoId=P08253-3; Sequence=VSP_045704;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Produced by normal skin fibroblasts. PEX is
expressed in a number of tumors including gliomas, breast and
prostate. {ECO:0000269|PubMed:11751392}.
-!- INDUCTION: Aspirin appears to inhibit expression.
{ECO:0000269|PubMed:18971601}.
-!- 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.
{ECO:0000269|PubMed:17435175}.
-!- 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. {ECO:0000269|PubMed:12879005,
ECO:0000269|PubMed:9119036}.
-!- DISEASE: Multicentric osteolysis, nodulosis, and arthropathy
(MONA) [MIM:259600]: An autosomal recessive syndrome characterized
by severe multicentric osteolysis with predominant involvement of
the hands and feet. Additional features include coarse face,
corneal opacities, patches of thickened, hyperpigmented skin,
hypertrichosis and gum hypertrophy. {ECO:0000269|PubMed:11431697,
ECO:0000269|PubMed:15691365, ECO:0000269|PubMed:16542393}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MMP2ID41396ch16q13.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp2/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M55593; AAA52028.1; -; Genomic_DNA.
EMBL; M58552; AAA52028.1; JOINED; Genomic_DNA.
EMBL; M55582; AAA52028.1; JOINED; Genomic_DNA.
EMBL; M55583; AAA52028.1; JOINED; Genomic_DNA.
EMBL; M55584; AAA52028.1; JOINED; Genomic_DNA.
EMBL; M55585; AAA52028.1; JOINED; Genomic_DNA.
EMBL; M55586; AAA52028.1; JOINED; Genomic_DNA.
EMBL; M55587; AAA52028.1; JOINED; Genomic_DNA.
EMBL; M55588; AAA52028.1; JOINED; Genomic_DNA.
EMBL; M55589; AAA52028.1; JOINED; Genomic_DNA.
EMBL; M55590; AAA52028.1; JOINED; Genomic_DNA.
EMBL; M55591; AAA52028.1; JOINED; Genomic_DNA.
EMBL; M55592; AAA52028.1; JOINED; Genomic_DNA.
EMBL; AK301536; BAG63035.1; -; mRNA.
EMBL; AK310314; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK312711; BAG35588.1; -; mRNA.
EMBL; AY738117; AAU10089.1; -; Genomic_DNA.
EMBL; AC007336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002576; AAH02576.1; -; mRNA.
EMBL; M33789; AAA52027.1; -; Genomic_DNA.
EMBL; J03210; AAA35701.1; -; mRNA.
CCDS; CCDS10752.1; -. [P08253-1]
CCDS; CCDS45487.1; -. [P08253-3]
CCDS; CCDS76869.1; -. [P08253-2]
PIR; A28153; A28153.
RefSeq; NP_001121363.1; NM_001127891.2. [P08253-3]
RefSeq; NP_001289437.1; NM_001302508.1. [P08253-2]
RefSeq; NP_001289438.1; NM_001302509.1. [P08253-2]
RefSeq; NP_001289439.1; NM_001302510.1. [P08253-2]
RefSeq; NP_004521.1; NM_004530.5. [P08253-1]
UniGene; Hs.513617; -.
PDB; 1CK7; X-ray; 2.80 A; A=30-660.
PDB; 1CXW; NMR; -; A=278-336.
PDB; 1EAK; X-ray; 2.66 A; A/B/C/D=32-452.
PDB; 1GEN; X-ray; 2.15 A; A=443-660.
PDB; 1GXD; X-ray; 3.10 A; A/B=30-660.
PDB; 1HOV; NMR; -; A=110-431.
PDB; 1J7M; NMR; -; A=337-394.
PDB; 1KS0; NMR; -; A=223-282.
PDB; 1QIB; X-ray; 2.80 A; A=115-217, A=394-449.
PDB; 1RTG; X-ray; 2.60 A; A=451-660.
PDB; 3AYU; X-ray; 2.00 A; A=110-450.
PDBsum; 1CK7; -.
PDBsum; 1CXW; -.
PDBsum; 1EAK; -.
PDBsum; 1GEN; -.
PDBsum; 1GXD; -.
PDBsum; 1HOV; -.
PDBsum; 1J7M; -.
PDBsum; 1KS0; -.
PDBsum; 1QIB; -.
PDBsum; 1RTG; -.
PDBsum; 3AYU; -.
ProteinModelPortal; P08253; -.
SMR; P08253; -.
BioGrid; 110457; 36.
CORUM; P08253; -.
IntAct; P08253; 18.
STRING; 9606.ENSP00000219070; -.
BindingDB; P08253; -.
ChEMBL; CHEMBL333; -.
DrugBank; DB05387; AE-941.
DrugBank; DB01197; Captopril.
DrugBank; DB04866; Halofuginone.
DrugBank; DB00786; Marimastat.
DrugBank; DB01630; SC-74020.
GuidetoPHARMACOLOGY; 1629; -.
MEROPS; M10.003; -.
iPTMnet; P08253; -.
PhosphoSitePlus; P08253; -.
BioMuta; MMP2; -.
DMDM; 116856; -.
EPD; P08253; -.
MaxQB; P08253; -.
PaxDb; P08253; -.
PeptideAtlas; P08253; -.
PRIDE; P08253; -.
DNASU; 4313; -.
Ensembl; ENST00000219070; ENSP00000219070; ENSG00000087245. [P08253-1]
Ensembl; ENST00000437642; ENSP00000394237; ENSG00000087245. [P08253-3]
Ensembl; ENST00000543485; ENSP00000444143; ENSG00000087245. [P08253-2]
Ensembl; ENST00000570308; ENSP00000461421; ENSG00000087245. [P08253-2]
GeneID; 4313; -.
KEGG; hsa:4313; -.
UCSC; uc002ehz.5; human. [P08253-1]
CTD; 4313; -.
DisGeNET; 4313; -.
EuPathDB; HostDB:ENSG00000087245.12; -.
GeneCards; MMP2; -.
HGNC; HGNC:7166; MMP2.
HPA; CAB002788; -.
HPA; HPA001939; -.
MalaCards; MMP2; -.
MIM; 120360; gene.
MIM; 259600; phenotype.
neXtProt; NX_P08253; -.
OpenTargets; ENSG00000087245; -.
Orphanet; 85196; Nodulosis-arthropathy-osteolysis syndrome.
Orphanet; 3460; Torg-Winchester syndrome.
PharmGKB; PA30877; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00870000136399; -.
HOGENOM; HOG000217926; -.
HOVERGEN; HBG052484; -.
InParanoid; P08253; -.
KO; K01398; -.
OMA; HESCTSA; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; P08253; -.
TreeFam; TF315428; -.
BioCyc; MetaCyc:HS01565-MONOMER; -.
BRENDA; 3.4.24.24; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SIGNOR; P08253; -.
ChiTaRS; MMP2; human.
EvolutionaryTrace; P08253; -.
GeneWiki; MMP2; -.
GenomeRNAi; 4313; -.
PMAP-CutDB; P08253; -.
PRO; PR:P08253; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000087245; -.
CleanEx; HS_MMP2; -.
ExpressionAtlas; P08253; baseline and differential.
Genevisible; P08253; HS.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0030017; C:sarcomere; IEA:Ensembl.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; EXP:Reactome.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0001955; P:blood vessel maturation; IEA:Ensembl.
GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:ParkinsonsUK-UCL.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
GO; GO:0045089; P:positive regulation of innate immune response; IEA:Ensembl.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IMP:BHF-UCL.
GO; GO:0006508; P:proteolysis; IDA:ParkinsonsUK-UCL.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
CDD; cd00062; FN2; 3.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 1.10.101.10; -; 1.
Gene3D; 2.10.10.10; -; 2.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR028708; 72kDa_collagenase.
InterPro; IPR000562; FN_type2_col-bd.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR013806; Kringle-like.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
PANTHER; PTHR10201:SF199; PTHR10201:SF199; 1.
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.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis;
Autocatalytic cleavage; Calcium; Collagen degradation;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Disulfide bond; Extracellular matrix; Glycoprotein;
Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion;
Nucleus; Phosphoprotein; Polymorphism; Protease; Reference proteome;
Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 29 {ECO:0000250|UniProtKB:P33436}.
PROPEP 30 109 Activation peptide.
/FTId=PRO_0000028714.
CHAIN 110 660 72 kDa type IV collagenase.
/FTId=PRO_0000028715.
CHAIN 445 660 PEX.
/FTId=PRO_0000391626.
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 472 516 Hemopexin 1.
REPEAT 517 563 Hemopexin 2.
REPEAT 565 613 Hemopexin 3.
REPEAT 614 660 Hemopexin 4.
REGION 110 221 Collagenase-like 1.
REGION 222 396 Collagen-binding.
REGION 397 465 Collagenase-like 2.
REGION 414 660 Required for inhibitor TIMP2 binding.
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 476 476 Calcium 4; via carbonyl oxygen.
METAL 521 521 Calcium 4; via carbonyl oxygen.
METAL 569 569 Calcium 4; via carbonyl oxygen.
METAL 618 618 Calcium 4; via carbonyl oxygen.
CARBOHYD 573 573 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 642 642 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 469 660 {ECO:0000255|PROSITE-ProRule:PRU00479,
ECO:0000269|PubMed:10545322}.
VAR_SEQ 1 76 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044631.
VAR_SEQ 1 51 MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDV
APKTDKELAV -> M (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045704.
VARIANT 101 101 R -> H (in MONA; dbSNP:rs121912953).
{ECO:0000269|PubMed:11431697}.
/FTId=VAR_032423.
VARIANT 210 210 D -> Y. {ECO:0000269|PubMed:11431697}.
/FTId=VAR_032424.
VARIANT 228 228 A -> T (in a colorectal cancer sample;
somatic mutation; dbSNP:rs759302357).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036136.
VARIANT 400 400 Missing (in MONA).
{ECO:0000269|PubMed:16542393}.
/FTId=VAR_054996.
VARIANT 404 404 E -> K (in MONA; dbSNP:rs121912955).
{ECO:0000269|PubMed:15691365}.
/FTId=VAR_032425.
VARIANT 447 447 A -> V (in dbSNP:rs17859943).
{ECO:0000269|Ref.4}.
/FTId=VAR_020616.
VARIANT 498 498 T -> M (in a colorectal cancer sample;
somatic mutation; dbSNP:rs764961297).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036137.
VARIANT 621 621 V -> L (in dbSNP:rs16955280).
{ECO:0000269|Ref.4}.
/FTId=VAR_020617.
VARIANT 644 644 S -> I (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036138.
CONFLICT 235 235 F -> S (in Ref. 3; AK310314).
{ECO:0000305}.
CONFLICT 546 546 S -> G (in Ref. 3; BAG35588).
{ECO:0000305}.
CONFLICT 618 618 D -> G (in Ref. 3; BAG35588).
{ECO:0000305}.
HELIX 46 56 {ECO:0000244|PDB:1EAK}.
TURN 62 64 {ECO:0000244|PDB:1CK7}.
HELIX 67 80 {ECO:0000244|PDB:1EAK}.
STRAND 86 88 {ECO:0000244|PDB:1GXD}.
HELIX 91 97 {ECO:0000244|PDB:1EAK}.
STRAND 111 113 {ECO:0000244|PDB:1CK7}.
STRAND 120 128 {ECO:0000244|PDB:3AYU}.
STRAND 133 135 {ECO:0000244|PDB:1HOV}.
HELIX 137 152 {ECO:0000244|PDB:3AYU}.
STRAND 154 156 {ECO:0000244|PDB:3AYU}.
STRAND 158 161 {ECO:0000244|PDB:3AYU}.
STRAND 163 165 {ECO:0000244|PDB:3AYU}.
STRAND 168 174 {ECO:0000244|PDB:3AYU}.
STRAND 179 181 {ECO:0000244|PDB:3AYU}.
STRAND 186 189 {ECO:0000244|PDB:3AYU}.
STRAND 192 195 {ECO:0000244|PDB:3AYU}.
STRAND 197 199 {ECO:0000244|PDB:3AYU}.
TURN 200 203 {ECO:0000244|PDB:3AYU}.
STRAND 205 208 {ECO:0000244|PDB:3AYU}.
STRAND 209 211 {ECO:0000244|PDB:1HOV}.
STRAND 213 216 {ECO:0000244|PDB:3AYU}.
HELIX 226 228 {ECO:0000244|PDB:1EAK}.
STRAND 235 239 {ECO:0000244|PDB:1EAK}.
STRAND 242 246 {ECO:0000244|PDB:1EAK}.
STRAND 258 264 {ECO:0000244|PDB:1EAK}.
TURN 265 267 {ECO:0000244|PDB:1EAK}.
STRAND 271 273 {ECO:0000244|PDB:1EAK}.
TURN 277 279 {ECO:0000244|PDB:1EAK}.
TURN 284 288 {ECO:0000244|PDB:1EAK}.
STRAND 293 297 {ECO:0000244|PDB:1EAK}.
STRAND 300 304 {ECO:0000244|PDB:1EAK}.
STRAND 316 321 {ECO:0000244|PDB:1EAK}.
TURN 323 325 {ECO:0000244|PDB:1EAK}.
STRAND 329 331 {ECO:0000244|PDB:1EAK}.
STRAND 338 341 {ECO:0000244|PDB:1GXD}.
TURN 342 346 {ECO:0000244|PDB:1EAK}.
STRAND 351 355 {ECO:0000244|PDB:1EAK}.
STRAND 358 362 {ECO:0000244|PDB:1EAK}.
STRAND 369 371 {ECO:0000244|PDB:1EAK}.
STRAND 374 379 {ECO:0000244|PDB:1EAK}.
HELIX 381 384 {ECO:0000244|PDB:1EAK}.
STRAND 387 389 {ECO:0000244|PDB:1EAK}.
STRAND 394 396 {ECO:0000244|PDB:3AYU}.
HELIX 397 408 {ECO:0000244|PDB:3AYU}.
STRAND 422 424 {ECO:0000244|PDB:3AYU}.
HELIX 435 445 {ECO:0000244|PDB:3AYU}.
TURN 468 470 {ECO:0000244|PDB:1GEN}.
STRAND 476 481 {ECO:0000244|PDB:1GEN}.
STRAND 484 489 {ECO:0000244|PDB:1GEN}.
STRAND 492 498 {ECO:0000244|PDB:1GEN}.
STRAND 504 508 {ECO:0000244|PDB:1GEN}.
HELIX 509 511 {ECO:0000244|PDB:1GEN}.
STRAND 514 516 {ECO:0000244|PDB:1GXD}.
STRAND 521 526 {ECO:0000244|PDB:1GEN}.
TURN 527 530 {ECO:0000244|PDB:1GEN}.
STRAND 531 536 {ECO:0000244|PDB:1GEN}.
STRAND 539 544 {ECO:0000244|PDB:1GEN}.
STRAND 553 555 {ECO:0000244|PDB:1GEN}.
HELIX 556 559 {ECO:0000244|PDB:1GEN}.
TURN 563 566 {ECO:0000244|PDB:1GXD}.
STRAND 569 573 {ECO:0000244|PDB:1GEN}.
TURN 575 577 {ECO:0000244|PDB:1GEN}.
STRAND 580 584 {ECO:0000244|PDB:1GEN}.
STRAND 587 592 {ECO:0000244|PDB:1GEN}.
TURN 593 596 {ECO:0000244|PDB:1GEN}.
HELIX 606 609 {ECO:0000244|PDB:1GEN}.
STRAND 610 612 {ECO:0000244|PDB:1GEN}.
STRAND 618 622 {ECO:0000244|PDB:1GEN}.
TURN 624 626 {ECO:0000244|PDB:1GEN}.
STRAND 628 633 {ECO:0000244|PDB:1GEN}.
STRAND 636 641 {ECO:0000244|PDB:1GEN}.
STRAND 644 652 {ECO:0000244|PDB:1GEN}.
HELIX 653 656 {ECO:0000244|PDB:1GEN}.
SEQUENCE 660 AA; 73882 MW; BC7147DC8B49F289 CRC64;
MEALMARGAL TGPLRALCLL GCLLSHAAAA PSPIIKFPGD VAPKTDKELA VQYLNTFYGC
PKESCNLFVL KDTLKKMQKF FGLPQTGDLD QNTIETMRKP RCGNPDVANY NFFPRKPKWD
KNQITYRIIG YTPDLDPETV DDAFARAFQV WSDVTPLRFS RIHDGEADIM INFGRWEHGD
GYPFDGKDGL LAHAFAPGTG VGGDSHFDDD ELWTLGEGQV VRVKYGNADG EYCKFPFLFN
GKEYNSCTDT GRSDGFLWCS TTYNFEKDGK YGFCPHEALF TMGGNAEGQP CKFPFRFQGT
SYDSCTTEGR TDGYRWCGTT EDYDRDKKYG FCPETAMSTV GGNSEGAPCV FPFTFLGNKY
ESCTSAGRSD GKMWCATTAN YDDDRKWGFC PDQGYSLFLV AAHEFGHAMG LEHSQDPGAL
MAPIYTYTKN FRLSQDDIKG IQELYGASPD IDLGTGPTPT LGPVTPEICK QDIVFDGIAQ
IRGEIFFFKD RFIWRTVTPR DKPMGPLLVA TFWPELPEKI DAVYEAPQEE KAVFFAGNEY
WIYSASTLER GYPKPLTSLG LPPDVQRVDA AFNWSKNKKT YIFAGDKFWR YNEVKKKMDP
GFPKLIADAW NAIPDNLDAV VDLQGGGHSY FFKGAYYLKL ENQSLKSVKF GSIKSDWLGC


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E0100m ELISA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Mouse,Mus musculus 96T
E0100m ELISA kit 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Mouse,Mus musculus 96T
E0100r ELISA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Rat,Rattus norvegicus 96T
E0100r ELISA kit 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Rat,Rattus norvegicus 96T
U0100m CLIA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Mouse,Mus musculus 96T
U0100r CLIA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Rat,Rattus norvegicus 96T
E0553r ELISA 92 kDa gelatinase,92 kDa type IV collagenase,Gelatinase B,GELB,Matrix metalloproteinase-9,Mmp9,MMP-9,Rat,Rattus norvegicus 96T
U0553r CLIA 92 kDa gelatinase,92 kDa type IV collagenase,Gelatinase B,GELB,Matrix metalloproteinase-9,Mmp9,MMP-9,Rat,Rattus norvegicus 96T
U0553b CLIA 92 kDa gelatinase,92 kDa type IV collagenase,Bos taurus,Bovine,Gelatinase B,GELB,Matrix metalloproteinase-9,MMP9,MMP-9 96T
U0100Rb CLIA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,MMP2,MMP-2,Oryctolagus cuniculus,Rabbit 96T
E0553b ELISA kit 92 kDa gelatinase,92 kDa type IV collagenase,Bos taurus,Bovine,Gelatinase B,GELB,Matrix metalloproteinase-9,MMP9,MMP-9 96T
E0100Rb ELISA kit 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,MMP2,MMP-2,Oryctolagus cuniculus,Rabbit 96T
E0100Rb ELISA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,MMP2,MMP-2,Oryctolagus cuniculus,Rabbit 96T
E0553r ELISA kit 92 kDa gelatinase,92 kDa type IV collagenase,Gelatinase B,GELB,Matrix metalloproteinase-9,Mmp9,MMP-9,Rat,Rattus norvegicus 96T
E0553b ELISA 92 kDa gelatinase,92 kDa type IV collagenase,Bos taurus,Bovine,Gelatinase B,GELB,Matrix metalloproteinase-9,MMP9,MMP-9 96T
U0100h CLIA 72 kDa gelatinase,72 kDa type IV collagenase,CLG4A,Gelatinase A,Homo sapiens,Human,Matrix metalloproteinase-2,MMP2,MMP-2,TBE-1 96T
E0100h ELISA kit 72 kDa gelatinase,72 kDa type IV collagenase,CLG4A,Gelatinase A,Homo sapiens,Human,Matrix metalloproteinase-2,MMP2,MMP-2,TBE-1 96T
E0100h ELISA 72 kDa gelatinase,72 kDa type IV collagenase,CLG4A,Gelatinase A,Homo sapiens,Human,Matrix metalloproteinase-2,MMP2,MMP-2,TBE-1 96T
E0553m ELISA kit 92 kDa gelatinase,92 kDa type IV collagenase,Clg4b,Gelatinase B,GELB,Matrix metalloproteinase-9,Mmp9,MMP-9,Mouse,Mus musculus 96T
E0553m ELISA 92 kDa gelatinase,92 kDa type IV collagenase,Clg4b,Gelatinase B,GELB,Matrix metalloproteinase-9,Mmp9,MMP-9,Mouse,Mus musculus 96T
E0553Rb ELISA kit 92 kDa gelatinase,92 kDa type IV collagenase,Gelatinase B,GELB,Matrix metalloproteinase-9,MMP9,MMP-9,Oryctolagus cuniculus,Rabbit 96T


 

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