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Q9JHI0

- MMP19_MOUSE

UniProt

Q9JHI0 - MMP19_MOUSE

Protein

Matrix metalloproteinase-19

Gene

Mmp19

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 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis By similarity. Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin By similarity.By similarity

    Catalytic activityi

    Cleaves aggrecan at the 360-Ser-|-Phe-361 site.

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi86 – 861Zinc; in inhibited formBy similarity
    Metal bindingi213 – 2131Zinc; catalyticPROSITE-ProRule annotation
    Active sitei214 – 2141PROSITE-ProRule annotation
    Metal bindingi217 – 2171Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi223 – 2231Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell differentiation Source: UniProtKB-KW
    3. collagen catabolic process Source: UniProtKB-KW
    4. luteolysis Source: Ensembl
    5. ovarian follicle development Source: Ensembl
    6. ovulation from ovarian follicle Source: Ensembl
    7. response to cAMP Source: Ensembl
    8. response to hormone Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Angiogenesis, Collagen degradation, Differentiation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199052. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiM10.021.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-19 (EC:3.4.24.-)
    Short name:
    MMP-19
    Alternative name(s):
    Matrix metalloproteinase RASI
    Gene namesi
    Name:Mmp19
    Synonyms:Rasi
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1927899. Mmp19.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Extracellular matrix, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 9880By similarityPRO_0000028828Add
    BLAST
    Chaini99 – 512414Matrix metalloproteinase-19PRO_0000028829Add
    BLAST
    Propeptidei513 – 52715Removed in mature formSequence AnalysisPRO_0000028830Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi289 ↔ 471By similarity
    Glycosylationi464 – 4641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi479 – 4791N-linked (GlcNAc...)Sequence Analysis
    Lipidationi512 – 5121GPI-anchor amidated aspartateSequence Analysis
    Glycosylationi521 – 5211N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Activated by autolytic cleavage after Lys-98.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

    Proteomic databases

    MaxQBiQ9JHI0.
    PRIDEiQ9JHI0.

    PTM databases

    PhosphoSiteiQ9JHI0.

    Expressioni

    Tissue specificityi

    Highly expressed in the liver. Expressed in the arterial tunica media of large blood vessels.

    Developmental stagei

    Expressed in proliferating chondrocytes in the chondroepiphysis during musculoskeletal development.

    Gene expression databases

    ArrayExpressiQ9JHI0.
    BgeeiQ9JHI0.
    CleanExiMM_MMP19.
    GenevestigatoriQ9JHI0.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000026411.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JHI0.
    SMRiQ9JHI0. Positions 39-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati286 – 33348Hemopexin 1Add
    BLAST
    Repeati334 – 37239Hemopexin 2Add
    BLAST
    Repeati377 – 42549Hemopexin 3Add
    BLAST
    Repeati426 – 47146Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi84 – 918Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi266 – 2716Poly-Glu

    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.
    GeneTreeiENSGT00730000110806.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiQ9JHI0.
    KOiK07998.
    OMAiVAKGYPR.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiQ9JHI0.
    TreeFamiTF315428.

    Family and domain databases

    Gene3Di1.10.101.10. 1 hit.
    2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR028724. MMP19.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF117. PTHR10201:SF117. 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.

    Q9JHI0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDWQQLWLAF LLPMTVSGRA LGPTEKEAVL DYLLQYGYLQ KPLEGADDFR    50
    LEDITEALRT FQEASGLPIS GQMDDATRAR MKQPRCGLED PFNQKSLKYL 100
    LLGHWRKKNL TFRIFNVPST LSLPRVRAAL HQAFKYWSSV APLTFREVKA 150
    GWADIRLSFH GRQSLYCSNT FDGPGKVLAH ADIPELGSIH FDKDELWTEG 200
    TYQGVNLRII AAHEVGHALG LGHSRYTQAL MAPVYAGYQP FFKLHPDDVA 250
    GIQALYGKRS PETRDEEEET EMLTVSPVTA KPGPMPNPCS GEVDAMVLGP 300
    RGKTYAFKGD YVWTVTDSGP GPLFQISALW EGLPGNLDAA VYSPRTRRTH 350
    FFKGNKVWRY VDFKMSPGFP MKFNRVEPNL DAALYWPVNQ KVFLFKGSGY 400
    WQWDELARTD LSRYPKPIKE LFTGVPDRPS AAMSWQDGQV YFFKGKEYWR 450
    LNQQLRVAKG YPRNTTHWMH CGSQTPDTNS STGDVTPSTT DTVLGTTPST 500
    MGSTLDIPSA TDSASLSFSA NVTLLGA 527
    Length:527
    Mass (Da):59,122
    Last modified:October 1, 2000 - v1
    Checksum:i8AD0AE41A1CD335E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF155221 mRNA. Translation: AAF73292.1.
    AF162446 mRNA. Translation: AAF80464.1.
    AF153199 mRNA. Translation: AAG29880.1.
    AK086808 mRNA. Translation: BAC39747.1.
    CCDSiCCDS24292.1.
    RefSeqiNP_067387.1. NM_021412.2.
    UniGeneiMm.131266.

    Genome annotation databases

    EnsembliENSMUST00000026411; ENSMUSP00000026411; ENSMUSG00000025355.
    GeneIDi58223.
    KEGGimmu:58223.
    UCSCiuc007hof.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF155221 mRNA. Translation: AAF73292.1 .
    AF162446 mRNA. Translation: AAF80464.1 .
    AF153199 mRNA. Translation: AAG29880.1 .
    AK086808 mRNA. Translation: BAC39747.1 .
    CCDSi CCDS24292.1.
    RefSeqi NP_067387.1. NM_021412.2.
    UniGenei Mm.131266.

    3D structure databases

    ProteinModelPortali Q9JHI0.
    SMRi Q9JHI0. Positions 39-473.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000026411.

    Protein family/group databases

    MEROPSi M10.021.

    PTM databases

    PhosphoSitei Q9JHI0.

    Proteomic databases

    MaxQBi Q9JHI0.
    PRIDEi Q9JHI0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026411 ; ENSMUSP00000026411 ; ENSMUSG00000025355 .
    GeneIDi 58223.
    KEGGi mmu:58223.
    UCSCi uc007hof.1. mouse.

    Organism-specific databases

    CTDi 4327.
    MGIi MGI:1927899. Mmp19.

    Phylogenomic databases

    eggNOGi NOG295915.
    GeneTreei ENSGT00730000110806.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi Q9JHI0.
    KOi K07998.
    OMAi VAKGYPR.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi Q9JHI0.
    TreeFami TF315428.

    Enzyme and pathway databases

    Reactomei REACT_199052. Degradation of the extracellular matrix.

    Miscellaneous databases

    NextBioi 314237.
    PROi Q9JHI0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JHI0.
    Bgeei Q9JHI0.
    CleanExi MM_MMP19.
    Genevestigatori Q9JHI0.

    Family and domain databases

    Gene3Di 1.10.101.10. 1 hit.
    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.
    IPR028724. MMP19.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF117. PTHR10201:SF117. 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. "Characterization, expression analysis and chromosomal mapping of mouse matrix metalloproteinase-19 (MMP-19)."
      Caterina J.J., Shi J., Kozak C.A., Engler J.A., Birkedal-Hansen H.
      Mol. Biol. Rep. 27:73-79(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C3H.
    2. "Mmp19 encodes a GPI anchored matrix metalloprotease expressed in musculoskeletal, neural and epithelial tissues."
      Hurskainen T., Seldin M.F., Pendas A., Lopez-Otin C., Apte S.S.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The murine ortholog of matrix metalloproteinase 19: its cloning, gene organization, and expression."
      Mueller M.S., Harnasch M., Kolb C., Kusch J., Sadowski T., Sedlacek R.
      Gene 256:101-111(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129/Ola.
    4. "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] OF 54-527.
      Strain: C57BL/6J.
      Tissue: Lung.

    Entry informationi

    Entry nameiMMP19_MOUSE
    AccessioniPrimary (citable) accession number: Q9JHI0
    Secondary accession number(s): Q8C360
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 134 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. 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