[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 [LARGE SCALE MRNA].
Kalnine N.,
Chen X.,
Rolfs A.,
Halleck A.,
Hines L.,
Eisenstein S.,
Koundinya M.,
Raphael J.,
Moreira D.,
Kelley T.,
LaBaer J.,
Lin Y.,
Phelan M.,
Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-4; LYS-53; ARG-65; LEU-226; GLU-282; PHE-440 AND LEU-475.
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
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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[5]
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VARIANT [LARGE SCALE ANALYSIS] GLN-142.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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- FUNCTION: Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase.
- CATALYTIC ACTIVITY: Similar to stromelysin 1, but action on collagen types III, IV and V is weak.
- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
- COFACTOR: Calcium (By similarity).
- 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].
- SIMILARITY: Contains 4 hemopexin-like domains.
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