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Q10739

- MMP14_RAT

UniProt

Q10739 - MMP14_RAT

Protein

Matrix metalloproteinase-14

Gene

Mmp14

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    Functioni

    Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7 By similarity. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues By similarity.By similarity

    Catalytic activityi

    Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi93 – 931Zinc; in inhibited formBy similarity
    Metal bindingi239 – 2391Zinc; catalyticPROSITE-ProRule annotation
    Active sitei240 – 2401PROSITE-ProRule annotation
    Metal bindingi243 – 2431Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi249 – 2491Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. integrin binding Source: RGD
    3. metalloendopeptidase activity Source: InterPro
    4. peptidase activator activity Source: RGD
    5. sequence-specific DNA binding transcription factor activity Source: Ensembl
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: RGD
    2. astrocyte cell migration Source: RGD
    3. branching morphogenesis of an epithelial tube Source: Ensembl
    4. endothelial cell proliferation Source: RGD
    5. lung development Source: Ensembl
    6. male gonad development Source: RGD
    7. negative regulation of focal adhesion assembly Source: RGD
    8. ossification Source: RGD
    9. ovarian follicle development Source: RGD
    10. positive regulation of cell growth Source: Ensembl
    11. positive regulation of cell migration Source: Ensembl
    12. positive regulation of peptidase activity Source: GOC
    13. response to estrogen Source: RGD
    14. response to hormone Source: RGD
    15. response to hypoxia Source: RGD
    16. response to mechanical stimulus Source: RGD
    17. response to organic cyclic compound Source: RGD
    18. response to oxidative stress Source: RGD
    19. tissue remodeling Source: RGD
    20. zymogen activation Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198590. Activation of Matrix Metalloproteinases.
    REACT_199177. Collagen degradation.
    REACT_199178. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiM10.014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-14 (EC:3.4.24.80)
    Short name:
    MMP-14
    Alternative name(s):
    Membrane-type matrix metalloproteinase 1
    Short name:
    MT-MMP 1
    Short name:
    MTMMP1
    Membrane-type-1 matrix metalloproteinase
    Short name:
    MT-MMP
    Short name:
    MT1-MMP
    Short name:
    MT1MMP
    Gene namesi
    Name:Mmp14
    Synonyms:Mtmmp
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 15

    Organism-specific databases

    RGDi620198. Mmp14.

    Subcellular locationi

    Membrane Curated; Single-pass type I membrane protein Curated. Melanosome By similarity. Cytoplasm By similarity
    Note: Forms a complex with BST2 and localizes to the cytoplasm.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. extracellular matrix Source: InterPro
    3. integral component of membrane Source: UniProtKB-KW
    4. melanosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 11191Activation peptidePRO_0000028806Add
    BLAST
    Chaini112 – 582471Matrix metalloproteinase-14PRO_0000028807Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi319 ↔ 508By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Zymogen

    Proteomic databases

    PRIDEiQ10739.

    PTM databases

    PhosphoSiteiQ10739.

    Expressioni

    Gene expression databases

    GenevestigatoriQ10739.

    Interactioni

    Subunit structurei

    Interacts (via C-terminal cytoplasmic tail) with BST2.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000049168.

    Structurei

    3D structure databases

    ProteinModelPortaliQ10739.
    SMRiQ10739. Positions 114-287.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini112 – 541430ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini563 – 58220CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei542 – 56221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati316 – 36449Hemopexin 1Add
    BLAST
    Repeati365 – 41046Hemopexin 2Add
    BLAST
    Repeati412 – 46049Hemopexin 3Add
    BLAST
    Repeati461 – 50848Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi91 – 988Cysteine 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.
    InParanoidiQ10739.
    KOiK07763.
    OMAiWMGCPSG.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiQ10739.
    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.
    IPR028693. MMP14.
    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:SF24. PTHR10201:SF24. 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.

    Q10739-1 [UniParc]FASTAAdd to Basket

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    MSPAPRPSRS LLLPLLTLGT TLASLGWAQS SNFSPEAWLQ QYGYLPPGDL    50
    RTHTQRSPQS LSAAIAAMQR FYGLQVTGKA DSDTMKAMRR PRCGVPDKFG 100
    TEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT FEAIRKAFRV 150
    WESATPLRFR EVPYAYIREG HEKQADIMIL FAEGFHGDST PFDGEGGFLA 200
    HAYFPGPNIG GDTHFDSAEP WTVQNEDLNG NDIFLVAVHE LGHALGLEHS 250
    NDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGSKSGSP TKMPPQPRTT 300
    SRPSVPDKPR NPTYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM 350
    DGYPMPIGQF WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP 400
    KHIKELGRGL PTDKIDAALF WMPNGKTYFF RGNKYYRFNE EFRAVDSEYP 450
    KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG NKYWKFNNQK LKVEPGYPKS 500
    ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGSGAVSAA AVVLPVLLLL 550
    LVLAVGLAVF FFRRHGTPKR LLYCQRSLLD KV 582
    Length:582
    Mass (Da):66,080
    Last modified:May 1, 2007 - v2
    Checksum:i48F1A8E3065E1AE8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681M → I in CAA58521. (PubMed:7708715)Curated
    Sequence conflicti255 – 2551A → D in CAA58521. (PubMed:7708715)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83537 mRNA. Translation: CAA58521.1.
    X91785 mRNA. Translation: CAA62897.1.
    BC072509 mRNA. Translation: AAH72509.1.
    PIRiI84471.
    RefSeqiNP_112318.1. NM_031056.1.
    UniGeneiRn.10371.

    Genome annotation databases

    EnsembliENSRNOT00000042938; ENSRNOP00000049168; ENSRNOG00000010947.
    ENSRNOT00000075610; ENSRNOP00000065434; ENSRNOG00000010947.
    GeneIDi81707.
    KEGGirno:81707.
    UCSCiRGD:620198. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83537 mRNA. Translation: CAA58521.1 .
    X91785 mRNA. Translation: CAA62897.1 .
    BC072509 mRNA. Translation: AAH72509.1 .
    PIRi I84471.
    RefSeqi NP_112318.1. NM_031056.1.
    UniGenei Rn.10371.

    3D structure databases

    ProteinModelPortali Q10739.
    SMRi Q10739. Positions 114-287.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000049168.

    Protein family/group databases

    MEROPSi M10.014.

    PTM databases

    PhosphoSitei Q10739.

    Proteomic databases

    PRIDEi Q10739.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000042938 ; ENSRNOP00000049168 ; ENSRNOG00000010947 .
    ENSRNOT00000075610 ; ENSRNOP00000065434 ; ENSRNOG00000010947 .
    GeneIDi 81707.
    KEGGi rno:81707.
    UCSCi RGD:620198. rat.

    Organism-specific databases

    CTDi 4323.
    RGDi 620198. Mmp14.

    Phylogenomic databases

    eggNOGi NOG295915.
    GeneTreei ENSGT00750000117332.
    HOGENOMi HOG000217928.
    HOVERGENi HBG052484.
    InParanoidi Q10739.
    KOi K07763.
    OMAi WMGCPSG.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi Q10739.
    TreeFami TF352396.

    Enzyme and pathway databases

    Reactomei REACT_198590. Activation of Matrix Metalloproteinases.
    REACT_199177. Collagen degradation.
    REACT_199178. Degradation of the extracellular matrix.

    Miscellaneous databases

    NextBioi 615328.
    PROi Q10739.

    Gene expression databases

    Genevestigatori Q10739.

    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.
    IPR028693. MMP14.
    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:SF24. PTHR10201:SF24. 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. "Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas."
      Okada A., Bellocq J.-P., Rouyer N., Chenard M.P., Rio M.C., Chambon P., Basset P.
      Proc. Natl. Acad. Sci. U.S.A. 92:2730-2734(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Expression and function of MT-MMP in glial cells."
      Cossins J., Clements J., Catlin G., Wells G.
      Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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: Heart.

    Entry informationi

    Entry nameiMMP14_RAT
    AccessioniPrimary (citable) accession number: Q10739
    Secondary accession number(s): Q6IN06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 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