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Q9R0S2

- MMP24_MOUSE

UniProt

Q9R0S2 - MMP24_MOUSE

Protein

Matrix metalloproteinase-24

Gene

Mmp24

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 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence (PubMed:19805319, PubMed:24952463). Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia (PubMed:19805319). Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence (PubMed:24952463). May play a role in axonal growth (PubMed:11714638). Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (PubMed:10622708).4 Publications

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi112 – 1121Zinc; in inhibited formBy similarity
    Metal bindingi255 – 2551Zinc; catalyticPROSITE-ProRule annotation
    Active sitei256 – 25611 PublicationPROSITE-ProRule annotation
    Metal bindingi259 – 2591Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi265 – 2651Zinc; catalyticPROSITE-ProRule annotation
    Sitei554 – 5552Cleavage; by furin

    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 - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM10.023.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-24 (EC:3.4.24.-)
    Short name:
    MMP-24
    Alternative name(s):
    Matrix metalloproteinase-21
    Short name:
    MMP-21
    Membrane-type matrix metalloproteinase 5
    Short name:
    MT-MMP 5
    Short name:
    MTMMP5
    Membrane-type-5 matrix metalloproteinase
    Short name:
    MT5-MMP
    Short name:
    MT5MMP
    Cleaved into the following chain:
    Gene namesi
    Name:Mmp24
    Synonyms:Mmp21, Mt5mmp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1341867. Mmp24.

    Subcellular locationi

    Chain Matrix metalloproteinase-24 : Cell membrane; Single-pass type I membrane protein. Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein
    Note: Recycled back to the plasma membrane through the trans-Golgi network via interaction with APBA3.1 Publication
    Chain Processed matrix metalloproteinase-24 : Secretedextracellular spaceextracellular matrix
    Note: Also shed from cell surface as soluble proteinase, by a proteolytic cleavage.1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Extracellular matrix, Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Mice are viable, develop normally and are fertile. They however display enhanced sensitivity to noxious thermal stimuli under basal conditions characterized by an absence of thermal inflammatory hyperalgesia (PubMed:19805319). In subependymal zone, more intense signal is observed for extracellular N-cadherin (Cdh2) as well as increased levels of full-length Cdh2 without changes in Cdh2 messenger RNA levels (PubMed:24952463).2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi256 – 2561E → A: Loss of function. Does not prevent proteolytic processing. 3 Publications
    Mutagenesisi549 – 5546Missing: Abolishes proteolytic processing. Gain of function mutant. 1 Publication
    Mutagenesisi616 – 6183Missing: Impaired recycling affecting its internalization, leading to decreased activity on the plasma surface. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Sequence AnalysisAdd
    BLAST
    Propeptidei42 – 12887By similarityPRO_0000028848Add
    BLAST
    Chaini129 – 618490Matrix metalloproteinase-24PRO_0000028849Add
    BLAST
    Chaini129 – 554426Processed matrix metalloproteinase-24CuratedPRO_0000302759Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi353 ↔ 542By similarity

    Post-translational modificationi

    Cleaved by a furin endopeptidase in the trans-Golgi network.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiQ9R0S2.
    PRIDEiQ9R0S2.

    PTM databases

    PhosphoSiteiQ9R0S2.

    Miscellaneous databases

    PMAP-CutDBQ9R0S2.

    Expressioni

    Tissue specificityi

    Mainly expressed in neuronal cells of both central and peripheral nervous systems. Expressed by CGRP-containing peptidergic nociceptors in dorsal root ganglia (PubMed:19805319). Expressed in adult neural stem cell and ependymocytes (PubMed:24952463). Expressed at low level in testis.3 Publications

    Developmental stagei

    Expressed at day 11 until day 15, before dropping around day 17 before birth. Expressed in the cerebrum in embryos, but it declines after birth, while expression in the cerebellum starts to increase postnatally and continues thereafter.1 Publication

    Gene expression databases

    ArrayExpressiQ9R0S2.
    BgeeiQ9R0S2.
    CleanExiMM_MMP21.
    MM_MMP24.
    GenevestigatoriQ9R0S2.

    Interactioni

    Subunit structurei

    Interacts with GRIP1 and GRIP2 By similarity. Interacts (via PDZ-binding motif) with APBA3 (via PDZ domain).By similarity1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R0S2.
    SMRiQ9R0S2. Positions 84-521.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini42 – 575534ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini597 – 61822CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei576 – 59621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati350 – 39849Hemopexin 1Add
    BLAST
    Repeati399 – 44446Hemopexin 2Add
    BLAST
    Repeati446 – 49449Hemopexin 3Add
    BLAST
    Repeati495 – 54248Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi110 – 1178Cysteine switchBy similarity
    Motifi616 – 6183PDZ-binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi122 – 1254Poly-Arg

    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.
    The PDZ-binding motif (also named EWV motif) is required for interaction with PDZ domains of APBA3 and recycling through the trans-Golgi network.1 Publication

    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.
    InParanoidiA2AUV7.
    KOiK08002.
    OMAiFKNKAGP.
    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.
    IPR028723. MMP24.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021805. Pept_M10A_metallopeptidase_C.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF138. PTHR10201:SF138. 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.
    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.

    Q9R0S2-1 [UniParc]FASTAAdd to Basket

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    MPRSRGGRAA PGQASRWSGW RAPGRLLPLL PALCCLAAAA GAGKPAGADA    50
    PFAGQNWLKS YGYLLPYESR ASALHSGKAL QSAVSTMQQF YGIPVTGVLD 100
    QTTIEWMKKP RCGVPDHPHL SRRRRNKRYA LTGQKWRQKH ITYSIHNYTP 150
    KVGELDTRKA IRQAFDVWQK VTPLTFEEVP YHEIKSDRKE ADIMIFFASG 200
    FHGDSSPFDG EGGFLAHAYF PGPGIGGDTH FDSDEPWTLG NANHDGNDLF 250
    LVAVHELGHA LGLEHSNDPS AIMAPFYQYM ETHNFKLPQD DLQGIQKIYG 300
    PPAEPLEPTR PLPTLPVRRI HSPSERKHER HPRPPRPPLG DRPSTPGAKP 350
    NICDGNFNTV ALFRGEMFVF KDRWFWRLRN NRVQEGYPMQ IEQFWKGLPA 400
    RIDAAYERAD GRFVFFKGDK YWVFKEVTVE PGYPHSLGEL GSCLPREGID 450
    TALRWEPVGK TYFFKGERYW RYSEERRATD PGYPKPITVW KGIPQAPQGA 500
    FISKEGYYTY FYKGRDYWKF DNQKLSVEPG YPRNILRDWM GCKQKEVERR 550
    KERRLPQDDV DIMVTIDDVP GSVNAVAVVV PCTLSLCLLV LLYTIFQFKN 600
    KAGPQPVTYY KRPVQEWV 618
    Length:618
    Mass (Da):70,460
    Last modified:July 27, 2011 - v2
    Checksum:i51C8E61B187264F5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 2822GRAAP…GRLLP → AALRRARPRAGALAGPGAAA in CAA09055. (PubMed:10085137)CuratedAdd
    BLAST
    Sequence conflicti44 – 507KPAGADA → SRPGR in CAA09055. (PubMed:10085137)Curated
    Sequence conflicti46 – 461A → T in BAA82966. 1 PublicationCurated
    Sequence conflicti306 – 3083LEP → SGA in CAA09055. (PubMed:10085137)Curated
    Sequence conflicti326 – 3261R → K in CAA09055. (PubMed:10085137)Curated
    Sequence conflicti337 – 3415PPLGD → RPWG in CAA09055. (PubMed:10085137)Curated
    Sequence conflicti449 – 4491I → KP in CAA09055. (PubMed:10085137)Curated
    Sequence conflicti502 – 5021I → L in CAA09055. (PubMed:10085137)Curated
    Sequence conflicti589 – 5891L → R in CAA09055. (PubMed:10085137)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021226 mRNA. Translation: BAA82966.1.
    AJ010262 mRNA. Translation: CAA09055.1.
    AL929233 Genomic DNA. Translation: CAM22837.1.
    CCDSiCCDS16955.1.
    RefSeqiNP_034938.3. NM_010808.3.
    UniGeneiMm.330707.
    Mm.389325.

    Genome annotation databases

    EnsembliENSMUST00000029141; ENSMUSP00000029141; ENSMUSG00000027612.
    GeneIDi17391.
    KEGGimmu:17391.
    UCSCiuc008nlj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021226 mRNA. Translation: BAA82966.1 .
    AJ010262 mRNA. Translation: CAA09055.1 .
    AL929233 Genomic DNA. Translation: CAM22837.1 .
    CCDSi CCDS16955.1.
    RefSeqi NP_034938.3. NM_010808.3.
    UniGenei Mm.330707.
    Mm.389325.

    3D structure databases

    ProteinModelPortali Q9R0S2.
    SMRi Q9R0S2. Positions 84-521.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M10.023.

    PTM databases

    PhosphoSitei Q9R0S2.

    Proteomic databases

    PaxDbi Q9R0S2.
    PRIDEi Q9R0S2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029141 ; ENSMUSP00000029141 ; ENSMUSG00000027612 .
    GeneIDi 17391.
    KEGGi mmu:17391.
    UCSCi uc008nlj.1. mouse.

    Organism-specific databases

    CTDi 10893.
    MGIi MGI:1341867. Mmp24.

    Phylogenomic databases

    eggNOGi NOG295915.
    GeneTreei ENSGT00750000117332.
    HOGENOMi HOG000217928.
    HOVERGENi HBG052484.
    InParanoidi A2AUV7.
    KOi K08002.
    OMAi FKNKAGP.
    OrthoDBi EOG7XPZ57.
    TreeFami TF352396.

    Miscellaneous databases

    NextBioi 292016.
    PMAP-CutDB Q9R0S2.
    PROi Q9R0S2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9R0S2.
    Bgeei Q9R0S2.
    CleanExi MM_MMP21.
    MM_MMP24.
    Genevestigatori Q9R0S2.

    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.
    IPR028723. MMP24.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021805. Pept_M10A_metallopeptidase_C.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF138. PTHR10201:SF138. 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 PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a new membrane-type matrix metalloproteinase, MT5-MMP, that is expressed predominantly in cerebellum."
      Seiki M.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MMP."
      Pei D.Q.
      J. Biol. Chem. 274:8925-8932(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLU-256, ACTIVE SITE.
      Strain: BALB/c.
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "Expression, purification and characterization of recombinant mouse MT5-MMP protein products."
      Wang X., Yi J., Lei J., Pei D.Q.
      FEBS Lett. 462:261-266(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Shedding of membrane type matrix metalloproteinase 5 by a furin-type convertase: a potential mechanism for down-regulation."
      Wang X., Pei D.
      J. Biol. Chem. 276:35953-35960(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF GLU-256 AND 549-ARG--ARG-555.
    6. "Membrane-type 5 matrix metalloproteinase is expressed in differentiated neurons and regulates axonal growth."
      Hayashita-Kinoh H., Kinoh H., Okada A., Komori K., Itoh Y., Chiba T., Kajita M., Yana I., Seiki M.
      Cell Growth Differ. 12:573-580(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    7. "Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV."
      Wang P., Wang X., Pei D.
      J. Biol. Chem. 279:20461-20470(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH APBA3, MUTAGENESIS OF 616-GLU--VAL-618.
    8. Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    9. "MT5-MMP regulates adult neural stem cell functional quiescence through the cleavage of N-cadherin."
      Porlan E., Marti-Prado B., Morante-Redolat J.M., Consiglio A., Delgado A.C., Kypta R., Lopez-Otin C., Kirstein M., Farinas I.
      Nat. Cell Biol. 16:629-638(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiMMP24_MOUSE
    AccessioniPrimary (citable) accession number: Q9R0S2
    Secondary accession number(s): A2AUV7, Q9Z0J9
    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 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. 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