Human Gene MMP24 (ENST00000246186.8_4) from GENCODE V47lift37
  Description: matrix metallopeptidase 24 (from RefSeq NM_006690.4)
Gencode Transcript: ENST00000246186.8_4
Gencode Gene: ENSG00000125966.10_7
Transcript (Including UTRs)
   Position: hg19 chr20:33,814,493-33,864,801 Size: 50,309 Total Exon Count: 9 Strand: +
Coding Region
   Position: hg19 chr20:33,814,542-33,862,412 Size: 47,871 Coding Exon Count: 9 

Page IndexSequence and LinksUniProtKB CommentsPrimersCTDGene Alleles
RNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther SpeciesGO Annotations
mRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated at UCSC: 2024-08-22 23:36:26

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr20:33,814,493-33,864,801)mRNA (may differ from genome)Protein (645 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
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HGNCMGIOMIMPubMedReactomeUniProtKB
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-  Comments and Description Text from UniProtKB
  ID: MMP24_HUMAN
DESCRIPTION: RecName: Full=Matrix metalloproteinase-24; Short=MMP-24; EC=3.4.24.-; AltName: Full=Membrane-type matrix metalloproteinase 5; Short=MT-MMP 5; Short=MTMMP5; AltName: Full=Membrane-type-5 matrix metalloproteinase; Short=MT5-MMP; Short=MT5MMP; Contains: RecName: Full=Processed matrix metalloproteinase-24; Flags: Precursor;
FUNCTION: Activates 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).
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
COFACTOR: Calcium (By similarity).
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein; Extracellular side (By similarity).
SUBCELLULAR LOCATION: Processed matrix metalloproteinase-24: Secreted, extracellular space, extracellular matrix (By similarity). Note=Also shed from cell surface as soluble proteinase, by a proteolytic cleavage (By similarity).
TISSUE SPECIFICITY: Predominantly expressed in brain, kidney, pancreas and lung. Overexpressed in a series of brain tumors, including astrocytomas and glioblastomas.
DOMAIN: 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.
PTM: The precursor is cleaved by a furin endopeptidase (By similarity).
SIMILARITY: Belongs to the peptidase M10A family.
SIMILARITY: Contains 4 hemopexin-like domains.

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 67.88 RPKM in Brain - Cerebellum
Total median expression: 380.74 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -30.4049-0.620 Picture PostScript Text
3' UTR -1031.902389-0.432 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR000585 - Hemopexin/matrixin
IPR018486 - Hemopexin/matrixin_CS
IPR018487 - Hemopexin/matrixin_repeat
IPR024079 - MetalloPept_cat_dom
IPR001818 - Pept_M10_metallopeptidase
IPR016293 - Pept_M10A_matrix_strom
IPR021190 - Pept_M10A_matrixin
IPR021805 - Pept_M10A_metallopeptidase_C
IPR006026 - Peptidase_Metallo
IPR002477 - Peptidoglycan-bd-like

Pfam Domains:
PF00045 - Hemopexin
PF00413 - Matrixin
PF01471 - Putative peptidoglycan binding domain
PF11857 - Domain of unknown function (DUF3377)

SCOP Domains:
47090 - PGBD-like
101447 - Formin homology 2 domain (FH2 domain)
50923 - Hemopexin-like domain
55486 - Metalloproteases ("zincins"), catalytic domain

ModBase Predicted Comparative 3D Structure on Q9Y5R2
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologNo orthologNo orthologNo orthologNo ortholog
Gene DetailsGene Details    
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-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0004222 metalloendopeptidase activity
GO:0008047 enzyme activator activity
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0045296 cadherin binding
GO:0046872 metal ion binding

Biological Process:
GO:0006508 proteolysis
GO:0007155 cell adhesion
GO:0010001 glial cell differentiation
GO:0043085 positive regulation of catalytic activity
GO:0044331 cell-cell adhesion mediated by cadherin
GO:0050965 detection of temperature stimulus involved in sensory perception of pain
GO:0097150 neuronal stem cell population maintenance
GO:0098742 cell-cell adhesion via plasma-membrane adhesion molecules

Cellular Component:
GO:0005576 extracellular region
GO:0005794 Golgi apparatus
GO:0005886 plasma membrane
GO:0005887 integral component of plasma membrane
GO:0016020 membrane
GO:0016021 integral component of membrane
GO:0031012 extracellular matrix
GO:0032588 trans-Golgi network membrane
GO:0070062 extracellular exosome


-  Descriptions from all associated GenBank mRNAs
  AB021227 - Homo sapiens mt5-mmp mRNA for membrane-type-5 matrix metalloproteinase, complete cds.
DQ300264 - Homo sapiens matrix metalloproteinase 24 variant mRNA, partial cds.
BC172450 - Synthetic construct Homo sapiens clone IMAGE:100069144, MGC:199155 matrix metallopeptidase 24 (membrane-inserted) (MMP24) mRNA, encodes complete protein.
AF131284 - Homo sapiens membrane type 5 matrix metalloproteinase (MMP24) mRNA, complete cds.
BC047614 - Homo sapiens matrix metallopeptidase 24 (membrane-inserted), mRNA (cDNA clone IMAGE:5768916), partial cds.
MP015277 - Sequence 480 from Patent WO2019016252.
JD475939 - Sequence 456963 from Patent EP1572962.
JD413064 - Sequence 394088 from Patent EP1572962.
JD513336 - Sequence 494360 from Patent EP1572962.
JD533545 - Sequence 514569 from Patent EP1572962.
JD142806 - Sequence 123830 from Patent EP1572962.
JD530680 - Sequence 511704 from Patent EP1572962.
JD475140 - Sequence 456164 from Patent EP1572962.
JD158517 - Sequence 139541 from Patent EP1572962.
JD387831 - Sequence 368855 from Patent EP1572962.
JD371815 - Sequence 352839 from Patent EP1572962.
JD425282 - Sequence 406306 from Patent EP1572962.
JD075489 - Sequence 56513 from Patent EP1572962.
JD111623 - Sequence 92647 from Patent EP1572962.
JD136934 - Sequence 117958 from Patent EP1572962.
JD533622 - Sequence 514646 from Patent EP1572962.
JD468745 - Sequence 449769 from Patent EP1572962.
JD269269 - Sequence 250293 from Patent EP1572962.
JD121643 - Sequence 102667 from Patent EP1572962.
JD045064 - Sequence 26088 from Patent EP1572962.
JD373728 - Sequence 354752 from Patent EP1572962.
JD164367 - Sequence 145391 from Patent EP1572962.
JD439460 - Sequence 420484 from Patent EP1572962.
JD535755 - Sequence 516779 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein Q9Y5R2 (Reactome details) participates in the following event(s):

R-HSA-1602466 Activation of MT-MMPs by FURIN
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1474244 Extracellular matrix organization

-  Other Names for This Gene
  Alternate Gene Symbols: B7ZBG8, ENST00000246186.1, ENST00000246186.2, ENST00000246186.3, ENST00000246186.4, ENST00000246186.5, ENST00000246186.6, ENST00000246186.7, MMP24_HUMAN, MT5MMP, NM_006690, Q9H440, Q9Y5R2, uc317etc.1, uc317etc.2
UCSC ID: ENST00000246186.8_4
RefSeq Accession: NM_006690.4
Protein: Q9Y5R2 (aka MMP24_HUMAN or MM24_HUMAN)

-  Gene Model Information
  Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.