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Stromelysin-1 (SL-1) (EC 3.4.24.17) (Matrix metalloproteinase-3) (MMP-3) (Transin-1)

 MMP3_HUMAN              Reviewed;         477 AA.
P08254; B2R8B8; Q3B7S0; Q6GRF8;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
23-MAY-2018, entry version 203.
RecName: Full=Stromelysin-1;
Short=SL-1;
EC=3.4.24.17;
AltName: Full=Matrix metalloproteinase-3;
Short=MMP-3;
AltName: Full=Transin-1;
Flags: Precursor;
Name=MMP3; Synonyms=STMY1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-24.
PubMed=3360803;
Saus J., Quinones S., Otani Y., Nagase H., Harris E.D. Jr.,
Kurkinen M.;
"The complete primary structure of human matrix metalloproteinase-3.
Identity with stromelysin.";
J. Biol. Chem. 263:6742-6745(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=3030290; DOI=10.1042/bj2400913;
Whitham S.E., Murphy G., Angel P., Rahmsdorf H.J., Smith B., Lyons A.,
Harris T.J.R., Reynolds J.J., Herrlich P., Docherty A.J.P.;
"Comparison of human stromelysin and collagenase by cloning and
sequence analysis.";
Biochem. J. 240:913-916(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3477804; DOI=10.1073/pnas.84.19.6725;
Wilhelm S.M., Collier I.E., Kronberger A., Eisen A.Z., Marmer B.L.,
Grant G.A., Bauer E.A., Goldberg G.I.;
"Human skin fibroblast stromelysin: structure, glycosylation,
substrate specificity, and differential expression in normal and
tumorigenic cells.";
Proc. Natl. Acad. Sci. U.S.A. 84:6725-6729(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lin D., Duncan M., Allen E., Araujo R., Aparicio A., Chai A.,
Chung E., Davis K., Federspiel N., Hyman R., Kalman S., Komp C.,
Kurdi O., Lashkari D., Lew H., Namath A., Oefner P., Roberts D.,
Heller R., Davis R.W.;
"Three matrix metalloproteinases on 81kb of P1 insert.";
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Synovium;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-45.
TISSUE=Synovium;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-45.
SeattleSNPs variation discovery resource;
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-45.
TISSUE=Lung;
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).
[10]
ZYMOGEN ACTIVATION.
PubMed=2383557; DOI=10.1021/bi00476a020;
Nagase H., Enghild J.J., Suzuki K., Salvesen G.;
"Stepwise activation mechanisms of the precursor of matrix
metalloproteinase 3 (stromelysin) by proteinases and (4-
aminophenyl)mercuric acetate.";
Biochemistry 29:5783-5789(1990).
[11]
INVOLVEMENT IN CHDS6.
PubMed=8662692; DOI=10.1074/jbc.271.22.13244;
Ye S., Eriksson P., Hamsten A., Kurkinen M., Humphries S.E.,
Henney A.M.;
"Progression of coronary atherosclerosis is associated with a common
genetic variant of the human stromelysin-1 promoter which results in
reduced gene expression.";
J. Biol. Chem. 271:13055-13060(1996).
[12]
INVOLVEMENT IN CHDS6.
PubMed=12477941; DOI=10.1056/NEJMoa021445;
Yamada Y., Izawa H., Ichihara S., Takatsu F., Ishihara H.,
Hirayama H., Sone T., Tanaka M., Yokota M.;
"Prediction of the risk of myocardial infarction from polymorphisms in
candidate genes.";
N. Engl. J. Med. 347:1916-1923(2002).
[13]
STRUCTURE BY NMR OF CATALYTIC DOMAIN.
PubMed=7656014; DOI=10.1038/nsb0294-111;
Gooley P.R., O'Connell J.F., Marcy A.I., Cuca G.C., Salowe S.P.,
Bush B.L., Hermes J.D., Esser C.K., Hagmann W.K., Springer J.P.,
Johnson B.A.;
"The NMR structure of the inhibited catalytic domain of human
stromelysin-1.";
Nat. Struct. Biol. 1:111-118(1994).
[14]
STRUCTURE BY NMR OF 100-267.
PubMed=9827994; DOI=10.1002/pro.5560071105;
Stockman B.J., Waldon D.J., Gates J.A., Scahill T.A.,
Kloosterman D.A., Mizsak S.A., Jacobsen E.J., Belonga K.L.,
Mitchell M.A., Mao B., Petke J.D., Goodman L., Powers E.A.,
Ledbetter S.R., Kaytes P.S., Vogeli G., Marshall V.P., Petzold G.L.,
Poorman R.A.;
"Solution structures of stromelysin complexed to thiadiazole
inhibitors.";
Protein Sci. 7:2281-2286(1998).
[15]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-272.
PubMed=8535233; DOI=10.1002/pro.5560041002;
Becker J.W., Marcy A.I., Rokosz L.L., Axel M.G., Burbaum J.J.,
Fitzgerald P.M.D., Cameron P.M., Esser C.K., Hagmann W.K.,
Hermes J.D., Springer J.P.;
"Stromelysin-1: three-dimensional structure of the inhibited catalytic
domain and of the C-truncated proenzyme.";
Protein Sci. 4:1966-1976(1995).
[16]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-266.
PubMed=8740360; DOI=10.1016/S0969-2126(96)00043-3;
Dhanaraj V., Ye Q.-Z., Johnson L.L., Hupe D.J., Otwine D.F.,
Dunbar J.B. Jr., Rubin J.R., Pavlovsky A., Humblet C., Blundell T.L.;
"X-ray structure of a hydroxamate inhibitor complex of stromelysin
catalytic domain and its comparison with members of the zinc
metalloproteinase superfamily.";
Structure 4:375-386(1996).
[17]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 105-264.
PubMed=9083493; DOI=10.1021/jm960465t;
Esser C.K., Bugianesi R.L., Caldwell C.G., Chapman K.T., Durette P.L.,
Girotra N.N., Kopka I.E., Lanza T.J., Levorse D.A., Maccoss M.,
Owens K.A., Ponpipom M.M., Simeone J.P., Harrison R.K.,
Niedzwiecki L., Becker J.W., Marcy A.I., Axel M.G., Christen A.J.,
McDonnell J., Moore V.L., Olszewski J.M., Saphos C., Visco D.M.,
Shen F., Colletti A., Kriter P.A., Hagmann W.K.;
"Inhibition of stromelysin-1 (MMP-3) by P1'-biphenylylethyl
carboxyalkyl dipeptides.";
J. Med. Chem. 40:1026-1040(1997).
[18]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 100-267 IN COMPLEX WITH
TIMP1.
PubMed=9288970; DOI=10.1038/37995;
Gomis-Rueth F.-X., Maskos K., Betz M., Bergner A., Huber R.,
Suzuki K., Yoshida N., Nagase H., Brew K., Bourenkov G.P.,
Bartunik H., Bode W.;
"Mechanism of inhibition of the human matrix metalloproteinase
stromelysin-1 by TIMP-1.";
Nature 389:77-81(1997).
[19]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 100-264.
PubMed=9792098; DOI=10.1002/pro.5560071008;
Finzel B.C., Baldwin E.T., Bryant G.L. Jr., Hess G.F., Wilks J.W.,
Trepod C.M., Mott J.E., Marshall V.P., Petzold G.L., Poorman R.A.,
O'Sullivan T.J., Schostarez H.J., Mitchell M.A.;
"Structural characterizations of nonpeptidic thiadiazole inhibitors of
matrix metalloproteinases reveal the basis for stromelysin
selectivity.";
Protein Sci. 7:2118-2126(1998).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-272.
PubMed=10543949; DOI=10.1006/jmbi.1999.3147;
Chen L., Rydel T.J., Gu F., Dunaway C.M., Pikul S., Dunham K.M.,
Barnett B.L.;
"Crystal structure of the stromelysin catalytic domain at 2.0-A
resolution: inhibitor-induced conformational changes.";
J. Mol. Biol. 293:545-557(1999).
[21]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 100-267.
PubMed=10422833; DOI=10.1110/ps.8.7.1455;
Pavlovsky A.G., Williams M.G., Ye Q.-Z., Ortwine D.F.,
Purchase C.F. II, White A.D., Dhanaraj V., Roth B.D., Johnson L.L.,
Hupe D., Humblet C., Blundell T.L.;
"X-ray structure of human stromelysin catalytic domain complexed with
nonpeptide inhibitors: implications for inhibitor selectivity.";
Protein Sci. 8:1455-1462(1999).
[22]
STRUCTURE BY NMR OF 100-272.
PubMed=9760240; DOI=10.1021/bi981328w;
Li Y.C., Zhang X., Melton R., Ganu V., Gonnella N.C.;
"Solution structure of the catalytic domain of human stromelysin-1
complexed to a potent, nonpeptidic inhibitor.";
Biochemistry 37:14048-14056(1998).
-!- FUNCTION: Can degrade fibronectin, laminin, gelatins of type I,
III, IV, and V; collagens III, IV, X, and IX, and cartilage
proteoglycans. Activates procollagenase.
-!- CATALYTIC ACTIVITY: Preferential cleavage where P1', P2' and P3'
are hydrophobic residues.
-!- 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.;
-!- INTERACTION:
P50222:MEOX2; NbExp=3; IntAct=EBI-6957351, EBI-748397;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000305}.
-!- 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.
-!- DISEASE: Coronary heart disease 6 (CHDS6) [MIM:614466]: A
multifactorial disease characterized by an imbalance between
myocardial functional requirements and the capacity of the
coronary vessels to supply sufficient blood flow. Decreased
capacity of the coronary vessels is often associated with
thickening and loss of elasticity of the coronary arteries.
{ECO:0000269|PubMed:12477941, ECO:0000269|PubMed:8662692}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry. A polymorphism in
the MMP3 promoter region is associated with the risk of coronary
heart disease and myocardial infarction, due to lower MMP3
proteolytic activity and higher extracellular matrix deposition in
atherosclerotic lesions.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/mmp3/";
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EMBL; X05232; CAA28859.1; -; mRNA.
EMBL; J03209; AAA36321.1; -; mRNA.
EMBL; U78045; AAB36942.1; -; Genomic_DNA.
EMBL; AK223283; BAD97003.1; -; mRNA.
EMBL; AK223291; BAD97011.1; -; mRNA.
EMBL; AK313310; BAG36115.1; -; mRNA.
EMBL; AF405705; AAK95247.1; -; Genomic_DNA.
EMBL; CH471065; EAW67032.1; -; Genomic_DNA.
EMBL; BC069676; AAH69676.1; -; mRNA.
EMBL; BC069716; AAH69716.1; -; mRNA.
EMBL; BC074815; AAH74815.1; -; mRNA.
EMBL; BC074869; AAH74869.1; -; mRNA.
EMBL; BC105954; AAI05955.1; -; mRNA.
EMBL; BC107490; AAI07491.1; -; mRNA.
EMBL; BC107491; AAI07492.1; -; mRNA.
CCDS; CCDS8323.1; -.
PIR; A28156; KCHUS1.
RefSeq; NP_002413.1; NM_002422.4.
UniGene; Hs.375129; -.
PDB; 1B3D; X-ray; 2.30 A; A/B=100-272.
PDB; 1B8Y; X-ray; 2.00 A; A=100-266.
PDB; 1BIW; X-ray; 2.50 A; A/B=100-272.
PDB; 1BM6; NMR; -; A=100-272.
PDB; 1BQO; X-ray; 2.30 A; A/B=100-272.
PDB; 1C3I; X-ray; 1.83 A; A/B=100-272.
PDB; 1C8T; X-ray; 2.60 A; A/B=103-268.
PDB; 1CAQ; X-ray; 1.80 A; A=100-267.
PDB; 1CIZ; X-ray; 1.64 A; A=100-267.
PDB; 1CQR; X-ray; 2.00 A; A/B=100-272.
PDB; 1D5J; X-ray; 2.60 A; A/B=100-272.
PDB; 1D7X; X-ray; 2.00 A; A/B=100-272.
PDB; 1D8F; X-ray; 2.40 A; A/B=100-272.
PDB; 1D8M; X-ray; 2.44 A; A/B=100-272.
PDB; 1G05; X-ray; 2.45 A; A/B=100-272.
PDB; 1G49; X-ray; 1.90 A; A/B=100-272.
PDB; 1G4K; X-ray; 2.00 A; A/B/C=100-267.
PDB; 1HFS; X-ray; 1.70 A; A=105-264.
PDB; 1HY7; X-ray; 1.50 A; A/B=100-272.
PDB; 1M1W; Model; -; A=100-268.
PDB; 1OO9; NMR; -; A=100-267.
PDB; 1QIA; X-ray; 2.00 A; A/B/C/D=106-267.
PDB; 1QIC; X-ray; 2.00 A; A/B/C/D=106-266.
PDB; 1SLM; X-ray; 1.90 A; A=18-272.
PDB; 1SLN; X-ray; 2.27 A; A=100-272.
PDB; 1UEA; X-ray; 2.80 A; A/C=100-272.
PDB; 1UMS; NMR; -; A=100-273.
PDB; 1UMT; NMR; -; A=100-273.
PDB; 1USN; X-ray; 1.80 A; A=100-264.
PDB; 2D1O; X-ray; 2.02 A; A/B=100-270.
PDB; 2JNP; NMR; -; A=105-265.
PDB; 2JT5; NMR; -; A=105-265.
PDB; 2JT6; NMR; -; A=105-265.
PDB; 2SRT; NMR; -; A=100-272.
PDB; 2USN; X-ray; 2.20 A; A=100-264.
PDB; 3OHL; X-ray; 2.36 A; A=100-266.
PDB; 3OHO; X-ray; 2.50 A; A=100-268.
PDB; 3USN; NMR; -; A=100-267.
PDB; 4DPE; X-ray; 1.96 A; A/B=100-272.
PDB; 4G9L; X-ray; 1.88 A; A/B=100-272.
PDB; 4JA1; X-ray; 1.96 A; A/B=100-272.
PDBsum; 1B3D; -.
PDBsum; 1B8Y; -.
PDBsum; 1BIW; -.
PDBsum; 1BM6; -.
PDBsum; 1BQO; -.
PDBsum; 1C3I; -.
PDBsum; 1C8T; -.
PDBsum; 1CAQ; -.
PDBsum; 1CIZ; -.
PDBsum; 1CQR; -.
PDBsum; 1D5J; -.
PDBsum; 1D7X; -.
PDBsum; 1D8F; -.
PDBsum; 1D8M; -.
PDBsum; 1G05; -.
PDBsum; 1G49; -.
PDBsum; 1G4K; -.
PDBsum; 1HFS; -.
PDBsum; 1HY7; -.
PDBsum; 1M1W; -.
PDBsum; 1OO9; -.
PDBsum; 1QIA; -.
PDBsum; 1QIC; -.
PDBsum; 1SLM; -.
PDBsum; 1SLN; -.
PDBsum; 1UEA; -.
PDBsum; 1UMS; -.
PDBsum; 1UMT; -.
PDBsum; 1USN; -.
PDBsum; 2D1O; -.
PDBsum; 2JNP; -.
PDBsum; 2JT5; -.
PDBsum; 2JT6; -.
PDBsum; 2SRT; -.
PDBsum; 2USN; -.
PDBsum; 3OHL; -.
PDBsum; 3OHO; -.
PDBsum; 3USN; -.
PDBsum; 4DPE; -.
PDBsum; 4G9L; -.
PDBsum; 4JA1; -.
ProteinModelPortal; P08254; -.
SMR; P08254; -.
BioGrid; 110458; 15.
IntAct; P08254; 1.
MINT; P08254; -.
STRING; 9606.ENSP00000299855; -.
BindingDB; P08254; -.
ChEMBL; CHEMBL283; -.
DrugBank; DB02367; (1n)-4-N-Butoxyphenylsulfonyl-(2r)-N-Hydroxycarboxamido-(4s)-Methanesulfonylamino-Pyrrolidine.
DrugBank; DB04140; 1-Benzyl-3-(4-Methoxy-Benzenesulfonyl)-6-Oxo-Hexahydro-Pyrimidine-4-Carboxylic Acid Hydroxyamide.
DrugBank; DB03033; 1-Methyloxy-4-Sulfone-Benzene.
DrugBank; DB08643; 2-(2-{2-[(BIPHENYL-4-YLMETHYL)-AMINO]-3-MERCAPTO-PENTANOYLAMINO}-ACETYLAMINO)-3-METHYL-BUTYRIC ACID METHYL ESTER.
DrugBank; DB02449; 3-(1h-Indol-3-Yl)-2-[4-(4-Phenyl-Piperidin-1-Yl)-Benzenesulfonylamino]-Propionic Acid.
DrugBank; DB08030; 3-[(4'-cyanobiphenyl-4-yl)oxy]-N-hydroxypropanamide.
DrugBank; DB01996; 3-Methylpyridine.
DrugBank; DB07986; [4-(4-PHENYL-PIPERIDIN-1-YL)-BENZENESULFONYLAMINO]-ACETIC ACID.
DrugBank; DB02090; A Disubstituted Succinyl Caprolactam Hydroxymate Mmp3inhibitor.
DrugBank; DB02697; Hydroxyaminovaline.
DrugBank; DB00786; Marimastat.
DrugBank; DB08507; N-[[2-METHYL-4-HYDROXYCARBAMOYL]BUT-4-YL-N]-BENZYL-P-[PHENYL]-P-[METHYL]PHOSPHINAMID.
DrugBank; DB04232; N-Hydroxy-1-(4-Methoxyphenyl)Sulfonyl-4-Benzyloxycarbonyl-Piperazine-2-Carboxamide.
DrugBank; DB08271; N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID.
DrugBank; DB08029; N~2~-(biphenyl-4-ylsulfonyl)-N-hydroxy-N~2~-(2-hydroxyethyl)glycinamide.
GuidetoPHARMACOLOGY; 1630; -.
MEROPS; M10.005; -.
iPTMnet; P08254; -.
PhosphoSitePlus; P08254; -.
BioMuta; MMP3; -.
DMDM; 116857; -.
EPD; P08254; -.
PaxDb; P08254; -.
PeptideAtlas; P08254; -.
PRIDE; P08254; -.
DNASU; 4314; -.
Ensembl; ENST00000299855; ENSP00000299855; ENSG00000149968.
GeneID; 4314; -.
KEGG; hsa:4314; -.
UCSC; uc001phj.2; human.
CTD; 4314; -.
DisGeNET; 4314; -.
EuPathDB; HostDB:ENSG00000149968.11; -.
GeneCards; MMP3; -.
HGNC; HGNC:7173; MMP3.
HPA; HPA007875; -.
MalaCards; MMP3; -.
MIM; 185250; gene.
MIM; 614466; phenotype.
neXtProt; NX_P08254; -.
OpenTargets; ENSG00000149968; -.
PharmGKB; PA30886; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; P08254; -.
KO; K01394; -.
OMA; VAVCSAY; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; P08254; -.
TreeFam; TF315428; -.
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-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-2179392; EGFR Transactivation by Gastrin.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SIGNOR; P08254; -.
ChiTaRS; MMP3; human.
EvolutionaryTrace; P08254; -.
GeneWiki; MMP3; -.
GenomeRNAi; 4314; -.
PMAP-CutDB; P08254; -.
PRO; PR:P08254; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149968; -.
CleanEx; HS_MMP3; -.
ExpressionAtlas; P08254; baseline and differential.
Genevisible; P08254; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0004175; F:endopeptidase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0071732; P:cellular response to nitric oxide; TAS:ParkinsonsUK-UCL.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0010727; P:negative regulation of hydrogen peroxide metabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:1903209; P:positive regulation of oxidative stress-induced cell death; ISS:ParkinsonsUK-UCL.
GO; GO:0032461; P:positive regulation of protein oligomerization; IDA:ParkinsonsUK-UCL.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
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.
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; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Calcium; Collagen degradation; Complete proteome;
Direct protein sequencing; Disulfide bond; Extracellular matrix;
Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Polymorphism;
Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 17 {ECO:0000305|PubMed:3360803}.
PROPEP 18 99 Activation peptide.
/FTId=PRO_0000028728.
CHAIN 100 477 Stromelysin-1.
/FTId=PRO_0000028729.
REPEAT 287 336 Hemopexin 1.
REPEAT 337 383 Hemopexin 2.
REPEAT 385 433 Hemopexin 3.
REPEAT 434 477 Hemopexin 4.
MOTIF 90 97 Cysteine switch. {ECO:0000250}.
ACT_SITE 219 219
METAL 92 92 Zinc 2; in inhibited form.
METAL 124 124 Calcium 1.
METAL 158 158 Calcium 2.
METAL 168 168 Zinc 1.
METAL 170 170 Zinc 1.
METAL 175 175 Calcium 3.
METAL 176 176 Calcium 3; via carbonyl oxygen.
METAL 178 178 Calcium 3; via carbonyl oxygen.
METAL 180 180 Calcium 3; via carbonyl oxygen.
METAL 183 183 Zinc 1.
METAL 190 190 Calcium 2; via carbonyl oxygen.
METAL 192 192 Calcium 2; via carbonyl oxygen.
METAL 194 194 Calcium 2.
METAL 196 196 Zinc 1.
METAL 198 198 Calcium 3.
METAL 199 199 Calcium 1.
METAL 201 201 Calcium 1.
METAL 201 201 Calcium 3.
METAL 218 218 Zinc 2; catalytic.
{ECO:0000269|PubMed:8740360}.
METAL 222 222 Zinc 2; catalytic.
{ECO:0000269|PubMed:8740360}.
METAL 228 228 Zinc 2; catalytic.
{ECO:0000269|PubMed:8740360}.
METAL 297 297 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 389 389 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 438 438 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 290 477 {ECO:0000250}.
VARIANT 45 45 K -> E (in dbSNP:rs679620).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.6, ECO:0000269|Ref.7}.
/FTId=VAR_013090.
CONFLICT 420 420 P -> L (in Ref. 3). {ECO:0000305}.
HELIX 34 41 {ECO:0000244|PDB:1SLM}.
HELIX 58 70 {ECO:0000244|PDB:1SLM}.
HELIX 81 86 {ECO:0000244|PDB:1SLM}.
STRAND 96 98 {ECO:0000244|PDB:1SLM}.
STRAND 102 104 {ECO:0000244|PDB:1UEA}.
STRAND 110 118 {ECO:0000244|PDB:1HY7}.
STRAND 123 125 {ECO:0000244|PDB:1CAQ}.
HELIX 127 142 {ECO:0000244|PDB:1HY7}.
STRAND 144 146 {ECO:0000244|PDB:2SRT}.
STRAND 148 151 {ECO:0000244|PDB:1HY7}.
STRAND 153 155 {ECO:0000244|PDB:1HY7}.
STRAND 158 164 {ECO:0000244|PDB:1HY7}.
STRAND 169 171 {ECO:0000244|PDB:1HY7}.
STRAND 176 179 {ECO:0000244|PDB:1HY7}.
STRAND 182 184 {ECO:0000244|PDB:1HY7}.
STRAND 187 189 {ECO:0000244|PDB:1HY7}.
TURN 190 193 {ECO:0000244|PDB:1HY7}.
STRAND 195 198 {ECO:0000244|PDB:1HY7}.
STRAND 199 201 {ECO:0000244|PDB:2SRT}.
STRAND 203 211 {ECO:0000244|PDB:1HY7}.
HELIX 212 223 {ECO:0000244|PDB:1HY7}.
STRAND 232 234 {ECO:0000244|PDB:4JA1}.
STRAND 237 239 {ECO:0000244|PDB:1SLM}.
HELIX 240 243 {ECO:0000244|PDB:1USN}.
HELIX 246 248 {ECO:0000244|PDB:1CIZ}.
HELIX 253 263 {ECO:0000244|PDB:1HY7}.
SEQUENCE 477 AA; 53977 MW; 96194833B907668D CRC64;
MKSLPILLLL CVAVCSAYPL DGAARGEDTS MNLVQKYLEN YYDLKKDVKQ FVRRKDSGPV
VKKIREMQKF LGLEVTGKLD SDTLEVMRKP RCGVPDVGHF RTFPGIPKWR KTHLTYRIVN
YTPDLPKDAV DSAVEKALKV WEEVTPLTFS RLYEGEADIM ISFAVREHGD FYPFDGPGNV
LAHAYAPGPG INGDAHFDDD EQWTKDTTGT NLFLVAAHEI GHSLGLFHSA NTEALMYPLY
HSLTDLTRFR LSQDDINGIQ SLYGPPPDSP ETPLVPTEPV PPEPGTPANC DPALSFDAVS
TLRGEILIFK DRHFWRKSLR KLEPELHLIS SFWPSLPSGV DAAYEVTSKD LVFIFKGNQF
WAIRGNEVRA GYPRGIHTLG FPPTVRKIDA AISDKEKNKT YFFVEDKYWR FDEKRNSMEP
GFPKQIAEDF PGIDSKIDAV FEEFGFFYFF TGSSQLEFDP NAKKVTHTLK SNSWLNC


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