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Q9WTR0

- MMP16_MOUSE

UniProt

Q9WTR0 - MMP16_MOUSE

Protein

Matrix metalloproteinase-16

Gene

Mmp16

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 134 (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 collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells By similarity.By similarity

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi101 – 1011Zinc 1; in inhibited formBy similarity
    Metal bindingi183 – 1831Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi193 – 1931Zinc 1By similarity
    Metal bindingi195 – 1951Zinc 1By similarity
    Metal bindingi200 – 2001Calcium 2By similarity
    Metal bindingi201 – 2011Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi203 – 2031Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi205 – 2051Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi215 – 2151Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi217 – 2171Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi219 – 2191Calcium 1By similarity
    Metal bindingi223 – 2231Calcium 2By similarity
    Metal bindingi226 – 2261Calcium 2By similarity
    Metal bindingi246 – 2461Zinc 2; catalyticBy similarity
    Active sitei247 – 2471PROSITE-ProRule annotation
    Metal bindingi250 – 2501Zinc 2; catalyticBy similarity
    Metal bindingi256 – 2561Zinc 2; catalyticBy 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. bone development Source: MGI
    2. chondrocyte proliferation Source: MGI
    3. collagen catabolic process Source: MGI
    4. craniofacial suture morphogenesis Source: MGI
    5. embryonic cranial skeleton morphogenesis Source: MGI
    6. endochondral ossification Source: MGI
    7. ossification Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.

    Protein family/group databases

    MEROPSiM10.016.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-16 (EC:3.4.24.-)
    Short name:
    MMP-16
    Alternative name(s):
    Membrane-type matrix metalloproteinase 3
    Short name:
    MT-MMP 3
    Short name:
    MTMMP3
    Membrane-type-3 matrix metalloproteinase
    Short name:
    MT3-MMP
    Short name:
    MT3MMP
    Gene namesi
    Name:Mmp16
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1276107. Mmp16.

    Subcellular locationi

    Cell membrane Curated; Single-pass type I membrane protein Curated; Extracellular side Curated
    Note: Localized at the cell surface of melanoma cells.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Propeptidei32 – 11988By similarityPRO_0000028814Add
    BLAST
    Chaini120 – 607488Matrix metalloproteinase-16PRO_0000028815Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi343 ↔ 532By similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PRIDEiQ9WTR0.

    PTM databases

    PhosphoSiteiQ9WTR0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9WTR0.
    BgeeiQ9WTR0.
    CleanExiMM_MMP16.
    GenevestigatoriQ9WTR0.

    Interactioni

    Subunit structurei

    Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000029881.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WTR0.
    SMRiQ9WTR0. Positions 85-561.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini120 – 564445ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini586 – 60722CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei565 – 58521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati340 – 38849Hemopexin 1Add
    BLAST
    Repeati389 – 43446Hemopexin 2Add
    BLAST
    Repeati436 – 48449Hemopexin 3Add
    BLAST
    Repeati485 – 53248Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi99 – 1068Cysteine 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, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG295915.
    GeneTreeiENSGT00750000117332.
    HOGENOMiHOG000217928.
    HOVERGENiHBG052484.
    InParanoidiQ6PEQ6.
    KOiK07996.
    OMAiVPPHRSV.
    OrthoDBiEOG7XPZ57.
    TreeFamiTF352396.

    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.
    IPR028697. MMP16.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021805. Pept_M10A_metallopeptidase_C.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF26. PTHR10201:SF26. 1 hit.
    PfamiPF11857. DUF3377. 1 hit.
    PF00045. 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.

    Q9WTR0-1 [UniParc]FASTAAdd to Basket

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    MILLAFSSGR RLDFVHRSGV FFLQTLLWIL CATVCGTEQY FNVEVWLQKY    50
    GYLPPTDPRM SVLRSAETMQ SALAAMQQFY GINMTGKVDR NTIDWMKKPR 100
    CGVPDQTRGS SKFNIRRKRY ALTGQKWQHK HITYSIKNVT PKVGDPETRR 150
    AIRRAFDVWQ NVTPLTFEEV PYSELENGKR DVDITIIFAS GFHGDSSPFD 200
    GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL FLVAVHELGH 250
    ALGLEHSNDP TAIMAPFYQY METDNFKLPN DDLQGIQKIY GPPDKIPPPT 300
    RPLPTVPPHR SVPPADPRRH DRPKPPRPPT GRPSYPGAKP NICDGNFNTL 350
    AILRREMFVF KDQWFWRVRN NRVMDGYPMQ ITYFWRGLPP SIDAVYENSD 400
    GNFVFFKGNK YWVFKDTTLQ PGYPHDLITL GNGIPPHGID SAIWWEDVGK 450
    TYFFKGDRYW RYSEEMKTMD PGYPKPITIW KGIPESPQGA FVHKENGFTY 500
    FYKGKEYWKF NNQILKVEPG YPRSILKDFM GCDGPTDRDK EGLSPPDDVD 550
    IVIKLDNTAS TVKAIAIVIP CILALCLLVL VYTVFQFKRK GTPRHILYCK 600
    RSMQEWV 607
    Length:607
    Mass (Da):69,571
    Last modified:July 27, 2011 - v3
    Checksum:iC4CB54F75B26A296
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171R → H in BAA78420. 1 PublicationCurated
    Sequence conflicti19 – 191G → V in AAG17704. 1 PublicationCurated
    Sequence conflicti196 – 1961S → R in AAG17704. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021228 mRNA. Translation: BAA78420.1.
    AF282844 mRNA. Translation: AAG17704.1.
    AL683877, AL805957 Genomic DNA. Translation: CAM13981.1.
    AL805957, AL683877 Genomic DNA. Translation: CAM18851.1.
    CH466538 Genomic DNA. Translation: EDL05585.1.
    CH466538 Genomic DNA. Translation: EDL05587.1.
    BC057926 mRNA. Translation: AAH57926.1.
    CCDSiCCDS17989.1.
    RefSeqiNP_062698.2. NM_019724.3.
    XP_006537704.1. XM_006537641.1.
    UniGeneiMm.187315.

    Genome annotation databases

    EnsembliENSMUST00000029881; ENSMUSP00000029881; ENSMUSG00000028226.
    GeneIDi17389.
    KEGGimmu:17389.
    UCSCiuc008sbw.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021228 mRNA. Translation: BAA78420.1 .
    AF282844 mRNA. Translation: AAG17704.1 .
    AL683877 , AL805957 Genomic DNA. Translation: CAM13981.1 .
    AL805957 , AL683877 Genomic DNA. Translation: CAM18851.1 .
    CH466538 Genomic DNA. Translation: EDL05585.1 .
    CH466538 Genomic DNA. Translation: EDL05587.1 .
    BC057926 mRNA. Translation: AAH57926.1 .
    CCDSi CCDS17989.1.
    RefSeqi NP_062698.2. NM_019724.3.
    XP_006537704.1. XM_006537641.1.
    UniGenei Mm.187315.

    3D structure databases

    ProteinModelPortali Q9WTR0.
    SMRi Q9WTR0. Positions 85-561.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000029881.

    Protein family/group databases

    MEROPSi M10.016.

    PTM databases

    PhosphoSitei Q9WTR0.

    Proteomic databases

    PRIDEi Q9WTR0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029881 ; ENSMUSP00000029881 ; ENSMUSG00000028226 .
    GeneIDi 17389.
    KEGGi mmu:17389.
    UCSCi uc008sbw.2. mouse.

    Organism-specific databases

    CTDi 4325.
    MGIi MGI:1276107. Mmp16.

    Phylogenomic databases

    eggNOGi NOG295915.
    GeneTreei ENSGT00750000117332.
    HOGENOMi HOG000217928.
    HOVERGENi HBG052484.
    InParanoidi Q6PEQ6.
    KOi K07996.
    OMAi VPPHRSV.
    OrthoDBi EOG7XPZ57.
    TreeFami TF352396.

    Enzyme and pathway databases

    Reactomei REACT_199000. Activation of Matrix Metalloproteinases.

    Miscellaneous databases

    ChiTaRSi MMP16. mouse.
    NextBioi 292008.
    PROi Q9WTR0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9WTR0.
    Bgeei Q9WTR0.
    CleanExi MM_MMP16.
    Genevestigatori Q9WTR0.

    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.
    IPR028697. MMP16.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021805. Pept_M10A_metallopeptidase_C.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF26. PTHR10201:SF26. 1 hit.
    Pfami PF11857. DUF3377. 1 hit.
    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. Seiki M., Kinoh H.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Differential localization and Triton X-100 solubility of membrane-type matrix metalloproteinases 1-3."
      Budde P., Gatsios P., Nienaber N.T., Li H., Staege M.S., Graeve L., Heinrich P.C., Frey J.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-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: 129.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiMMP16_MOUSE
    AccessioniPrimary (citable) accession number: Q9WTR0
    Secondary accession number(s): Q6PEQ6, Q9ERT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 134 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