Q9NPA2 · MMP25_HUMAN
- ProteinMatrix metalloproteinase-25
- GeneMMP25
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids562 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May activate progelatinase A.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 90 | Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 233 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 234 | |||||
Sequence: E | ||||||
Binding site | 237 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 243 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular matrix | |
Cellular Component | extracellular space | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Cellular Component | side of membrane | |
Cellular Component | specific granule membrane | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | collagen catabolic process | |
Biological Process | extracellular matrix organization | |
Biological Process | hard palate development | |
Biological Process | inflammatory response | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMatrix metalloproteinase-25
- EC number
- Short namesMMP-25
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NPA2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 877 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MRLRLRLLALLLLLLAPPARA | ||||||
Propeptide | PRO_0000028852 | 22-107 | ||||
Sequence: PKPSAQDVSLGVDWLTRYGYLPPPHPAQAQLQSPEKLRDAIKVMQRFAGLPETGRMDPGTVATMRKPRCSLPDVLGVAGLVRRRRR | ||||||
Chain | PRO_0000028853 | 108-539 | Matrix metalloproteinase-25 | |||
Sequence: YALSGSVWKKRTLTWRVRSFPQSSQLSQETVRVLMSYALMAWGMESGLTFHEVDSPQGQEPDILIDFARAFHQDSYPFDGLGGTLAHAFFPGEHPISGDTHFDDEETWTFGSKDGEGTDLFAVAVHEFGHALGLGHSSAPNSIMRPFYQGPVGDPDKYRLSQDDRDGLQQLYGKAPQTPYDKPTRKPLAPPPQPPASPTHSPSFPIPDRCEGNFDAIANIRGETFFFKGPWFWRLQPSGQLVSPRPARLHRFWEGLPAQVRVVQAAYARHRDGRILLFSGPQFWVFQDRQLEGGARPLTELGLPPGEEVDAVFSWPQNGKTYLVRGRQYWRYDEAAARPDPGYPRDLSLWEGAPPSPDDVTVSNAGDTYFFKGAHYWRFPKNSIKTEPDAPQPMGPNWLDCPAPSSGPRAPRPPKATPVSETCDCQCELNQA | ||||||
Disulfide bond | 317↔508 | |||||
Sequence: CEGNFDAIANIRGETFFFKGPWFWRLQPSGQLVSPRPARLHRFWEGLPAQVRVVQAAYARHRDGRILLFSGPQFWVFQDRQLEGGARPLTELGLPPGEEVDAVFSWPQNGKTYLVRGRQYWRYDEAAARPDPGYPRDLSLWEGAPPSPDDVTVSNAGDTYFFKGAHYWRFPKNSIKTEPDAPQPMGPNWLDC | ||||||
Lipidation | 539 | GPI-anchor amidated alanine | ||||
Sequence: A | ||||||
Propeptide | PRO_0000028854 | 540-562 | Removed in mature form | |||
Sequence: AGRWPAPIPLLLLPLLVGGVASR |
Post-translational modification
The precursor is cleaved by a furin endopeptidase.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed predominantly in leukocytes, lung and spleen. Expressed also in colon carcinoma, astrocytoma and glioblastomas.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NPA2 | MEOX2 Q6FHY5 | 3 | EBI-12346397, EBI-16439278 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 88-95 | Cysteine switch | ||||
Sequence: PRCSLPDV | ||||||
Region | 278-313 | Disordered | ||||
Sequence: LYGKAPQTPYDKPTRKPLAPPPQPPASPTHSPSFPI | ||||||
Compositional bias | 290-309 | Pro residues | ||||
Sequence: PTRKPLAPPPQPPASPTHSP | ||||||
Repeat | 314-363 | Hemopexin 1 | ||||
Sequence: PDRCEGNFDAIANIRGETFFFKGPWFWRLQPSGQLVSPRPARLHRFWEGL | ||||||
Repeat | 367-412 | Hemopexin 2 | ||||
Sequence: VRVVQAAYARHRDGRILLFSGPQFWVFQDRQLEGGARPLTELGLPP | ||||||
Repeat | 413-461 | Hemopexin 3 | ||||
Sequence: GEEVDAVFSWPQNGKTYLVRGRQYWRYDEAAARPDPGYPRDLSLWEGAP | ||||||
Repeat | 462-508 | Hemopexin 4 | ||||
Sequence: PSPDDVTVSNAGDTYFFKGAHYWRFPKNSIKTEPDAPQPMGPNWLDC | ||||||
Region | 490-526 | Disordered | ||||
Sequence: SIKTEPDAPQPMGPNWLDCPAPSSGPRAPRPPKATPV |
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.
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length562
- Mass (Da)62,554
- Last updated2000-10-01 v1
- ChecksumA6A50AE05D969C64
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A087WZS5 | A0A087WZS5_HUMAN | MMP25 | 235 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 47 | in Ref. 3; BAB20584 | ||||
Sequence: P → R | ||||||
Compositional bias | 290-309 | Pro residues | ||||
Sequence: PTRKPLAPPPQPPASPTHSP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ239053 EMBL· GenBank· DDBJ | CAB94713.1 EMBL· GenBank· DDBJ | mRNA | ||
AF145442 EMBL· GenBank· DDBJ | AAF66697.2 EMBL· GenBank· DDBJ | mRNA | ||
AF185270 EMBL· GenBank· DDBJ | AAG17007.1 EMBL· GenBank· DDBJ | mRNA | ||
AB042328 EMBL· GenBank· DDBJ | BAB20584.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ272137 EMBL· GenBank· DDBJ | CAC03490.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471112 EMBL· GenBank· DDBJ | EAW85413.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471112 EMBL· GenBank· DDBJ | EAW85415.1 EMBL· GenBank· DDBJ | Genomic DNA |