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P08254

- MMP3_HUMAN

UniProt

P08254 - MMP3_HUMAN

Protein

Stromelysin-1

Gene

MMP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 2 (01 Feb 1991)
      Previous versions | rss
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    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 oxygenBy similarity
    Metal bindingi389 – 3891Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi438 – 4381Calcium 4; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. endopeptidase activity Source: ParkinsonsUK-UCL
    3. metalloendopeptidase activity Source: ProtInc
    4. 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. negative regulation of hydrogen peroxide metabolic process Source: ParkinsonsUK-UCL
    6. proteolysis Source: ParkinsonsUK-UCL
    7. regulation of cell migration Source: Ensembl

    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

    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.2 Publications
    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.

    Organism-specific databases

    MIMi614466. phenotype.
    PharmGKBiPA30886.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17171 PublicationAdd
    BLAST
    Propeptidei18 – 9982Activation peptidePRO_0000028728Add
    BLAST
    Chaini100 – 477378Stromelysin-1PRO_0000028729Add
    BLAST

    Amino acid modifications

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

    1
    477
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08254.

    Family & Domainsi

    Domains and Repeats

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

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi90 – 978Cysteine switchBy 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.

    Sequence similaritiesi

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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti420 – 4201P → L(PubMed:3477804)Curated

    Natural variant

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

    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.
    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 .
    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

    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: October 1, 2014
    This is version 167 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