[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Placenta;
DOI=10.1074/jbc.270.39.23013; PubMed=7559440 [NCBI, ExPASy, EBI, Israel, Japan]
Takino T.,
Sato H.,
Shinagawa A.,
Seiki M.;
"Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family.";
J. Biol. Chem. 270:23013-23020(1995).
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[2]
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SEQUENCE REVISION.
Seiki M.;
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
TISSUE=Ovary;
DOI=10.1016/S0167-4781(97)00120-6; PubMed=9396633 [NCBI, ExPASy, EBI, Israel, Japan]
Matsumoto S.,
Katoh M.,
Saito S.,
Watanabe T.,
Masuho Y.;
"Identification of soluble type of membrane-type matrix metalloproteinase-3 formed by alternatively spliced mRNA.";
Biochim. Biophys. Acta 1354:159-170(1997).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Fetal brain;
DOI=10.1074/jbc.272.15.9749; PubMed=9092507 [NCBI, ExPASy, EBI, Israel, Japan]
Shofuda K.,
Yasumitsu H.,
Nishihashi A.,
Miki K.,
Miyazaki K.;
"Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain.";
J. Biol. Chem. 272:9749-9754(1997).
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[5]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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[6]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[7]
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INTERACTION WITH CSPG4, SUBCELLULAR LOCATION, AND FUNCTION.
DOI=10.1074/jbc.M010053200; PubMed=11278606 [NCBI, ExPASy, EBI, Israel, Japan]
Iida J.,
Pei D.,
Kang T.,
Simpson M.A.,
Herlyn M.,
Furcht L.T.,
McCarthy J.B.;
"Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen.";
J. Biol. Chem. 276:18786-18794(2001).
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[8]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K.,
Guo A.,
Zeng Q.,
Possemato A.,
Yu J.,
Haack H.,
Nardone J.,
Lee K.,
Reeves C.,
Li Y.,
Hu Y.,
Tan Z.,
Stokes M.,
Sullivan L.,
Mitchell J.,
Wetzel R.,
Macneill J.,
Ren J.M.,
Yuan J., ![]()
Bakalarski C.E.,
Villen J.,
Kornhauser J.M.,
Smith B.,
Li D.,
Zhou X.,
Gygi S.P.,
Gu T.-L.,
Polakiewicz R.D.,
Rush J.,
Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
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- FUNCTION: Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. The short isoform cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.
- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
- COFACTOR: Calcium (By similarity).
- ENZYME REGULATION: TIMP-2 shows little inhibitory activity compared to TIMP-1. TIMP-1 seems to have less binding affinity than TIMP-2 for the short isoform.
- SUBUNIT: Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan.
- SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Single-pass type I membrane protein; Extracellular side (Potential). Note=Localized at the cell surface of melanoma cells.
- SUBCELLULAR LOCATION: Isoform Short: Secreted, extracellular space, extracellular matrix. Cell surface. Note=Localized at the cell surface of melanoma cells.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, ovary and small intestine. The short isoform is found in the ovary.
- DEVELOPMENTAL STAGE: Expressed in tissues undergoing reconstruction. Present in fetal tissues, especially in brain. Expression seems to decline with advanced development.
- 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: The precursor is cleaved by a furin endopeptidase (By similarity).
- SIMILARITY: Belongs to the peptidase M10A family [view classification].
- SIMILARITY: Contains 4 hemopexin-like domains.
- WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mmp16/";.
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