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Q9Y5R2

- MMP24_HUMAN

UniProt

Q9Y5R2 - MMP24_HUMAN

Protein

Matrix metalloproteinase-24

Gene

MMP24

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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. 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. 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. May play a role in axonal growth. 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 By similarity.By similarity

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi139 – 1391Zinc; in inhibited formBy similarity
    Metal bindingi282 – 2821Zinc; catalyticPROSITE-ProRule annotation
    Active sitei283 – 2831PROSITE-ProRule annotation
    Metal bindingi286 – 2861Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi292 – 2921Zinc; catalyticPROSITE-ProRule annotation
    Sitei581 – 5822Cleavage; by furinBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. enzyme activator activity Source: ProtInc
    3. metalloendopeptidase activity Source: ProtInc
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. positive regulation of catalytic activity Source: GOC
    2. proteolysis Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118682. Activation of Matrix Metalloproteinases.

    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):
    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:MT5MMP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:7172. MMP24.

    Subcellular locationi

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

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of plasma membrane Source: ProtInc
    3. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30881.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 5252Sequence AnalysisAdd
    BLAST
    Propeptidei53 – 155103By similarityPRO_0000028846Add
    BLAST
    Chaini156 – 645490Matrix metalloproteinase-24PRO_0000028847Add
    BLAST
    Chaini156 – 581426Processed matrix metalloproteinase-24By similarityPRO_0000302758Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi380 ↔ 569By similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiQ9Y5R2.
    PRIDEiQ9Y5R2.

    PTM databases

    PhosphoSiteiQ9Y5R2.

    Expressioni

    Tissue specificityi

    Predominantly expressed in brain, kidney, pancreas and lung. Overexpressed in a series of brain tumors, including astrocytomas and glioblastomas.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y5R2.
    BgeeiQ9Y5R2.
    CleanExiHS_MMP24.
    GenevestigatoriQ9Y5R2.

    Organism-specific databases

    HPAiHPA049280.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiQ9Y5R2. 1 interaction.
    MINTiMINT-7897838.
    STRINGi9606.ENSP00000246186.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y5R2.
    SMRiQ9Y5R2. Positions 111-548.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini53 – 602550ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini624 – 64522CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei603 – 62321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati377 – 42549Hemopexin 1Add
    BLAST
    Repeati426 – 47146Hemopexin 2Add
    BLAST
    Repeati473 – 52149Hemopexin 3Add
    BLAST
    Repeati522 – 56948Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi137 – 1448Cysteine switchBy similarity
    Motifi643 – 6453PDZ-binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi149 – 1524Poly-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.By similarity

    Sequence similaritiesi

    Belongs to the peptidase M10A family.Curated
    Contains 4 hemopexin repeats.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG295915.
    HOGENOMiHOG000217928.
    HOVERGENiHBG052484.
    InParanoidiQ9Y5R2.
    KOiK08002.
    OMAiFKNKAGP.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiQ9Y5R2.
    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.

    Q9Y5R2-1 [UniParc]FASTAAdd to Basket

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    MPRSRGGRAA PGPPPPPPPP GQAPRWSRWR VPGRLLLLLL PALCCLPGAA    50
    RAAAAAAGAG NRAAVAVAVA RADEAEAPFA GQNWLKSYGY LLPYDSRASA 100
    LHSAKALQSA VSTMQQFYGI PVTGVLDQTT IEWMKKPRCG VPDHPHLSRR 150
    RRNKRYALTG QKWRQKHITY SIHNYTPKVG ELDTRKAIRQ AFDVWQKVTP 200
    LTFEEVPYHE IKSDRKEADI MIFFASGFHG DSSPFDGEGG FLAHAYFPGP 250
    GIGGDTHFDS DEPWTLGNAN HDGNDLFLVA VHELGHALGL EHSSDPSAIM 300
    APFYQYMETH NFKLPQDDLQ GIQKIYGPPA EPLEPTRPLP TLPVRRIHSP 350
    SERKHERQPR PPRPPLGDRP STPGTKPNIC DGNFNTVALF RGEMFVFKDR 400
    WFWRLRNNRV QEGYPMQIEQ FWKGLPARID AAYERADGRF VFFKGDKYWV 450
    FKEVTVEPGY PHSLGELGSC LPREGIDTAL RWEPVGKTYF FKGERYWRYS 500
    EERRATDPGY PKPITVWKGI PQAPQGAFIS KEGYYTYFYK GRDYWKFDNQ 550
    KLSVEPGYPR NILRDWMGCN QKEVERRKER RLPQDDVDIM VTINDVPGSV 600
    NAVAVVIPCI LSLCILVLVY TIFQFKNKTG PQPVTYYKRP VQEWV 645
    Length:645
    Mass (Da):73,231
    Last modified:November 1, 1999 - v1
    Checksum:i06B2B76EA3DABB9D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti564 – 5641R → H.
    Corresponds to variant rs751887 [ dbSNP | Ensembl ].
    VAR_060166

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF131284 mRNA. Translation: AAD42962.1.
    AB021227 mRNA. Translation: BAA82967.1.
    AL121753 Genomic DNA. Translation: CAX12722.1.
    CCDSiCCDS46593.1.
    RefSeqiNP_006681.1. NM_006690.3.
    UniGeneiHs.715494.

    Genome annotation databases

    EnsembliENST00000246186; ENSP00000246186; ENSG00000125966.
    GeneIDi10893.
    KEGGihsa:10893.
    UCSCiuc002xbu.2. human.

    Polymorphism databases

    DMDMi12585280.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF131284 mRNA. Translation: AAD42962.1 .
    AB021227 mRNA. Translation: BAA82967.1 .
    AL121753 Genomic DNA. Translation: CAX12722.1 .
    CCDSi CCDS46593.1.
    RefSeqi NP_006681.1. NM_006690.3.
    UniGenei Hs.715494.

    3D structure databases

    ProteinModelPortali Q9Y5R2.
    SMRi Q9Y5R2. Positions 111-548.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9Y5R2. 1 interaction.
    MINTi MINT-7897838.
    STRINGi 9606.ENSP00000246186.

    Chemistry

    BindingDBi Q9Y5R2.
    ChEMBLi CHEMBL5050.

    Protein family/group databases

    MEROPSi M10.023.

    PTM databases

    PhosphoSitei Q9Y5R2.

    Polymorphism databases

    DMDMi 12585280.

    Proteomic databases

    PaxDbi Q9Y5R2.
    PRIDEi Q9Y5R2.

    Protocols and materials databases

    DNASUi 10893.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000246186 ; ENSP00000246186 ; ENSG00000125966 .
    GeneIDi 10893.
    KEGGi hsa:10893.
    UCSCi uc002xbu.2. human.

    Organism-specific databases

    CTDi 10893.
    GeneCardsi GC20P033814.
    HGNCi HGNC:7172. MMP24.
    HPAi HPA049280.
    MIMi 604871. gene.
    neXtProti NX_Q9Y5R2.
    PharmGKBi PA30881.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295915.
    HOGENOMi HOG000217928.
    HOVERGENi HBG052484.
    InParanoidi Q9Y5R2.
    KOi K08002.
    OMAi FKNKAGP.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi Q9Y5R2.
    TreeFami TF352396.

    Enzyme and pathway databases

    Reactomei REACT_118682. Activation of Matrix Metalloproteinases.

    Miscellaneous databases

    GeneWikii MMP24.
    GenomeRNAii 10893.
    NextBioi 41363.
    PROi Q9Y5R2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y5R2.
    Bgeei Q9Y5R2.
    CleanExi HS_MMP24.
    Genevestigatori Q9Y5R2.

    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 and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors."
      Llano E., Pendas A.M., Freije J.P., Nakano A., Knaeuper V., Murphy G., Lopez-Otin C.
      Cancer Res. 59:2570-2576(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "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].
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiMMP24_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y5R2
    Secondary accession number(s): B7ZBG8, Q9H440
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3