Protein detail
MMP24
Matrix metalloproteinase-24 (MMP-24) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 5) (MT-MMP 5) (MTMMP5) (Membrane-type-5 matrix metalloproteinase) (MT5-MMP) (MT5MMP) [Cleaved into: Processed matrix metalloproteinase-24]
Entry name MMP24 | UniProt ID | EVMP confidence score 0.38 |
Supporting publications (n) 4 | Transmembrane count 1 | Protein classification EnzymesPredicted membrane proteinsPredicted secreted proteins |
EVMP confidence score
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40Basic Information13
Protein Names
Matrix metalloproteinase-24 (MMP-24) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 5) (MT-MMP 5) (MTMMP5) (Membrane-type-5 matrix metalloproteinase) (MT5-MMP) (MT5MMP) [Cleaved into: Processed matrix metalloproteinase-24]
Protein Class (3)
EnzymesPredicted membrane proteinsPredicted secreted proteins
Protein Function (3)
- Peptidases:Metallopeptidases
- Enzymes
- Predicted secreted proteins
Transmembrane
603..623; Helical
Transmembrane Count
1
Ensembl
Entrez Gene Symbol
Gene Synonym
MT5-MMP
Gene Description
Matrix metallopeptidase 24
Chromosome
20
Position
35226690-35276998
Supporting publications (n)
4
EVMP confidence score
0.38
Fluorescence & Localization1
Function & Pathway7
Protein Function (3)
- Peptidases:Metallopeptidases
- Enzymes
- Predicted secreted proteins
Cellular Component (5)
Molecular Function (4)
Biological Process (3)
KEGG (2)
- hsa04928 Parathyroid hormone synthesis
- secretion and action
Reactome (3)
Mediation Categories (2)
Adhesion and uptake mediationFusion and delivery mediation
Relations & Evidence33
Ligand-Receptor Signaling (32)
32 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| cell_surface_enzyme | cell_surface_enzyme | OmniPath | Yes | No | Yes | Yes | No |
| cell_surface_peptidase | cell_surface_peptidase | OmniPath | Yes | No | Yes | Yes | No |
| transmembrane | transmembrane | UniProt_location | No | No | Yes | Yes | No |
| transmembrane | transmembrane | UniProt_topology | No | No | Yes | Yes | No |
| transmembrane | transmembrane | UniProt_keyword | No | No | Yes | Yes | No |
| transmembrane_predicted | transmembrane | OmniPath | No | No | Yes | Yes | No |
| transmembrane | transmembrane | LOCATE | No | No | Yes | Yes | No |
| transmembrane | transmembrane | Ramilowski_location | No | No | Yes | Yes | No |
| transmembrane | transmembrane | OmniPath | No | No | Yes | Yes | No |
| plasma_membrane | plasma_membrane | UniProt_location | No | No | Yes | Yes | No |
Sequence, Structure & Domains10
Sequences
Length
645
Mass
73,231
Sequence
MPRSRGGRAAPGPPPPPPPPGQAPRWSRWRVPGRLLLLLLPALCCLPGAARAAAAAAGAGNRAAVAVAVARADEAEAPFAGQNWLKSYGYLLPYDSRASALHSAKALQSAVSTMQQFYGIPVTGVLDQTTIEWMKKPRCGVPDHPHLSRRRRNKRYALTGQKWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEIKSDRKEADIMIFFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSSDPSAIMAPFYQYMETHNFKLPQDDLQGIQKIYGPPAEPLEPTRPLPTLPVRRIHSPSERKHERQPRPPRPPLGDRPSTPGTKPNICDGNFNTVALFRGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWKGLPARIDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPKPITVWKGIPQAPQGAFISKEGYYTYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGCNQKEVERRKERRLPQDDVDIMVTINDVPGSVNAVAVVIPCILSLCILVLVYTIFQFKNKTGPQPVTYYKRPVQEWV
Domain & Motif Annotations
Compositional Bias
1..10; Low complexity; 11..22; Pro residues; 329..341; Pro residues; 349..359; Basic and acidic residues
Repeat
377..425; Hemopexin 1; 426..471; Hemopexin 2; 473..521; Hemopexin 3; 522..569; Hemopexin 4
Motif
137..144; Cysteine switch; 643..645; PDZ-binding
Domain (CC)
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.; DOMAIN: The PDZ-binding motif (also named EWV motif) is required for interaction with PDZ domains of APBA3 and recycling through the trans-Golgi network.
Region
1..26; Disordered; 323..380; Disordered
Protein Families
Peptidase M10A family
Sequence Similarities
Belongs to the peptidase M10A family.
Supporting Publications4
| PMID | Title | Abstract |
|---|---|---|
| 19837982 | Proteomics analysis of A33 immunoaffinity-purified exosomes released from the human colon tumor cell line LIM1215 reveals a tissue-specific protein signature. | A conspicuous finding of this comparative analysis was the presence of host cell-specific (LIM1215 exosome) proteins such as A33, cadherin-17, carcinoembryonic antigen, epithelial cell surface antigen (EpCAM), proliferating cell nuclear antigen, epidermal growth factor receptor, mucin 13, misshapen-like kinase 1, keratin 18, mitogen-activated protein kinase 4, claudins (1, 3, and 7), centrosomal protein 55 kDa, and ephrin-B1 and -B2. Here, we describe an immunoaffinity capture method using the colon epithelial cell-specific A33 antibody to purify colorectal cancer cell (LIM1215)-derived exosomes. |
| 27605433 | Secreted primary human malignant mesothelioma exosome signature reflects oncogenic cargo. | No abstract available |
| 32249794 | Urinary Exosomes from Bladder Cancer Patients Show a Residual Cancer Phenotype despite Complete Pathological Downstaging. | No abstract available |
| 37438638 | Extracellular Vesicles Play a Central Role in Cerebral Venous Disease-Associated Brain Atrophy. | No abstract available |