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P08254

- MMP3_HUMAN

UniProt

P08254 - MMP3_HUMAN

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Protein
Stromelysin-1
Gene
MMP3, STMY1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.

Catalytic activityi

Preferential cleavage where P1', P2' and P3' are hydrophobic residues.

Cofactori

Binds 4 calcium ions per subunit.
Binds 2 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Zinc 2; in inhibited form
Metal bindingi124 – 1241Calcium 1
Metal bindingi158 – 1581Calcium 2
Metal bindingi168 – 1681Zinc 1
Metal bindingi170 – 1701Zinc 1
Metal bindingi175 – 1751Calcium 3
Metal bindingi176 – 1761Calcium 3; via carbonyl oxygen
Metal bindingi178 – 1781Calcium 3; via carbonyl oxygen
Metal bindingi180 – 1801Calcium 3; via carbonyl oxygen
Metal bindingi183 – 1831Zinc 1
Metal bindingi190 – 1901Calcium 2; via carbonyl oxygen
Metal bindingi192 – 1921Calcium 2; via carbonyl oxygen
Metal bindingi194 – 1941Calcium 2
Metal bindingi196 – 1961Zinc 1
Metal bindingi198 – 1981Calcium 3
Metal bindingi199 – 1991Calcium 1
Metal bindingi201 – 2011Calcium 1
Metal bindingi201 – 2011Calcium 3
Metal bindingi218 – 2181Zinc 2; catalytic1 Publication
Active sitei219 – 2191
Metal bindingi222 – 2221Zinc 2; catalytic1 Publication
Metal bindingi228 – 2281Zinc 2; catalytic1 Publication
Metal bindingi297 – 2971Calcium 4; via carbonyl oxygen By similarity
Metal bindingi389 – 3891Calcium 4; via carbonyl oxygen By similarity
Metal bindingi438 – 4381Calcium 4; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: ProtInc
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular response to amino acid stimulus Source: Ensembl
  2. collagen catabolic process Source: Reactome
  3. extracellular matrix disassembly Source: Reactome
  4. extracellular matrix organization Source: Reactome
  5. proteolysis Source: ProtInc
  6. regulation of cell migration Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_121096. EGFR Transactivation by Gastrin.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
REACT_222620. Collagen degradation.

Protein family/group databases

MEROPSiM10.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Stromelysin-1 (EC:3.4.24.17)
Short name:
SL-1
Alternative name(s):
Matrix metalloproteinase-3
Short name:
MMP-3
Transin-1
Gene namesi
Name:MMP3
Synonyms:STMY1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:7173. MMP3.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: ProtInc
  3. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

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.
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.2 Publications

Organism-specific databases

MIMi614466. phenotype.
PharmGKBiPA30886.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Inferred
Add
BLAST
Propeptidei18 – 9982Activation peptide
PRO_0000028728Add
BLAST
Chaini100 – 477378Stromelysin-1
PRO_0000028729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi120 – 1201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi290 ↔ 477 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP08254.
PRIDEiP08254.

PTM databases

PhosphoSiteiP08254.

Miscellaneous databases

PMAP-CutDBP08254.

Expressioni

Gene expression databases

ArrayExpressiP08254.
BgeeiP08254.
CleanExiHS_MMP3.
GenevestigatoriP08254.

Organism-specific databases

HPAiCAB016139.
HPA007875.

Interactioni

Protein-protein interaction databases

BioGridi110458. 3 interactions.
MINTiMINT-269333.
STRINGi9606.ENSP00000299855.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 418
Helixi58 – 7013
Helixi81 – 866
Beta strandi96 – 983
Beta strandi102 – 1043
Beta strandi110 – 1189
Beta strandi123 – 1253
Helixi127 – 14216
Beta strandi144 – 1463
Beta strandi148 – 1514
Beta strandi153 – 1553
Beta strandi158 – 1647
Beta strandi169 – 1713
Beta strandi176 – 1794
Beta strandi182 – 1843
Beta strandi187 – 1893
Turni190 – 1934
Beta strandi195 – 1984
Beta strandi199 – 2013
Beta strandi203 – 2119
Helixi212 – 22312
Beta strandi232 – 2343
Beta strandi237 – 2393
Helixi240 – 2434
Helixi246 – 2483
Helixi253 – 26311

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B3DX-ray2.30A/B100-272[»]
1B8YX-ray2.00A100-266[»]
1BIWX-ray2.50A/B100-272[»]
1BM6NMR-A100-272[»]
1BQOX-ray2.30A/B100-272[»]
1C3IX-ray1.83A/B100-272[»]
1C8TX-ray2.60A/B103-268[»]
1CAQX-ray1.80A100-267[»]
1CIZX-ray1.64A100-267[»]
1CQRX-ray2.00A/B100-272[»]
1D5JX-ray2.60A/B100-272[»]
1D7XX-ray2.00A/B100-272[»]
1D8FX-ray2.40A/B100-272[»]
1D8MX-ray2.44A/B100-272[»]
1G05X-ray2.45A/B100-272[»]
1G49X-ray1.90A/B100-272[»]
1G4KX-ray2.00A/B/C100-267[»]
1HFSX-ray1.70A105-264[»]
1HY7X-ray1.50A/B100-272[»]
1M1Wmodel-A100-268[»]
1OO9NMR-A100-267[»]
1QIAX-ray2.00A/B/C/D106-267[»]
1QICX-ray2.00A/B/C/D106-266[»]
1SLMX-ray1.90A18-272[»]
1SLNX-ray2.27A100-272[»]
1UEAX-ray2.80A/C100-272[»]
1UMSNMR-A100-273[»]
1UMTNMR-A100-273[»]
1USNX-ray1.80A100-264[»]
2D1OX-ray2.02A/B100-270[»]
2JNPNMR-A105-265[»]
2JT5NMR-A105-265[»]
2JT6NMR-A105-265[»]
2SRTNMR-A100-272[»]
2USNX-ray2.20A100-264[»]
3OHLX-ray2.36A100-266[»]
3OHOX-ray2.50A100-268[»]
3USNNMR-A100-267[»]
4DPEX-ray1.96A/B100-272[»]
4G9LX-ray1.88A/B100-272[»]
4JA1X-ray1.96A/B100-272[»]
ProteinModelPortaliP08254.
SMRiP08254. Positions 32-477.

Miscellaneous databases

EvolutionaryTraceiP08254.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati287 – 33650Hemopexin 1
Add
BLAST
Repeati337 – 38347Hemopexin 2
Add
BLAST
Repeati385 – 43349Hemopexin 3
Add
BLAST
Repeati434 – 47744Hemopexin 4
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi90 – 978Cysteine switch By similarity

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the peptidase M10A family.
Contains 4 hemopexin repeats.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG258253.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP08254.
KOiK01394.
OMAiVAVCSAY.
PhylomeDBiP08254.
TreeFamiTF315428.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
IPR028700. Stromelysin_1.
[Graphical view]
PANTHERiPTHR10201:SF38. PTHR10201:SF38. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08254-1 [UniParc]FASTAAdd to Basket

« Hide

MKSLPILLLL CVAVCSAYPL DGAARGEDTS MNLVQKYLEN YYDLKKDVKQ    50
FVRRKDSGPV VKKIREMQKF LGLEVTGKLD SDTLEVMRKP RCGVPDVGHF 100
RTFPGIPKWR KTHLTYRIVN YTPDLPKDAV DSAVEKALKV WEEVTPLTFS 150
RLYEGEADIM ISFAVREHGD FYPFDGPGNV LAHAYAPGPG INGDAHFDDD 200
EQWTKDTTGT NLFLVAAHEI GHSLGLFHSA NTEALMYPLY HSLTDLTRFR 250
LSQDDINGIQ SLYGPPPDSP ETPLVPTEPV PPEPGTPANC DPALSFDAVS 300
TLRGEILIFK DRHFWRKSLR KLEPELHLIS SFWPSLPSGV DAAYEVTSKD 350
LVFIFKGNQF WAIRGNEVRA GYPRGIHTLG FPPTVRKIDA AISDKEKNKT 400
YFFVEDKYWR FDEKRNSMEP GFPKQIAEDF PGIDSKIDAV FEEFGFFYFF 450
TGSSQLEFDP NAKKVTHTLK SNSWLNC 477
Length:477
Mass (Da):53,977
Last modified:February 1, 1991 - v2
Checksum:i96194833B907668D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451K → E.3 Publications
Corresponds to variant rs679620 [ dbSNP | Ensembl ].
VAR_013090

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti420 – 4201P → L1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05232 mRNA. Translation: CAA28859.1.
J03209 mRNA. Translation: AAA36321.1.
U78045 Genomic DNA. Translation: AAB36942.1.
AK223283 mRNA. Translation: BAD97003.1.
AK223291 mRNA. Translation: BAD97011.1.
AK313310 mRNA. Translation: BAG36115.1.
AF405705 Genomic DNA. Translation: AAK95247.1.
CH471065 Genomic DNA. Translation: EAW67032.1.
BC069676 mRNA. Translation: AAH69676.1.
BC069716 mRNA. Translation: AAH69716.1.
BC074815 mRNA. Translation: AAH74815.1.
BC074869 mRNA. Translation: AAH74869.1.
BC105954 mRNA. Translation: AAI05955.1.
BC107490 mRNA. Translation: AAI07491.1.
BC107491 mRNA. Translation: AAI07492.1.
CCDSiCCDS8323.1.
PIRiA28156. KCHUS1.
RefSeqiNP_002413.1. NM_002422.3.
UniGeneiHs.375129.

Genome annotation databases

EnsembliENST00000299855; ENSP00000299855; ENSG00000149968.
ENST00000572537; ENSP00000458496; ENSG00000263313.
GeneIDi4314.
KEGGihsa:4314.
UCSCiuc001phj.1. human.

Polymorphism databases

DMDMi116857.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05232 mRNA. Translation: CAA28859.1 .
J03209 mRNA. Translation: AAA36321.1 .
U78045 Genomic DNA. Translation: AAB36942.1 .
AK223283 mRNA. Translation: BAD97003.1 .
AK223291 mRNA. Translation: BAD97011.1 .
AK313310 mRNA. Translation: BAG36115.1 .
AF405705 Genomic DNA. Translation: AAK95247.1 .
CH471065 Genomic DNA. Translation: EAW67032.1 .
BC069676 mRNA. Translation: AAH69676.1 .
BC069716 mRNA. Translation: AAH69716.1 .
BC074815 mRNA. Translation: AAH74815.1 .
BC074869 mRNA. Translation: AAH74869.1 .
BC105954 mRNA. Translation: AAI05955.1 .
BC107490 mRNA. Translation: AAI07491.1 .
BC107491 mRNA. Translation: AAI07492.1 .
CCDSi CCDS8323.1.
PIRi A28156. KCHUS1.
RefSeqi NP_002413.1. NM_002422.3.
UniGenei Hs.375129.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B3D X-ray 2.30 A/B 100-272 [» ]
1B8Y X-ray 2.00 A 100-266 [» ]
1BIW X-ray 2.50 A/B 100-272 [» ]
1BM6 NMR - A 100-272 [» ]
1BQO X-ray 2.30 A/B 100-272 [» ]
1C3I X-ray 1.83 A/B 100-272 [» ]
1C8T X-ray 2.60 A/B 103-268 [» ]
1CAQ X-ray 1.80 A 100-267 [» ]
1CIZ X-ray 1.64 A 100-267 [» ]
1CQR X-ray 2.00 A/B 100-272 [» ]
1D5J X-ray 2.60 A/B 100-272 [» ]
1D7X X-ray 2.00 A/B 100-272 [» ]
1D8F X-ray 2.40 A/B 100-272 [» ]
1D8M X-ray 2.44 A/B 100-272 [» ]
1G05 X-ray 2.45 A/B 100-272 [» ]
1G49 X-ray 1.90 A/B 100-272 [» ]
1G4K X-ray 2.00 A/B/C 100-267 [» ]
1HFS X-ray 1.70 A 105-264 [» ]
1HY7 X-ray 1.50 A/B 100-272 [» ]
1M1W model - A 100-268 [» ]
1OO9 NMR - A 100-267 [» ]
1QIA X-ray 2.00 A/B/C/D 106-267 [» ]
1QIC X-ray 2.00 A/B/C/D 106-266 [» ]
1SLM X-ray 1.90 A 18-272 [» ]
1SLN X-ray 2.27 A 100-272 [» ]
1UEA X-ray 2.80 A/C 100-272 [» ]
1UMS NMR - A 100-273 [» ]
1UMT NMR - A 100-273 [» ]
1USN X-ray 1.80 A 100-264 [» ]
2D1O X-ray 2.02 A/B 100-270 [» ]
2JNP NMR - A 105-265 [» ]
2JT5 NMR - A 105-265 [» ]
2JT6 NMR - A 105-265 [» ]
2SRT NMR - A 100-272 [» ]
2USN X-ray 2.20 A 100-264 [» ]
3OHL X-ray 2.36 A 100-266 [» ]
3OHO X-ray 2.50 A 100-268 [» ]
3USN NMR - A 100-267 [» ]
4DPE X-ray 1.96 A/B 100-272 [» ]
4G9L X-ray 1.88 A/B 100-272 [» ]
4JA1 X-ray 1.96 A/B 100-272 [» ]
ProteinModelPortali P08254.
SMRi P08254. Positions 32-477.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110458. 3 interactions.
MINTi MINT-269333.
STRINGi 9606.ENSP00000299855.

Chemistry

BindingDBi P08254.
ChEMBLi CHEMBL2111321.
DrugBanki DB00786. Marimastat.
DB00641. Simvastatin.
GuidetoPHARMACOLOGYi 1630.

Protein family/group databases

MEROPSi M10.005.

PTM databases

PhosphoSitei P08254.

Polymorphism databases

DMDMi 116857.

Proteomic databases

PaxDbi P08254.
PRIDEi P08254.

Protocols and materials databases

DNASUi 4314.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299855 ; ENSP00000299855 ; ENSG00000149968 .
ENST00000572537 ; ENSP00000458496 ; ENSG00000263313 .
GeneIDi 4314.
KEGGi hsa:4314.
UCSCi uc001phj.1. human.

Organism-specific databases

CTDi 4314.
GeneCardsi GC11M102706.
HGNCi HGNC:7173. MMP3.
HPAi CAB016139.
HPA007875.
MIMi 185250. gene.
614466. phenotype.
neXtProti NX_P08254.
PharmGKBi PA30886.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG258253.
HOGENOMi HOG000217927.
HOVERGENi HBG052484.
InParanoidi P08254.
KOi K01394.
OMAi VAVCSAY.
PhylomeDBi P08254.
TreeFami TF315428.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_121096. EGFR Transactivation by Gastrin.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
REACT_222620. Collagen degradation.

Miscellaneous databases

ChiTaRSi MMP3. human.
EvolutionaryTracei P08254.
GeneWikii MMP3.
GenomeRNAii 4314.
NextBioi 16977.
PMAP-CutDB P08254.
PROi P08254.
SOURCEi Search...

Gene expression databases

ArrayExpressi P08254.
Bgeei P08254.
CleanExi HS_MMP3.
Genevestigatori P08254.

Family and domain databases

Gene3Di 2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
IPR028700. Stromelysin_1.
[Graphical view ]
PANTHERi PTHR10201:SF38. PTHR10201:SF38. 1 hit.
Pfami PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSi PR00138. MATRIXIN.
SMARTi SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete primary structure of human matrix metalloproteinase-3. Identity with stromelysin."
    Saus J., Quinones S., Otani Y., Nagase H., Harris E.D. Jr., Kurkinen M.
    J. Biol. Chem. 263:6742-6745(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-24.
  2. "Comparison of human stromelysin and collagenase by cloning and sequence analysis."
    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.
    Biochem. J. 240:913-916(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fibroblast.
  3. "Human skin fibroblast stromelysin: structure, glycosylation, substrate specificity, and differential expression in normal and tumorigenic cells."
    Wilhelm S.M., Collier I.E., Kronberger A., Eisen A.Z., Marmer B.L., Grant G.A., Bauer E.A., Goldberg G.I.
    Proc. Natl. Acad. Sci. U.S.A. 84:6725-6729(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Three matrix metalloproteinases on 81kb of P1 insert."
    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.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Synovium.
  6. 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
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-45.
    Tissue: Synovium.
  7. SeattleSNPs variation discovery resource
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-45.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-45.
    Tissue: Lung.
  10. "Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate."
    Nagase H., Enghild J.J., Suzuki K., Salvesen G.
    Biochemistry 29:5783-5789(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ZYMOGEN ACTIVATION.
  11. "Progression of coronary atherosclerosis is associated with a common genetic variant of the human stromelysin-1 promoter which results in reduced gene expression."
    Ye S., Eriksson P., Hamsten A., Kurkinen M., Humphries S.E., Henney A.M.
    J. Biol. Chem. 271:13055-13060(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CHDS6.
  12. "Prediction of the risk of myocardial infarction from polymorphisms in candidate genes."
    Yamada Y., Izawa H., Ichihara S., Takatsu F., Ishihara H., Hirayama H., Sone T., Tanaka M., Yokota M.
    N. Engl. J. Med. 347:1916-1923(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CHDS6.
  13. Cited for: STRUCTURE BY NMR OF CATALYTIC DOMAIN.
  14. Cited for: STRUCTURE BY NMR OF 100-267.
  15. "Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme."
    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.
    Protein Sci. 4:1966-1976(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-272.
  16. "X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily."
    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.
    Structure 4:375-386(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-266.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 105-264.
  18. "Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1."
    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.
    Nature 389:77-81(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 100-267 IN COMPLEX WITH TIMP1.
  19. "Structural characterizations of nonpeptidic thiadiazole inhibitors of matrix metalloproteinases reveal the basis for stromelysin selectivity."
    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.
    Protein Sci. 7:2118-2126(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 100-264.
  20. "Crystal structure of the stromelysin catalytic domain at 2.0-A resolution: inhibitor-induced conformational changes."
    Chen L., Rydel T.J., Gu F., Dunaway C.M., Pikul S., Dunham K.M., Barnett B.L.
    J. Mol. Biol. 293:545-557(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-272.
  21. "X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity."
    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.
    Protein Sci. 8:1455-1462(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 100-267.
  22. "Solution structure of the catalytic domain of human stromelysin-1 complexed to a potent, nonpeptidic inhibitor."
    Li Y.C., Zhang X., Melton R., Ganu V., Gonnella N.C.
    Biochemistry 37:14048-14056(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 100-272.

Entry informationi

Entry nameiMMP3_HUMAN
AccessioniPrimary (citable) accession number: P08254
Secondary accession number(s): B2R8B8, Q3B7S0, Q6GRF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1991
Last modified: September 3, 2014
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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