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P39900

- MMP12_HUMAN

UniProt

P39900 - MMP12_HUMAN

Protein

Macrophage metalloelastase

Gene

MMP12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.

    Catalytic activityi

    Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.

    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 formBy similarity
    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; catalytic
    Active sitei219 – 2191
    Metal bindingi222 – 2221Zinc 2; catalytic
    Metal bindingi228 – 2281Zinc 2; catalytic
    Metal bindingi289 – 2891Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi333 – 3331Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi381 – 3811Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi430 – 4301Calcium 4; via carbonyl oxygenBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. collagen catabolic process Source: Reactome
    2. extracellular matrix disassembly Source: Reactome
    3. extracellular matrix organization Source: Reactome
    4. positive regulation of epithelial cell proliferation involved in wound healing Source: BHF-UCL
    5. proteolysis Source: ProtInc
    6. wound healing, spreading of epidermal cells Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_150401. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.009.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Macrophage metalloelastase (EC:3.4.24.65)
    Short name:
    MME
    Alternative name(s):
    Macrophage elastase
    Short name:
    ME
    Short name:
    hME
    Matrix metalloproteinase-12
    Short name:
    MMP-12
    Gene namesi
    Name:MMP12
    Synonyms:HME
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:7158. MMP12.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30870.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616CuratedAdd
    BLAST
    Propeptidei17 – 10589Activation peptideBy similarityPRO_0000028776Add
    BLAST
    Chaini106 – 470365Macrophage metalloelastasePRO_0000028777Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi20 – 201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi282 ↔ 470By similarity
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP39900.
    PRIDEiP39900.

    PTM databases

    PhosphoSiteiP39900.

    Expressioni

    Tissue specificityi

    Found in alveolar macrophages but not in peripheral blood monocytes.

    Inductioni

    By exposure to bacterial lipopolysaccharides (LPS). Inhibited by dexamethasone.

    Gene expression databases

    CleanExiHS_MMP12.
    GenevestigatoriP39900.

    Interactioni

    Protein-protein interaction databases

    BioGridi110464. 1 interaction.
    IntActiP39900. 1 interaction.
    MINTiMINT-7709562.
    STRINGi9606.ENSP00000320664.

    Structurei

    Secondary structure

    1
    470
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi106 – 1083
    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 strandi203 – 2119
    Helixi212 – 22312
    Turni232 – 2365
    Beta strandi237 – 2393
    Helixi245 – 2473
    Helixi252 – 2598
    Beta strandi260 – 2623
    Beta strandi266 – 2683
    Beta strandi281 – 2844
    Beta strandi291 – 2944
    Beta strandi297 – 3026
    Beta strandi305 – 3084
    Beta strandi318 – 3203
    Helixi321 – 3244
    Beta strandi334 – 3385
    Helixi339 – 3413
    Beta strandi343 – 3486
    Beta strandi351 – 3544
    Beta strandi357 – 3604
    Turni361 – 3633
    Beta strandi365 – 3673
    Turni368 – 3725
    Beta strandi382 – 3865
    Turni387 – 3904
    Beta strandi391 – 3966
    Beta strandi399 – 4046
    Turni405 – 4084
    Helixi418 – 4214
    Beta strandi430 – 4356
    Turni436 – 4383
    Beta strandi439 – 4446
    Beta strandi447 – 4526
    Turni453 – 4564
    Beta strandi457 – 4637
    Turni464 – 4696

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JIZX-ray2.60A/B100-264[»]
    1JK3X-ray1.09A106-263[»]
    1OS2X-ray2.15A/B/C/D/E/F106-268[»]
    1OS9X-ray1.85A/B/C/D/E/F106-268[»]
    1RMZX-ray1.34A106-263[»]
    1ROSX-ray2.00A/B106-268[»]
    1UTTX-ray2.20A106-264[»]
    1UTZX-ray2.50A/B106-264[»]
    1Y93X-ray1.03A106-263[»]
    1YCMNMR-A106-263[»]
    1Z3JNMR-A106-263[»]
    2HU6X-ray1.32A106-263[»]
    2JXYNMR-A278-470[»]
    2K2GNMR-A100-263[»]
    2K9CNMR-A112-263[»]
    2KRJNMR-A112-263[»]
    2OXUX-ray1.24A106-263[»]
    2OXWX-ray1.15A106-263[»]
    2OXZX-ray1.90A106-263[»]
    2POJNMR-A100-263[»]
    2W0DX-ray2.00A/B/C/D106-263[»]
    2WO8X-ray2.00A/B/C/D106-268[»]
    2WO9X-ray1.70A/B/C/D106-268[»]
    2WOAX-ray2.30A/B/C/D106-268[»]
    2Z2DNMR-A100-263[»]
    3BA0X-ray3.00A106-470[»]
    3EHXX-ray1.90A106-263[»]
    3EHYX-ray1.90A106-263[»]
    3F15X-ray1.70A106-263[»]
    3F16X-ray1.16A106-263[»]
    3F17X-ray1.10A106-263[»]
    3F18X-ray1.13A106-263[»]
    3F19X-ray1.13A106-263[»]
    3F1AX-ray1.25A106-263[»]
    3LIKX-ray1.80A106-263[»]
    3LILX-ray1.80A106-263[»]
    3LIRX-ray1.90A106-263[»]
    3LJGX-ray1.31A106-263[»]
    3LK8X-ray1.80A106-263[»]
    3LKAX-ray1.80A106-263[»]
    3N2UX-ray1.81A106-263[»]
    3N2VX-ray1.55A106-263[»]
    3NX7X-ray1.80A106-263[»]
    3RTSX-ray1.81A106-263[»]
    3RTTX-ray1.82A106-263[»]
    3TS4X-ray1.59A106-263[»]
    3TSKX-ray2.00A106-263[»]
    3UVCX-ray1.30A/B106-263[»]
    4EFSX-ray1.63A106-263[»]
    4GQLX-ray1.15A106-263[»]
    4GR0X-ray1.50A106-263[»]
    4GR3X-ray1.49A106-263[»]
    4GR8X-ray1.30A111-262[»]
    4GUYX-ray2.00A106-263[»]
    4H30X-ray1.43A/B106-263[»]
    4H49X-ray2.16A/B/C/D106-263[»]
    4H76X-ray1.50A106-263[»]
    4H84X-ray1.59A/B106-263[»]
    4I03X-ray1.70A106-263[»]
    4IJOX-ray1.90A106-263[»]
    DisProtiDP00571.
    ProteinModelPortaliP39900.
    SMRiP39900. Positions 34-470.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39900.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati279 – 32850Hemopexin 1Add
    BLAST
    Repeati329 – 37547Hemopexin 2Add
    BLAST
    Repeati377 – 42549Hemopexin 3Add
    BLAST
    Repeati426 – 47045Hemopexin 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

    eggNOGiNOG323958.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiP39900.
    KOiK01413.
    OMAiRKHYITY.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiP39900.

    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.
    IPR028718. MMP12.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF32. PTHR10201:SF32. 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.

    P39900-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFGERYLEKF YGLEINKLPV    50
    TKMKYSGNLM KEKIQEMQHF LGLKVTGQLD TSTLEMMHAP RCGVPDVHHF 100
    REMPGGPVWR KHYITYRINN YTPDMNREDV DYAIRKAFQV WSNVTPLKFS 150
    KINTGMADIL VVFARGAHGD FHAFDGKGGI LAHAFGPGSG IGGDAHFDED 200
    EFWTTHSGGT NLFLTAVHEI GHSLGLGHSS DPKAVMFPTY KYVDINTFRL 250
    SADDIRGIQS LYGDPKENQR LPNPDNSEPA LCDPNLSFDA VTTVGNKIFF 300
    FKDRFFWLKV SERPKTSVNL ISSLWPTLPS GIEAAYEIEA RNQVFLFKDD 350
    KYWLISNLRP EPNYPKSIHS FGFPNFVKKI DAAVFNPRFY RTYFFVDNQY 400
    WRYDERRQMM DPGYPKLITK NFQGIGPKID AVFYSKNKYY YFFQGSNQFE 450
    YDFLLQRITK TLKSNSWFGC 470
    Length:470
    Mass (Da):54,002
    Last modified:February 1, 1995 - v1
    Checksum:i8C745EEA8C0EA216
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti357 – 3571N → S.2 Publications
    Corresponds to variant rs652438 [ dbSNP | Ensembl ].
    VAR_021343
    Natural varianti469 – 4691G → R.1 Publication
    Corresponds to variant rs28381701 [ dbSNP | Ensembl ].
    VAR_021344

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L23808 mRNA. Translation: AAA58658.1. Sequence problems.
    AY856072 Genomic DNA. Translation: AAW29944.1.
    AK313959 mRNA. Translation: BAG36675.1.
    CH471065 Genomic DNA. Translation: EAW67033.1.
    BC112301 mRNA. Translation: AAI12302.1.
    BC143773 mRNA. Translation: AAI43774.1.
    PIRiA49499.
    RefSeqiNP_002417.2. NM_002426.4.
    UniGeneiHs.1695.
    Hs.709832.

    Genome annotation databases

    EnsembliENST00000571244; ENSP00000458585; ENSG00000262406.
    GeneIDi4321.
    KEGGihsa:4321.
    UCSCiuc001phk.3. human.

    Polymorphism databases

    DMDMi729179.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L23808 mRNA. Translation: AAA58658.1 . Sequence problems.
    AY856072 Genomic DNA. Translation: AAW29944.1 .
    AK313959 mRNA. Translation: BAG36675.1 .
    CH471065 Genomic DNA. Translation: EAW67033.1 .
    BC112301 mRNA. Translation: AAI12302.1 .
    BC143773 mRNA. Translation: AAI43774.1 .
    PIRi A49499.
    RefSeqi NP_002417.2. NM_002426.4.
    UniGenei Hs.1695.
    Hs.709832.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JIZ X-ray 2.60 A/B 100-264 [» ]
    1JK3 X-ray 1.09 A 106-263 [» ]
    1OS2 X-ray 2.15 A/B/C/D/E/F 106-268 [» ]
    1OS9 X-ray 1.85 A/B/C/D/E/F 106-268 [» ]
    1RMZ X-ray 1.34 A 106-263 [» ]
    1ROS X-ray 2.00 A/B 106-268 [» ]
    1UTT X-ray 2.20 A 106-264 [» ]
    1UTZ X-ray 2.50 A/B 106-264 [» ]
    1Y93 X-ray 1.03 A 106-263 [» ]
    1YCM NMR - A 106-263 [» ]
    1Z3J NMR - A 106-263 [» ]
    2HU6 X-ray 1.32 A 106-263 [» ]
    2JXY NMR - A 278-470 [» ]
    2K2G NMR - A 100-263 [» ]
    2K9C NMR - A 112-263 [» ]
    2KRJ NMR - A 112-263 [» ]
    2OXU X-ray 1.24 A 106-263 [» ]
    2OXW X-ray 1.15 A 106-263 [» ]
    2OXZ X-ray 1.90 A 106-263 [» ]
    2POJ NMR - A 100-263 [» ]
    2W0D X-ray 2.00 A/B/C/D 106-263 [» ]
    2WO8 X-ray 2.00 A/B/C/D 106-268 [» ]
    2WO9 X-ray 1.70 A/B/C/D 106-268 [» ]
    2WOA X-ray 2.30 A/B/C/D 106-268 [» ]
    2Z2D NMR - A 100-263 [» ]
    3BA0 X-ray 3.00 A 106-470 [» ]
    3EHX X-ray 1.90 A 106-263 [» ]
    3EHY X-ray 1.90 A 106-263 [» ]
    3F15 X-ray 1.70 A 106-263 [» ]
    3F16 X-ray 1.16 A 106-263 [» ]
    3F17 X-ray 1.10 A 106-263 [» ]
    3F18 X-ray 1.13 A 106-263 [» ]
    3F19 X-ray 1.13 A 106-263 [» ]
    3F1A X-ray 1.25 A 106-263 [» ]
    3LIK X-ray 1.80 A 106-263 [» ]
    3LIL X-ray 1.80 A 106-263 [» ]
    3LIR X-ray 1.90 A 106-263 [» ]
    3LJG X-ray 1.31 A 106-263 [» ]
    3LK8 X-ray 1.80 A 106-263 [» ]
    3LKA X-ray 1.80 A 106-263 [» ]
    3N2U X-ray 1.81 A 106-263 [» ]
    3N2V X-ray 1.55 A 106-263 [» ]
    3NX7 X-ray 1.80 A 106-263 [» ]
    3RTS X-ray 1.81 A 106-263 [» ]
    3RTT X-ray 1.82 A 106-263 [» ]
    3TS4 X-ray 1.59 A 106-263 [» ]
    3TSK X-ray 2.00 A 106-263 [» ]
    3UVC X-ray 1.30 A/B 106-263 [» ]
    4EFS X-ray 1.63 A 106-263 [» ]
    4GQL X-ray 1.15 A 106-263 [» ]
    4GR0 X-ray 1.50 A 106-263 [» ]
    4GR3 X-ray 1.49 A 106-263 [» ]
    4GR8 X-ray 1.30 A 111-262 [» ]
    4GUY X-ray 2.00 A 106-263 [» ]
    4H30 X-ray 1.43 A/B 106-263 [» ]
    4H49 X-ray 2.16 A/B/C/D 106-263 [» ]
    4H76 X-ray 1.50 A 106-263 [» ]
    4H84 X-ray 1.59 A/B 106-263 [» ]
    4I03 X-ray 1.70 A 106-263 [» ]
    4IJO X-ray 1.90 A 106-263 [» ]
    DisProti DP00571.
    ProteinModelPortali P39900.
    SMRi P39900. Positions 34-470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110464. 1 interaction.
    IntActi P39900. 1 interaction.
    MINTi MINT-7709562.
    STRINGi 9606.ENSP00000320664.

    Chemistry

    BindingDBi P39900.
    ChEMBLi CHEMBL4393.
    DrugBanki DB00551. Acetohydroxamic Acid.

    Protein family/group databases

    MEROPSi M10.009.

    PTM databases

    PhosphoSitei P39900.

    Polymorphism databases

    DMDMi 729179.

    Proteomic databases

    PaxDbi P39900.
    PRIDEi P39900.

    Protocols and materials databases

    DNASUi 4321.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000571244 ; ENSP00000458585 ; ENSG00000262406 .
    GeneIDi 4321.
    KEGGi hsa:4321.
    UCSCi uc001phk.3. human.

    Organism-specific databases

    CTDi 4321.
    GeneCardsi GC11M102767.
    HGNCi HGNC:7158. MMP12.
    MIMi 601046. gene.
    neXtProti NX_P39900.
    PharmGKBi PA30870.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG323958.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi P39900.
    KOi K01413.
    OMAi RKHYITY.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi P39900.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_150401. Collagen degradation.

    Miscellaneous databases

    ChiTaRSi MMP12. human.
    EvolutionaryTracei P39900.
    GeneWikii Matrix_metallopeptidase_12.
    GenomeRNAii 4321.
    NextBioi 17001.
    PROi P39900.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_MMP12.
    Genevestigatori P39900.

    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.
    IPR028718. MMP12.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF32. PTHR10201:SF32. 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. "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages."
      Shapiro S.D., Kobayashi D.K., Ley T.J.
      J. Biol. Chem. 268:23824-23829(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Alveolar macrophage.
    2. NIEHS SNPs program
      Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-357 AND ARG-469.
    3. "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: Esophagus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 SER-357.
    6. "Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase."
      Gronski T.J. Jr., Martin R.L., Kobayashi D.K., Walsh B.C., Holman M.C., Huber M., Van Wart H.E., Shapiro S.D.
      J. Biol. Chem. 272:12189-12194(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure."
      Lang R., Kocourek A., Braun M., Tschesche H., Huber R., Bode W., Maskos K.
      J. Mol. Biol. 312:731-742(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS) OF 106-263.
    8. "Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor."
      Nar H., Werle K., Bauer M.M.T., Dollinger H., Jung B.
      J. Mol. Biol. 312:743-751(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 100-280.

    Entry informationi

    Entry nameiMMP12_HUMAN
    AccessioniPrimary (citable) accession number: P39900
    Secondary accession number(s): B2R9X8, B7ZLF6, Q2M1L9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 158 of the entry and version 1 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, 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