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Q63341

- MMP12_RAT

UniProt

Q63341 - MMP12_RAT

Protein

Macrophage metalloelastase

Gene

Mmp12

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 By similarity.By similarity

    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.By similarity
    Binds 2 zinc ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi88 – 881Zinc 2; in inhibited formBy similarity
    Metal bindingi120 – 1201Calcium 1By similarity
    Metal bindingi154 – 1541Calcium 2By similarity
    Metal bindingi164 – 1641Zinc 1By similarity
    Metal bindingi166 – 1661Zinc 1By similarity
    Metal bindingi171 – 1711Calcium 3By similarity
    Metal bindingi172 – 1721Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi174 – 1741Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi176 – 1761Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi179 – 1791Zinc 1By similarity
    Metal bindingi186 – 1861Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi190 – 1901Calcium 2By similarity
    Metal bindingi192 – 1921Zinc 1By similarity
    Metal bindingi194 – 1941Calcium 3By similarity
    Metal bindingi195 – 1951Calcium 1By similarity
    Metal bindingi197 – 1971Calcium 1By similarity
    Metal bindingi197 – 1971Calcium 3By similarity
    Metal bindingi214 – 2141Zinc 2; catalyticBy similarity
    Active sitei215 – 2151PROSITE-ProRule annotation
    Metal bindingi218 – 2181Zinc 2; catalyticBy similarity
    Metal bindingi224 – 2241Zinc 2; catalyticBy similarity
    Metal bindingi285 – 2851Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi377 – 3771Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi426 – 4261Calcium 4; via carbonyl oxygenBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. positive regulation of epithelial cell proliferation Source: RGD
    2. response to drug Source: RGD
    3. response to organic cyclic compound Source: RGD
    4. wound healing Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    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):
    Matrix metalloproteinase-12
    Short name:
    MMP-12
    Gene namesi
    Name:Mmp12
    Synonyms:Mmel
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620195. Mmp12.

    Subcellular locationi

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121CuratedAdd
    BLAST
    Propeptidei22 – 10180Activation peptideBy similarityPRO_0000028782Add
    BLAST
    Chaini102 – 465364Macrophage metalloelastasePRO_0000028783Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi278 ↔ 465By similarity
    Glycosylationi313 – 3131N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PRIDEiQ63341.

    Expressioni

    Gene expression databases

    GenevestigatoriQ63341.

    Interactioni

    Structurei

    3D structure databases

    ProteinModelPortaliQ63341.
    SMRiQ63341. Positions 105-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati281 – 32444Hemopexin 1Add
    BLAST
    Repeati325 – 37147Hemopexin 2Add
    BLAST
    Repeati373 – 42149Hemopexin 3Add
    BLAST
    Repeati422 – 46544Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi86 – 938Cysteine 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.
    InParanoidiQ63341.
    KOiK01413.
    PhylomeDBiQ63341.
    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.
    IPR028718. MMP12.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    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.
    PROSITEiPS00024. 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.

    Q63341-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFLLVLVLL VSLQVSACGA APMNESEFAE WYLSRFFDYQ GDRIPMTKTK    50
    TNRNLLEEKL QEMQQFFGLE VTGQLDTSTL KIMHTSRCGV PDVQHLRAVP 100
    QRSRWMKRYL TYRIYNYTPD MKRADVDYIF QKAFQVWSDV TPLRFRKIHK 150
    GEADITILFA FGDHGDFYDF DGKGGTLAHA FYPGPGIQGD AHFDEAETWT 200
    KSFQGTNLFL VAVHELGHSL GLRHSNNPKS IMYPTYRYLH PNTFRLSADD 250
    IHSIQSLYGA PVKNPSLTNP GSPPSTVCHQ SLSFDAVTTV GDKIFFFKDW 300
    FFWWRLPGSP ATNITSISSM WPTIPSGIQA AYEIGGRNQL FLFKDEKYWL 350
    INNLVPEPHY PRSIHSLGFP ASVKKIDAAV FDPLRQKVYF FVDKQYWRYD 400
    VRQELMDAAY PKLISTHFPG IRPKIDAVLY FKRHYYIFQG AYQLEYDPLL 450
    DRVTKTLSST SWFGC 465
    Length:465
    Mass (Da):53,738
    Last modified:November 1, 1996 - v1
    Checksum:iE779B6014EC6FF68
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti223 – 2231R → P in AAH88120. (PubMed:15489334)Curated
    Sequence conflicti451 – 4511D → H in AAH88120. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98517 mRNA. Translation: CAA67142.1.
    BC088120 mRNA. Translation: AAH88120.1.
    RefSeqiNP_446415.2. NM_053963.2.
    UniGeneiRn.33193.

    Genome annotation databases

    GeneIDi117033.
    KEGGirno:117033.
    UCSCiRGD:620195. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98517 mRNA. Translation: CAA67142.1 .
    BC088120 mRNA. Translation: AAH88120.1 .
    RefSeqi NP_446415.2. NM_053963.2.
    UniGenei Rn.33193.

    3D structure databases

    ProteinModelPortali Q63341.
    SMRi Q63341. Positions 105-465.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi Q63341.
    ChEMBLi CHEMBL5506.

    Protein family/group databases

    MEROPSi M10.009.

    Proteomic databases

    PRIDEi Q63341.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 117033.
    KEGGi rno:117033.
    UCSCi RGD:620195. rat.

    Organism-specific databases

    CTDi 4321.
    RGDi 620195. Mmp12.

    Phylogenomic databases

    eggNOGi NOG323958.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi Q63341.
    KOi K01413.
    PhylomeDBi Q63341.
    TreeFami TF315428.

    Miscellaneous databases

    NextBioi 619817.
    PROi Q63341.

    Gene expression databases

    Genevestigatori Q63341.

    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.
    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 PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cossins J., Clements J., Catlin G.
      Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
    2. "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].
      Tissue: Thymus.

    Entry informationi

    Entry nameiMMP12_RAT
    AccessioniPrimary (citable) accession number: Q63341
    Secondary accession number(s): Q5I0P0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3