[1]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2844164 [NCBI, ExPASy, EBI, Israel, Japan]
Muller D.,
Quantin B.,
Gesnel M.-C.,
Millon-Collard R.,
Abecassis J.,
Breathnach R.;
"The collagenase gene family in humans consists of at least four members.";
Biochem. J. 253:187-192(1988).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=1497627 [NCBI, ExPASy, EBI, Israel, Japan]
Marti H.P.,
McNeil L.,
Thomas G.,
Davies M.,
Lovett D.H.;
"Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1.";
Biochem. J. 285:899-905(1992).
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=8294454 [NCBI, ExPASy, EBI, Israel, Japan]
Gaire M.,
Magbanua Z.,
McDonnell S.,
McNeil L.B.,
Lovett D.H.,
Matrisian L.M.;
"Structure and expression of the human gene for the matrix metalloproteinase matrilysin.";
J. Biol. Chem. 269:2032-2040(1994).
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[4]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-77; ASP-137 AND LEU-241.
Livingston R.J.,
Rieder M.J.,
Chung M.-W.,
Ritchie T.K.,
Olson A.N.,
Nguyen C.P.,
Nguyen D.A.,
Poel C.L.,
Chambers S.W.,
Schackwitz W.S.,
Sherwood J.K.,
Sherwood A.M.,
Leithauser B.J.,
Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
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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[6]
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PROTEIN SEQUENCE OF 18-42.
PubMed=2253219 [NCBI, ExPASy, EBI, Israel, Japan]
Miyazaki K.,
Hattori Y.,
Umenishi F.,
Yasumitsu H.,
Umeda M.;
"Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line.";
Cancer Res. 50:7758-7764(1990).
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[7]
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FUNCTION.
DOI=10.1021/bi00439a004; PubMed=2550050 [NCBI, ExPASy, EBI, Israel, Japan]
Quantin B.,
Murphy G.,
Breathnach R.;
"Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members.";
Biochemistry 28:5327-5334(1989).
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[8]
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X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1021/bi00020a004; PubMed=7756291 [NCBI, ExPASy, EBI, Israel, Japan]
Browner M.F.,
Smith W.W.,
Castelhano A.L.;
"Matrilysin-inhibitor complexes: common themes among metalloproteases.";
Biochemistry 34:6602-6610(1995).
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- FUNCTION: Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.
- CATALYTIC ACTIVITY: Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha-2(I) > alpha-1(I).
- COFACTOR: Binds 2 calcium ions per subunit.
- COFACTOR: Binds 2 zinc ions per subunit.
- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (Probable).
- 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.
- SIMILARITY: Belongs to the peptidase M10A family [view classification].
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