derlin-2 isoform X1 [Mus musculus]
Protein Classification
rhomboid family protein( domain architecture ID 229382)
rhomboid family protein may be a membrane-bound serine protease that catalyzes regulated intramembrane proteolysis, resulting in the release of functional polypeptides from their membrane anchors
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Rhomboid super family | cl21536 | Rhomboid family; This family contains integral membrane proteins that are related to ... |
13-59 | 5.14e-12 | ||
Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite. The actual alignment was detected with superfamily member pfam04511: Pssm-ID: 451297 Cd Length: 191 Bit Score: 57.74 E-value: 5.14e-12
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| DER1 | pfam04511 | Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae ... |
13-59 | 5.14e-12 | ||
Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae contains of proteolytic system able to selectively degrade misfolded lumenal secretory proteins. For examination of the components involved in this degradation process, mutants were isolated. They could be divided into four complementation groups. The mutations led to stabilization of two different substrates for this process. The mutant classes were called 'der' for 'degradation in the ER'. DER1 was cloned by complementation of the der1-2 mutation. The DER1 gene codes for a novel, hydrophobic protein, that is localized to the ER. Deletion of DER1 abolished degradation of the substrate proteins. The function of the Der1 protein seems to be specifically required for the degradation process associated with the ER. Interestingly this family seems distantly related to the Rhomboid family of membrane peptidases. Suggesting that this family may also mediate degradation of misfolded proteins (Bateman A pers. obs.). Pssm-ID: 427988 Cd Length: 191 Bit Score: 57.74 E-value: 5.14e-12
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| DER1 | pfam04511 | Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae ... |
13-59 | 5.14e-12 | ||
Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae contains of proteolytic system able to selectively degrade misfolded lumenal secretory proteins. For examination of the components involved in this degradation process, mutants were isolated. They could be divided into four complementation groups. The mutations led to stabilization of two different substrates for this process. The mutant classes were called 'der' for 'degradation in the ER'. DER1 was cloned by complementation of the der1-2 mutation. The DER1 gene codes for a novel, hydrophobic protein, that is localized to the ER. Deletion of DER1 abolished degradation of the substrate proteins. The function of the Der1 protein seems to be specifically required for the degradation process associated with the ER. Interestingly this family seems distantly related to the Rhomboid family of membrane peptidases. Suggesting that this family may also mediate degradation of misfolded proteins (Bateman A pers. obs.). Pssm-ID: 427988 Cd Length: 191 Bit Score: 57.74 E-value: 5.14e-12
|
||||||
| Blast search parameters | ||||
|
