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Literature summary for 3.4.21.109 extracted from
- Role of matriptase-2 (TMPRSS6) in iron metabolism (2009), Acta Haematol., 122, 87-96.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D521N | point mutations D521N and E522K located in the conserved D/NXSDE motif in the LDLa2 domain of matriptase-2 are associated with iron-refractory iron deficiency anemia in patients and affect residues predicted to bind Ca2+. In vitro, the D521N and E522K mutants show reduced cell surface localization, increased Golgi retention, impaired autoactivation of matriptase-2, impaired cleavage of hemojuvelin, and impaired ability to repress Hamp1 reporter expression but are able to bind hemojuvelin | Homo sapiens |
| E522K | point mutations D521N and E522K located in the conserved D/NXSDE motif in the LDLa2 domain of matriptase-2 are associated with iron-refractory iron deficiency anemia in patients and affect residues predicted to bind Ca2+. In vitro, the D521N and E522K mutants show reduced cell surface localization, increased Golgi retention, impaired autoactivation of matriptase-2, impaired cleavage of hemojuvelin, and impaired ability to repress Hamp1 reporter expression but are able to bind hemojuvelin | Homo sapiens |
| G442R | matriptase-2 containing the point mutation G442R located in the second CUB domain demonstrate impaired autoactivation, are still able to bind but demonstrate reduced cleavage of coexpressed hemojuvelin, and exhibit reduced ability to repress HAMP reporter expression | Homo sapiens |
| R599X | point mutation identified in zorro mice causing premature termination of matriptase-2 and an iron deficiency phenotype | Mus musculus |
| R774C | point mutation identified in an iron-refractory iron deficiency anemia patient is located in the protease domain and disrupts accurate C32/C36 or C35/C37 disulfide bonding within the protease domain | Homo sapiens |
| S762A | protease dead mutation is shown in vitro to be ineffective in repressing Hamp1 reporter expression | Homo sapiens |
| W783X | point mutation identified in masquerade mice causing premature termination of matriptase-2 and an iron deficiency phenotype | Mus musculus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| plasma membrane | - |
Mus musculus | 5886 | - |
| plasma membrane | - |
Homo sapiens | 5886 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q8IU80 | - |
- |
| Mus musculus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | sea urchin sperm protein, enteropeptidase, and agrin (SEA) domain is O-glycosylated | Mus musculus |
| glycoprotein | sea urchin sperm protein, enteropeptidase, and agrin (SEA) domain is O-glycosylated | Homo sapiens |
| proteolytic modification | the 811-amino-acid human protein is synthesized as an inactive zymogen and autoactivated by proteolytic cleavage | Mus musculus |
| proteolytic modification | the 811-amino-acid human protein is synthesized as an inactive zymogen and autoactivated by proteolytic cleavage | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | matriptase is almost exclusively expressed in liver | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alphaEbeta7integrin + H2O | - |
Homo sapiens | ? | - |
? |  |
| Boc-QAR-Amc + H2O | matriptase-2 mediates efficient cleavage of artificial peptides corresponding to cleavage sites located in the proteins filaggrin, CUB-domain-containing protein 1 (CDCP1), and alphaE beta7 integrin | Homo sapiens | ? | - |
? | |
| CUB-domain-containing protein 1 + H2O | - |
Homo sapiens | ? | - |
? | |
| Fibrinogen + H2O | - |
Homo sapiens | ? | - |
? | |
| Fibronectin + H2O | - |
Homo sapiens | ? | - |
? | |
| filaggrin + H2O | - |
Homo sapiens | ? | - |
? | |
| hemojuvelin (furin site) + H2O | - |
Homo sapiens | ? | - |
? | |
| N2-t-butyloxycarbonyl-QNR-7-amido-4-methylcoumarin + H2O | matriptase-2 mediates efficient cleavage of artificial peptides corresponding to cleavage sites located in the proteins filaggrin, CUB-domain-containing protein 1 (CDCP1), and alphaE beta7 integrin | Homo sapiens | ? | - |
? | |
| TMPRSS6 + H2O | autocleavage site: PSSR/IVGG | Homo sapiens | ? | - |
? | |
| Type I collagen + H2O | - |
Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| matriptase-2 | - |
Mus musculus |
| matriptase-2 | - |
Homo sapiens |
| TMPRSS6 | - |
Mus musculus |
| TMPRSS6 | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | matriptase-2 is important for iron homeostasis. Human patients with iron-refractory iron deficiency anemia show mutation in the TMPRSS6 gene | Homo sapiens |
| malfunction | Tmprss6-/- mice knockout mice exhibit an iron deficiency phenotype. Tmprss6 -/- mice exhibit reduced ferroportin immunostaining and iron accumulation in intestinal enterocytes | Mus musculus |
| physiological function | matriptase-2 regulates iron metabolism through proteolytic cleavage of hemojuvelin, a cell surface protein that regulates hepcidin expression through a bone morphogeneic protein/SMAD pathway | Mus musculus |
| physiological function | matriptase-2 regulates iron metabolism through proteolytic cleavage of hemojuvelin, a cell surface protein that regulates hepcidin expression through a bone morphogeneic protein/SMAD pathway | Homo sapiens |
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