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UniProtKB/Swiss-Prot entry P08254


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MMP3_HUMAN
Primary accession number P08254
Secondary accession numbers Q3B7S0 Q6GRF8
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on February 1, 1991 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 105)
Name and origin of the protein
Protein name Stromelysin-1 [Precursor]
Synonyms SL-1
EC 3.4.24.17
Matrix metalloproteinase-3
MMP-3
Transin-1
Gene name
Name: MMP3
Synonyms: STMY1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-24.
PubMed=3360803 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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], 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.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-45.
SeattleSNPs program for genomic applications;
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-45.
TISSUE=Lung;
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).
[8]
ZYMOGEN ACTIVATION.
DOI=10.1021/bi00476a020; PubMed=2383557 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
STRUCTURE BY NMR OF CATALYTIC DOMAIN.
DOI=10.1038/nsb0294-111; PubMed=7656014 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
STRUCTURE BY NMR OF 100-267.
PubMed=9827994 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-272.
PubMed=8535233 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-266.
DOI=10.1016/S0969-2126(96)00043-3; PubMed=8740360 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 105-264.
DOI=10.1021/jm960465t; PubMed=9083493 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 100-267 IN COMPLEX WITH TIMP1.
DOI=10.1038/37995; PubMed=9288970 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 100-264.
PubMed=9792098 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-272.
DOI=10.1006/jmbi.1999.3147; PubMed=10543949 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 100-267.
PubMed=10422833 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
STRUCTURE BY NMR OF 100-272.
DOI=10.1021/bi981328w; PubMed=9760240 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X05232; CAA28859.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03209; AAA36321.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U78045; AAB36942.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223283; BAD97003.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223291; BAD97011.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF405705; AAK95247.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069676; AAH69676.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069716; AAH69716.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC074815; AAH74815.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC074869; AAH74869.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105954; AAI05955.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC107490; AAI07491.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC107491; AAI07492.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28156; KCHUS1.
RefSeq NP_002413.1; -.
UniGene Hs.375129
3D structure databases
PDB
1B3D; X-ray; 2.30 A; A/B=100-272.[ExPASy / RCSB / EBI]
1B8Y; X-ray; 2.00 A; A=100-266.[ExPASy / RCSB / EBI]
1BIW; X-ray; 2.50 A; A/B=100-272.[ExPASy / RCSB / EBI]
1BM6; NMR; -; A=100-272.[ExPASy / RCSB / EBI]
1BQO; X-ray; 2.30 A; A/B=100-272.[ExPASy / RCSB / EBI]
1C3I; X-ray; 1.83 A; A/B=100-272.[ExPASy / RCSB / EBI]
1C8T; X-ray; 2.60 A; A/B=103-268.[ExPASy / RCSB / EBI]
1CAQ; X-ray; 1.80 A; A=100-267.[ExPASy / RCSB / EBI]
1CIZ; X-ray; 1.64 A; A=100-267.[ExPASy / RCSB / EBI]
1CQR; X-ray; 2.00 A; A/B=100-272.[ExPASy / RCSB / EBI]
1D5J; X-ray; 2.60 A; A/B=100-272.[ExPASy / RCSB / EBI]
1D7X; X-ray; 2.00 A; A/B=100-272.[ExPASy / RCSB / EBI]
1D8F; X-ray; 2.40 A; A/B=100-272.[ExPASy / RCSB / EBI]
1D8M; X-ray; 2.44 A; A/B=100-272.[ExPASy / RCSB / EBI]
1G05; X-ray; 2.45 A; A/B=100-272.[ExPASy / RCSB / EBI]
1G49; X-ray; 1.90 A; A/B=100-272.[ExPASy / RCSB / EBI]
1G4K; X-ray; 2.00 A; A/B/C=100-267.[ExPASy / RCSB / EBI]
1HFS; X-ray; 1.70 A; A=105-264.[ExPASy / RCSB / EBI]
1HY7; X-ray; 1.50 A; A/B=100-272.[ExPASy / RCSB / EBI]
1M1W; Model; -; A=100-268.[ExPASy / RCSB / EBI]
1OO9; NMR; -; A=100-267.[ExPASy / RCSB / EBI]
1QIA; X-ray; 2.00 A; A/B/C/D=106-267.[ExPASy / RCSB / EBI]
1QIC; X-ray; 2.00 A; A/B/C/D=106-266.[ExPASy / RCSB / EBI]
1SLM; X-ray; 1.90 A; A=18-272.[ExPASy / RCSB / EBI]
1SLN; X-ray; 2.27 A; A=100-272.[ExPASy / RCSB / EBI]
1UEA; X-ray; 2.80 A; A/C=100-272.[ExPASy / RCSB / EBI]
1UMS; NMR; -; A=100-273.[ExPASy / RCSB / EBI]
1UMT; NMR; -; A=100-273.[ExPASy / RCSB / EBI]
1USN; X-ray; 1.80 A; A=100-264.[ExPASy / RCSB / EBI]
2D1O; X-ray; 2.02 A; A/B=100-270.[ExPASy / RCSB / EBI]
2JNP; NMR; -; A=105-265.[ExPASy / RCSB / EBI]
2JT5; NMR; -; A=105-265.[ExPASy / RCSB / EBI]
2JT6; NMR; -; A=105-265.[ExPASy / RCSB / EBI]
2SRT; NMR; -; A=100-272.[ExPASy / RCSB / EBI]
2USN; X-ray; 2.20 A; A=100-264.[ExPASy / RCSB / EBI]
3USN; NMR; -; A=100-267.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1B3D; -.
1B8Y; -.
1BIW; -.
1BM6; -.
1BQO; -.
1C3I; -.
1C8T; -.
1CAQ; -.
1CIZ; -.
1CQR; -.
1D5J; -.
1D7X; -.
1D8F; -.
1D8M; -.
1G05; -.
1G49; -.
1G4K; -.
1HFS; -.
1HY7; -.
1M1W; -.
1OO9; -.
1QIA; -.
1QIC; -.
1SLM; -.
1SLN; -.
1UEA; -.
1UMS; -.
1UMT; -.
1USN; -.
2D1O; -.
2JNP; -.
2JT5; -.
2JT6; -.
2SRT; -.
2USN; -.
3USN; -.
ModBase P08254.
Protein family/group databases
MEROPS M10.005; -.
PTM databases
PhosphoSite P08254; -.
Organism-specific databases
H-InvDB HIX0035998; -.
HGNC HGNC:7173; MMP3.
GenAtlas MMP3.
HPA CAB016139; -.
HPA007875; -.
MIM 185250; gene+phenotype. [NCBI / EBI]
PharmGKB PA30886; -.
GeneCards P08254.
Gene expression databases
ArrayExpress P08254; -.
CleanEx HS_MMP3; -.
GermOnline ENSG00000149968; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0004248; Molecular function: stromelysin 1 activity (traceable author statement from ProtInc).
GO:0006508; Biological process: proteolysis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000585; Hemopexin.
IPR001818; Pept_M10A_M12B.
IPR016293; Pept_M10A_matrix.
IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR002477; Peptidoglycan-bd-like.
Graphical view of domain structure.
Gene3D G3DSA:2.110.10.10; Hemopexin; 1.
Pfam PF00045; Hemopexin; 4.
PF00413; Peptidase_M10; 1.
PF01471; PG_binding_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS PR00138; MATRIXIN.
SMART SM00120; HX; 4.
SM00235; ZnMc; 1.
SMART graphical view of domain structure.
PROSITE PS00546; CYSTEINE_SWITCH; 1.
PS00024; HEMOPEXIN; 1.
PS00142; ZINC_PROTEASE; 1.
BLOCKS P08254.
Genome annotation databases
Ensembl ENSG00000149968; Homo sapiens. [Contig view]
GeneID 4314; -.
KEGG hsa:4314; -.
Phylogenomic databases
HOGENOM P08254; -.
HOVERGEN P08254; -.
Other
DrugBank DB00786; Marimastat.
DB00641; Simvastatin.
LinkHub P08254; -.
SOURCE MMP3; Homo sapiens.
ProtoNet P08254.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Collagen degradation; Direct protein sequencing; Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; Repeat; Secreted; Signal; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    17  17     Probable. 
PROPEP   18    99  82     Activation peptide. PRO_0000028728
CHAIN   100   477  378     Stromelysin-1. PRO_0000028729
DOMAIN   296   338  43     Hemopexin-like 1. 
DOMAIN   340   383  44     Hemopexin-like 2. 
DOMAIN   388   435  48     Hemopexin-like 3. 
DOMAIN   437   477  41     Hemopexin-like 4. 
MOTIF   90    97  8     Cysteine switch (By similarity). 
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. 
METAL   222   222        Zinc 2; catalytic. 
METAL   228   228        Zinc 2; catalytic. 
METAL   297   297        Calcium 4; via carbonyl oxygen (By similarity). 
METAL   389   389        Calcium 4; via carbonyl oxygen (By similarity). 
METAL   438   438        Calcium 4; via carbonyl oxygen (By similarity). 
CARBOHYD   120   120        N-linked (GlcNAc...) (Potential). 
DISULFID   290   477        By similarity. 
VARIANT   45    45  1     K -> E (in dbSNP:rs679620 [NCBI]). VAR_013090 
CONFLICT   420   420        P -> L (in Ref. 3). 
HELIX   34    41  8      
HELIX   58    70  13      
HELIX   81    86  6      
STRAND   96    98  3      
STRAND   110   118  9      
HELIX   127   142  16      
STRAND   148   151  4      
STRAND   153   155  3      
STRAND   158   164  7      
STRAND   169   171  3      
STRAND   176   179  4      
STRAND   182   184  3      
STRAND   187   189  3      
TURN   190   193  4      
STRAND   195   198  4      
STRAND   203   206  4      
STRAND   209   211  3      
HELIX   212   224  13      
STRAND   246   248  3      
HELIX   253   263  11      
Sequence information
Length: 477 AA [This is the length of the unprocessed precursor] Molecular weight: 53977 Da [This is the MW of the unprocessed precursor] CRC64: 96194833B907668D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKSLPILLLL CVAVCSAYPL DGAARGEDTS MNLVQKYLEN YYDLKKDVKQ FVRRKDSGPV 

        70         80         90        100        110        120 
VKKIREMQKF LGLEVTGKLD SDTLEVMRKP RCGVPDVGHF RTFPGIPKWR KTHLTYRIVN 

       130        140        150        160        170        180 
YTPDLPKDAV DSAVEKALKV WEEVTPLTFS RLYEGEADIM ISFAVREHGD FYPFDGPGNV 

       190        200        210        220        230        240 
LAHAYAPGPG INGDAHFDDD EQWTKDTTGT NLFLVAAHEI GHSLGLFHSA NTEALMYPLY 

       250        260        270        280        290        300 
HSLTDLTRFR LSQDDINGIQ SLYGPPPDSP ETPLVPTEPV PPEPGTPANC DPALSFDAVS 

       310        320        330        340        350        360 
TLRGEILIFK DRHFWRKSLR KLEPELHLIS SFWPSLPSGV DAAYEVTSKD LVFIFKGNQF 

       370        380        390        400        410        420 
WAIRGNEVRA GYPRGIHTLG FPPTVRKIDA AISDKEKNKT YFFVEDKYWR FDEKRNSMEP 

       430        440        450        460        470 
GFPKQIAEDF PGIDSKIDAV FEEFGFFYFF TGSSQLEFDP NAKKVTHTLK SNSWLNC 

P08254 in FASTA format

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View entry in raw text format (no links)
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