Human Gene MMP27 (ENST00000260229.5_7) from GENCODE V47lift37
  Description: matrix metallopeptidase 27 (from RefSeq NM_022122.3)
Gencode Transcript: ENST00000260229.5_7
Gencode Gene: ENSG00000137675.5_9
Transcript (Including UTRs)
   Position: hg19 chr11:102,562,218-102,576,500 Size: 14,283 Total Exon Count: 10 Strand: -
Coding Region
   Position: hg19 chr11:102,562,497-102,576,445 Size: 13,949 Coding Exon Count: 10 

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

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr11:102,562,218-102,576,500)mRNA (may differ from genome)Protein (513 aa)
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-  Comments and Description Text from UniProtKB
  ID: MMP27_HUMAN
DESCRIPTION: RecName: Full=Matrix metalloproteinase-27; Short=MMP-27; EC=3.4.24.-; Flags: Precursor;
FUNCTION: Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens (By similarity).
COFACTOR: Binds 4 calcium ions per subunit (By similarity).
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity).
TISSUE SPECIFICITY: Expressed in B-cells.
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.
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

+  Common Gene Haplotype Alleles
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-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 1.45 RPKM in Minor Salivary Gland
Total median expression: 6.05 RPKM



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

+  Microarray Expression Data
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-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -10.5055-0.191 Picture PostScript Text
3' UTR -38.80279-0.139 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
IPR021158 - Pept_M10A_Zn_BS
IPR006026 - Peptidase_Metallo
IPR002477 - Peptidoglycan-bd-like

Pfam Domains:
PF00045 - Hemopexin
PF00413 - Matrixin
PF01471 - Putative peptidoglycan binding domain

SCOP Domains:
47090 - PGBD-like
50923 - Hemopexin-like domain
55486 - Metalloproteases ("zincins"), catalytic domain

ModBase Predicted Comparative 3D Structure on Q9H306
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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
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-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0004222 metalloendopeptidase activity
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding

Biological Process:
GO:0006508 proteolysis
GO:0030574 collagen catabolic process

Cellular Component:
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane
GO:0031012 extracellular matrix
GO:0042406 extrinsic component of endoplasmic reticulum membrane


-  Descriptions from all associated GenBank mRNAs
  AF195192 - Homo sapiens matrix metalloprotease MMP-27 mRNA, complete cds.
AY358752 - Homo sapiens clone DNA96871 MMP27 (UNQ2503) mRNA, complete cds.
BC140433 - Synthetic construct Homo sapiens clone IMAGE:100014479, MGC:173171 matrix metallopeptidase 27 (MMP27) mRNA, encodes complete protein.
AB527320 - Synthetic construct DNA, clone: pF1KE0039, Homo sapiens MMP27 gene for matrix metallopeptidase 27, without stop codon, in Flexi system.

-  Other Names for This Gene
  Alternate Gene Symbols: ENST00000260229.1, ENST00000260229.2, ENST00000260229.3, ENST00000260229.4, MMP27_HUMAN, NM_022122, Q6UWK6, Q9H306, uc317gjg.1, uc317gjg.2, UNQ2503/PRO5992
UCSC ID: ENST00000260229.5_7
RefSeq Accession: NM_022122.3
Protein: Q9H306 (aka MMP27_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.