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P53690

- MMP14_MOUSE

UniProt

P53690 - MMP14_MOUSE

Protein

Matrix metalloproteinase-14

Gene

Mmp14

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 139 (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. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. 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. metalloendopeptidase activity Source: InterPro
    3. peptidase activator activity Source: Ensembl
    4. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: Ensembl
    2. astrocyte cell migration Source: Ensembl
    3. bone development Source: MGI
    4. branching morphogenesis of an epithelial tube Source: MGI
    5. cell migration Source: MGI
    6. chondrocyte proliferation Source: MGI
    7. collagen catabolic process Source: MGI
    8. craniofacial suture morphogenesis Source: MGI
    9. embryonic cranial skeleton morphogenesis Source: MGI
    10. endochondral ossification Source: MGI
    11. endothelial cell proliferation Source: Ensembl
    12. lung development Source: MGI
    13. male gonad development Source: Ensembl
    14. negative regulation of focal adhesion assembly Source: Ensembl
    15. ossification Source: MGI
    16. ovarian follicle development Source: Ensembl
    17. positive regulation of cell growth Source: Ensembl
    18. positive regulation of cell migration Source: Ensembl
    19. regulation of transcription, DNA-templated Source: GOC
    20. response to estrogen Source: Ensembl
    21. response to hypoxia Source: Ensembl
    22. response to mechanical stimulus Source: Ensembl
    23. response to oxidative stress Source: Ensembl
    24. tissue remodeling Source: Ensembl
    25. zymogen activation 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.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.

    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):
    MMP-X1
    MT-MMP
    Membrane-type matrix metalloproteinase 1
    Short name:
    MT-MMP 1
    Short name:
    MTMMP1
    Membrane-type-1 matrix metalloproteinase
    Short name:
    MT1-MMP
    Short name:
    MT1MMP
    Gene namesi
    Name:Mmp14
    Synonyms:Mtmmp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:101900. Mmp14.

    Subcellular locationi

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

    GO - Cellular componenti

    1. extracellular matrix Source: InterPro
    2. integral component of membrane Source: UniProtKB-KW
    3. 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 – 11191By similarityPRO_0000028800Add
    BLAST
    Chaini112 – 582471Matrix metalloproteinase-14PRO_0000028801Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Zymogen

    Proteomic databases

    MaxQBiP53690.
    PRIDEiP53690.

    PTM databases

    PhosphoSiteiP53690.

    Expressioni

    Tissue specificityi

    Highly expressed in placenta, kidney, heart, lung, embryonic skeletal and periskeletal tissues.

    Developmental stagei

    Not detected before day 10.5. At day 12.5, prominently expressed in large arteries and the umbilical arteries, expressed at lower levels in the myocardium, craniofacial mesenchyme, nasal epithelium and liver capsule. At days 14.5 and 17.5, expressed in the musculoskeletal system, and ossification areas, with continued expression in the arterial tunica media.

    Gene expression databases

    ArrayExpressiP53690.
    BgeeiP53690.
    CleanExiMM_MMP14.
    GenevestigatoriP53690.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiP53690. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP53690.
    SMRiP53690. Positions 65-511.
    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.
    InParanoidiQ8BTX2.
    KOiK07763.
    OMAiWMGCPSG.
    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.
    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.

    P53690-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPAPRPSRS LLLPLLTLGT ALASLGWAQG SNFSPEAWLQ QYGYLPPGDL    50
    RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DLATMMAMRR 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
    SRPSVPDKPK NPAYGPNICD 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):65,919
    Last modified:July 27, 2011 - v3
    Checksum:i6CA95CFD5811B093
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti133 – 1331P → S in AAB86602. (PubMed:9325265)Curated
    Sequence conflicti255 – 2551A → D in CAA58520. (PubMed:7708715)Curated
    Sequence conflicti258 – 2581A → S in CAA58520. (PubMed:7708715)Curated
    Sequence conflicti258 – 2581A → S in AAB51753. (PubMed:9648071)Curated
    Sequence conflicti341 – 3411F → L in CAA58520. (PubMed:7708715)Curated
    Sequence conflicti346 – 3461N → P in AAB86602. (PubMed:9325265)Curated
    Sequence conflicti378 – 3781K → T in CAA58520. (PubMed:7708715)Curated
    Sequence conflicti390 – 3912FD → CV in CAA58520. (PubMed:7708715)Curated
    Sequence conflicti400 – 4012PK → AN in CAA58520. (PubMed:7708715)Curated
    Sequence conflicti407 – 4071G → V in CAA58520. (PubMed:7708715)Curated
    Sequence conflicti412 – 4121T → S in CAA58520. (PubMed:7708715)Curated
    Sequence conflicti417 – 4171A → T in CAA58520. (PubMed:7708715)Curated
    Sequence conflicti512 – 5121G → R in AAB51753. (PubMed:9648071)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83536 mRNA. Translation: CAA58520.2.
    AF022432
    , AF022424, AF022425, AF022426, AF022427, AF022428, AF022429, AF022430, AF022431 Genomic DNA. Translation: AAB86602.1.
    U54984 mRNA. Translation: AAB51753.1.
    DQ249870 mRNA. Translation: ABB45784.1.
    AK088476 mRNA. Translation: BAC40377.1.
    AK138611 mRNA. Translation: BAE23719.1.
    AK149907 mRNA. Translation: BAE29158.1.
    AK149988 mRNA. Translation: BAE29216.1.
    AK165014 mRNA. Translation: BAE38000.1.
    CH466535 Genomic DNA. Translation: EDL36348.1.
    CCDSiCCDS36922.1.
    PIRiI48673.
    RefSeqiNP_032634.3. NM_008608.3.
    UniGeneiMm.280175.
    Mm.486486.

    Genome annotation databases

    EnsembliENSMUST00000089688; ENSMUSP00000087119; ENSMUSG00000000957.
    GeneIDi17387.
    KEGGimmu:17387.
    UCSCiuc007twc.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83536 mRNA. Translation: CAA58520.2 .
    AF022432
    , AF022424 , AF022425 , AF022426 , AF022427 , AF022428 , AF022429 , AF022430 , AF022431 Genomic DNA. Translation: AAB86602.1 .
    U54984 mRNA. Translation: AAB51753.1 .
    DQ249870 mRNA. Translation: ABB45784.1 .
    AK088476 mRNA. Translation: BAC40377.1 .
    AK138611 mRNA. Translation: BAE23719.1 .
    AK149907 mRNA. Translation: BAE29158.1 .
    AK149988 mRNA. Translation: BAE29216.1 .
    AK165014 mRNA. Translation: BAE38000.1 .
    CH466535 Genomic DNA. Translation: EDL36348.1 .
    CCDSi CCDS36922.1.
    PIRi I48673.
    RefSeqi NP_032634.3. NM_008608.3.
    UniGenei Mm.280175.
    Mm.486486.

    3D structure databases

    ProteinModelPortali P53690.
    SMRi P53690. Positions 65-511.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P53690. 1 interaction.

    Protein family/group databases

    MEROPSi M10.014.

    PTM databases

    PhosphoSitei P53690.

    Proteomic databases

    MaxQBi P53690.
    PRIDEi P53690.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000089688 ; ENSMUSP00000087119 ; ENSMUSG00000000957 .
    GeneIDi 17387.
    KEGGi mmu:17387.
    UCSCi uc007twc.2. mouse.

    Organism-specific databases

    CTDi 4323.
    MGIi MGI:101900. Mmp14.

    Phylogenomic databases

    eggNOGi NOG295915.
    GeneTreei ENSGT00750000117332.
    HOGENOMi HOG000217928.
    HOVERGENi HBG052484.
    InParanoidi Q8BTX2.
    KOi K07763.
    OMAi WMGCPSG.
    OrthoDBi EOG7XPZ57.
    TreeFami TF352396.

    Enzyme and pathway databases

    Reactomei REACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.

    Miscellaneous databases

    ChiTaRSi MMP14. mouse.
    NextBioi 292000.
    PROi P53690.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53690.
    Bgeei P53690.
    CleanExi MM_MMP14.
    Genevestigatori P53690.

    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. Odaka A.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "The matrix metalloproteinase-14 (MMP-14) gene is structurally distinct from other MMP genes and is co-expressed with the TIMP-2 gene during mouse embryogenesis."
      Apte S.S., Fukai N., Beier D.R., Olsen B.R.
      J. Biol. Chem. 272:25511-25517(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
    4. "Cloning of murine membrane-type-1-matrix metalloproteinase (MT-1-MMP) and its metanephric developmental regulation with respect to MMP-2 and its inhibitor."
      Ota K., Stetler-Stevenson W.G., Yang Q., Kumar A., Wada J., Kashihara N., Wallner E.I., Kanwar Y.S.
      Kidney Int. 54:131-142(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: CD-1.
      Tissue: Kidney.
    5. "Interference with the complement system by tumor cell membrane type-1 matrix metalloproteinase plays a significant role in promoting metastasis in mice."
      Rozanov D.V., Savinov A.Y., Golubkov V.S., Tomlinson S., Strongin A.Y.
      Cancer Res. 66:6258-6263(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: FVB/N.
    6. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow, Eye, Spinal cord and Thymus.
    7. 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].
    8. "MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover."
      Holmbeck K., Bianco P., Caterina J., Yamada S., Kromer M., Kuznetsov S.A., Mankani M., Robey P.G., Poole A.R., Pidoux I., Ward J.M., Birkedal-Hansen H.
      Cell 99:81-92(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiMMP14_MOUSE
    AccessioniPrimary (citable) accession number: P53690
    Secondary accession number(s): O08645, O35369, Q8BTX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 139 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