derlin-2 isoform b [Homo sapiens]
derlin( domain architecture ID 10517525)
derlin (or degradation in endoplasmic reticulum protein) may be a functional component of the endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not for misfolded non-glycoproteins
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
DER1 | pfam04511 | Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae ... |
13-202 | 1.23e-84 | ||||
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: 249.96 E-value: 1.23e-84
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Name | Accession | Description | Interval | E-value | ||||
DER1 | pfam04511 | Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae ... |
13-202 | 1.23e-84 | ||||
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: 249.96 E-value: 1.23e-84
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COG5291 | COG5291 | Predicted membrane protein [Function unknown]; |
11-208 | 1.43e-36 | ||||
Predicted membrane protein [Function unknown]; Pssm-ID: 227611 Cd Length: 313 Bit Score: 130.88 E-value: 1.43e-36
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Name | Accession | Description | Interval | E-value | ||||
DER1 | pfam04511 | Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae ... |
13-202 | 1.23e-84 | ||||
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: 249.96 E-value: 1.23e-84
|
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COG5291 | COG5291 | Predicted membrane protein [Function unknown]; |
11-208 | 1.43e-36 | ||||
Predicted membrane protein [Function unknown]; Pssm-ID: 227611 Cd Length: 313 Bit Score: 130.88 E-value: 1.43e-36
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Blast search parameters | ||||
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