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Q9R0S3

- MMP17_MOUSE

UniProt

Q9R0S3 - MMP17_MOUSE

Protein

Matrix metalloproteinase-17

Gene

Mmp17

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin.1 Publication

    Catalytic activityi

    Cleaves pro-TNF-alpha at the 74-Ala-|-Gln-75 site.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity
    Calcium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi109 – 1091Zinc; in inhibited formBy similarity
    Metal bindingi247 – 2471Zinc; catalyticPROSITE-ProRule annotation
    Active sitei248 – 2481
    Metal bindingi251 – 2511Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi257 – 2571Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM10.017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-17 (EC:3.4.24.-)
    Short name:
    MMP-17
    Alternative name(s):
    Membrane-type matrix metalloproteinase 4
    Short name:
    MT-MMP 4
    Short name:
    MTMMP4
    Membrane-type-4 matrix metalloproteinase
    Short name:
    MT4-MMP
    Short name:
    MT4MMP
    Gene namesi
    Name:Mmp17
    Synonyms:Mt4mmp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1346076. Mmp17.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell
    3. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Extracellular matrix, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi248 – 2481E → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3939Sequence AnalysisAdd
    BLAST
    Propeptidei40 – 12485By similarityPRO_0000028821Add
    BLAST
    Chaini125 – 558434Matrix metalloproteinase-17PRO_0000028822Add
    BLAST
    Propeptidei559 – 57820Removed in mature formSequence AnalysisPRO_0000028823Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi336 ↔ 527By similarity
    Lipidationi558 – 5581GPI-anchor amidated serineSequence Analysis

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

    Proteomic databases

    PaxDbiQ9R0S3.
    PRIDEiQ9R0S3.

    2D gel databases

    REPRODUCTION-2DPAGEQ9R0S3.

    PTM databases

    PhosphoSiteiQ9R0S3.

    Expressioni

    Tissue specificityi

    Expressed by monocytes and macrophages.

    Gene expression databases

    BgeeiQ9R0S3.
    CleanExiMM_MMP17.
    GenevestigatoriQ9R0S3.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000031390.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R0S3.
    SMRiQ9R0S3. Positions 47-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati333 – 38250Hemopexin 1Add
    BLAST
    Repeati386 – 43247Hemopexin 2Add
    BLAST
    Repeati436 – 47944Hemopexin 3Add
    BLAST
    Repeati480 – 52748Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi107 – 1148Cysteine 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

    eggNOGiNOG295915.
    GeneTreeiENSGT00750000117336.
    HOGENOMiHOG000217928.
    HOVERGENiHBG052484.
    InParanoidiQ80UM9.
    KOiK07997.
    OMAiAHNDRTY.
    OrthoDBiEOG7XPZ57.
    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.
    IPR024079. MetalloPept_cat_dom.
    IPR028726. MMP17.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF118. PTHR10201:SF118. 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.
    PROSITEiPS51642. 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.

    Q9R0S3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRRPRGPGS PRGPGPPRPG PGLPPLLLVL ALAAHGGCAA PAPRAEDLSL    50
    GVEWLSRFGY LPPADPASGQ LQTQEELSKA ITAMQQFGGL ETTGILDEAT 100
    LALMKTPRCS LPDLPPGAQS RRKRQTPPPT KWSKRNLSWR VRTFPRDSPL 150
    GRDTVRALMY YALKVWSDIT PLNFHEVAGN AADIQIDFSK ADHNDGYPFD 200
    GPGGTVAHAF FPGDHHTAGD THFDDDEPWT FRSSDAHGMD LFAVAVHEFG 250
    HAIGLSHVAA PSSIMQPYYQ GPVGDPLRYG LPYEDRVRVW QLYGVRESVS 300
    PTAQLDTPEP EEPPLLPEPP NNRSSTPPQK DVPHRCTAHF DAVAQIRGEA 350
    FFFKGKYFWR LTRDRHLVSL QPAQMHRFWR GLPLHLDSVD AVYERTSDHK 400
    IVFFKGDRYW VFKDNNVEEG YPRPVSDFSL PPGGIDAVFS WAHNDRTYFF 450
    KDQLYWRYDD HTRRMDPGYP AQGPLWRGVP SMLDDAMRWS DGASYFFRGQ 500
    EYWKVLDGEL EAAPGYPQST ARDWLVCGEP LADAEDVGPG PQGRSGAQDG 550
    LAVCSCTSDA HRLALPSLLL LTPLLWGL 578
    Length:578
    Mass (Da):64,333
    Last modified:July 27, 2011 - v3
    Checksum:i168C933B63A1EB7B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451A → G in CAB92315. (PubMed:10799478)Curated
    Sequence conflicti277 – 2771L → V in BAA82708. (PubMed:10471807)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021224 mRNA. Translation: BAA82708.2.
    AJ010731 mRNA. Translation: CAB92315.1.
    CH466529 Genomic DNA. Translation: EDL19513.1.
    BC051917 mRNA. Translation: AAH51917.1.
    CCDSiCCDS19695.1.
    RefSeqiNP_035976.3. NM_011846.4.
    UniGeneiMm.42047.

    Genome annotation databases

    EnsembliENSMUST00000031390; ENSMUSP00000031390; ENSMUSG00000029436.
    GeneIDi23948.
    KEGGimmu:23948.
    UCSCiuc008zsy.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021224 mRNA. Translation: BAA82708.2 .
    AJ010731 mRNA. Translation: CAB92315.1 .
    CH466529 Genomic DNA. Translation: EDL19513.1 .
    BC051917 mRNA. Translation: AAH51917.1 .
    CCDSi CCDS19695.1.
    RefSeqi NP_035976.3. NM_011846.4.
    UniGenei Mm.42047.

    3D structure databases

    ProteinModelPortali Q9R0S3.
    SMRi Q9R0S3. Positions 47-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000031390.

    Protein family/group databases

    MEROPSi M10.017.

    PTM databases

    PhosphoSitei Q9R0S3.

    2D gel databases

    REPRODUCTION-2DPAGE Q9R0S3.

    Proteomic databases

    PaxDbi Q9R0S3.
    PRIDEi Q9R0S3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031390 ; ENSMUSP00000031390 ; ENSMUSG00000029436 .
    GeneIDi 23948.
    KEGGi mmu:23948.
    UCSCi uc008zsy.1. mouse.

    Organism-specific databases

    CTDi 4326.
    MGIi MGI:1346076. Mmp17.

    Phylogenomic databases

    eggNOGi NOG295915.
    GeneTreei ENSGT00750000117336.
    HOGENOMi HOG000217928.
    HOVERGENi HBG052484.
    InParanoidi Q80UM9.
    KOi K07997.
    OMAi AHNDRTY.
    OrthoDBi EOG7XPZ57.
    TreeFami TF315428.

    Miscellaneous databases

    NextBioi 303765.
    PROi Q9R0S3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9R0S3.
    CleanExi MM_MMP17.
    Genevestigatori Q9R0S3.

    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.
    IPR024079. MetalloPept_cat_dom.
    IPR028726. MMP17.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF118. PTHR10201:SF118. 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 PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human membrane type-4 matrix metalloproteinase (MT4-MMP) is encoded by a novel major transcript: isolation of complementary DNA clones for human and mouse mt4-mmp transcripts."
      Kajita M., Kinoh H., Ito N., Takamura A., Itoh Y., Okada A., Sato H., Seiki M.
      FEBS Lett. 457:353-356(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Embryonic brain.
    2. Seiki M.
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO C-TERMINUS.
    3. "Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2."
      English W.R., Puente X.S., Freije J.M.P., Knaeuper V., Amour A., Merryweather A., Lopez-Otin C., Murphy G.
      J. Biol. Chem. 275:14046-14055(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Brain.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      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].
      Strain: C57BL/6.
      Tissue: Embryonic brain.
    6. "Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase."
      Itoh Y., Kajita M., Kinoh H., Mori H., Okada A., Seiki M.
      J. Biol. Chem. 274:34260-34266(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR, MUTAGENESIS OF GLU-248.

    Entry informationi

    Entry nameiMMP17_MOUSE
    AccessioniPrimary (citable) accession number: Q9R0S3
    Secondary accession number(s): Q80UM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3