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Conserved domains on  [gi|2217312251|ref|XP_047292142|]
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derlin-2 isoform X2 [Homo sapiens]

Protein Classification

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DER1 pfam04511
Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae ...
 110-284 1.32e-83

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: 250.34  E-value: 1.32e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312251 110 MGGQLELITPFQLYFNPELIFKHFQIWRLITNFLFFGPVGFNFLFNMIFLYRYCRMLEEGSFRGRTADFVFMFLFGGFLM 189
Cdd:pfam04511  17 LLGRLGLISPFYLYLNWELVFRKFQIWRLITSFLYFGGTGFHFLMNLYFIYQYSTMLEEGSFRGRPADYLYMLLFGAVLI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312251 190 TLFGLFVSLVFLGQAFTIMLVYVWSRRNPYVRMNFFGLLNFQAPFLPWVLMGFSLLLGNSIIVDLLGIAVGHIYFFLEDV 269
Cdd:pfam04511  97 TIFGLIVDIYFLGQALIAMIVYVWSQRNPDVIVSFWFGLRFQAKYLPWVLLGFSFILGGSVVVDLIGILVGHIYFFLEDV 176

                         170
                  ....*....|....*
gi 2217312251 270 FPNQPGGIRILKTPS 284
Cdd:pfam04511 177 YPIDLGGKRLLSTPQ 191
 
Name Accession Description Interval E-value
DER1 pfam04511
Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae ...
 110-284 1.32e-83

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: 250.34  E-value: 1.32e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312251 110 MGGQLELITPFQLYFNPELIFKHFQIWRLITNFLFFGPVGFNFLFNMIFLYRYCRMLEEGSFRGRTADFVFMFLFGGFLM 189
Cdd:pfam04511  17 LLGRLGLISPFYLYLNWELVFRKFQIWRLITSFLYFGGTGFHFLMNLYFIYQYSTMLEEGSFRGRPADYLYMLLFGAVLI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312251 190 TLFGLFVSLVFLGQAFTIMLVYVWSRRNPYVRMNFFGLLNFQAPFLPWVLMGFSLLLGNSIIVDLLGIAVGHIYFFLEDV 269
Cdd:pfam04511  97 TIFGLIVDIYFLGQALIAMIVYVWSQRNPDVIVSFWFGLRFQAKYLPWVLLGFSFILGGSVVVDLIGILVGHIYFFLEDV 176

                         170
                  ....*....|....*
gi 2217312251 270 FPNQPGGIRILKTPS 284
Cdd:pfam04511 177 YPIDLGGKRLLSTPQ 191
COG5291 COG5291
Predicted membrane protein [Function unknown];
112-290 2.39e-34

Predicted membrane protein [Function unknown];


Pssm-ID: 227611  Cd Length: 313  Bit Score: 127.41  E-value: 2.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312251 112 GQLELITPFQLYFNPELIFKHFQIWRLITNFLFFGPVGFNFLFNMIFLYRYCRMLEEGSFRGRTADFVFMFLFGGFLMTL 191
Cdd:COG5291    37 VYVDLVSPWYSLYYSPLFLKRLQIWRLFTSFLYFGKPTLDMFMHVYFLYRYSRMLEEGCFNTSLVEYFWYLLVISLVIFA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312251 192 FGLFVSL-VFLGQAFTIMLVYVWSRRNPYVRMNFFGLLNFQAPFLPWVLMGFSLLLGNSI-IVDLLGIAVGHIYFFLEDV 269
Cdd:COG5291   117 ISNIYGGiSALGTSFSATITYIWSKRNPRAIIQFFGFISVPGKYLPFILLGFSFLSRRGIsIDDVLGFVVGHLFHYFGDI 196

                         170       180
                  ....*....|....*....|.
gi 2217312251 270 FPNQpgGIRILKTPSILKAIF 290
Cdd:COG5291   197 YPMI--GRDILSTPCWVKKLF 215
 
Name Accession Description Interval E-value
DER1 pfam04511
Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae ...
 110-284 1.32e-83

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: 250.34  E-value: 1.32e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312251 110 MGGQLELITPFQLYFNPELIFKHFQIWRLITNFLFFGPVGFNFLFNMIFLYRYCRMLEEGSFRGRTADFVFMFLFGGFLM 189
Cdd:pfam04511  17 LLGRLGLISPFYLYLNWELVFRKFQIWRLITSFLYFGGTGFHFLMNLYFIYQYSTMLEEGSFRGRPADYLYMLLFGAVLI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312251 190 TLFGLFVSLVFLGQAFTIMLVYVWSRRNPYVRMNFFGLLNFQAPFLPWVLMGFSLLLGNSIIVDLLGIAVGHIYFFLEDV 269
Cdd:pfam04511  97 TIFGLIVDIYFLGQALIAMIVYVWSQRNPDVIVSFWFGLRFQAKYLPWVLLGFSFILGGSVVVDLIGILVGHIYFFLEDV 176

                         170
                  ....*....|....*
gi 2217312251 270 FPNQPGGIRILKTPS 284
Cdd:pfam04511 177 YPIDLGGKRLLSTPQ 191
COG5291 COG5291
Predicted membrane protein [Function unknown];
112-290 2.39e-34

Predicted membrane protein [Function unknown];


Pssm-ID: 227611  Cd Length: 313  Bit Score: 127.41  E-value: 2.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312251 112 GQLELITPFQLYFNPELIFKHFQIWRLITNFLFFGPVGFNFLFNMIFLYRYCRMLEEGSFRGRTADFVFMFLFGGFLMTL 191
Cdd:COG5291    37 VYVDLVSPWYSLYYSPLFLKRLQIWRLFTSFLYFGKPTLDMFMHVYFLYRYSRMLEEGCFNTSLVEYFWYLLVISLVIFA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312251 192 FGLFVSL-VFLGQAFTIMLVYVWSRRNPYVRMNFFGLLNFQAPFLPWVLMGFSLLLGNSI-IVDLLGIAVGHIYFFLEDV 269
Cdd:COG5291   117 ISNIYGGiSALGTSFSATITYIWSKRNPRAIIQFFGFISVPGKYLPFILLGFSFLSRRGIsIDDVLGFVVGHLFHYFGDI 196

                         170       180
                  ....*....|....*....|.
gi 2217312251 270 FPNQpgGIRILKTPSILKAIF 290
Cdd:COG5291   197 YPMI--GRDILSTPCWVKKLF 215
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 129-266 8.73e-03

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.


Pssm-ID: 426384  Cd Length: 147  Bit Score: 36.05  E-value: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312251 129 IFKHFQIWRLIT-NFLFFGPvgFNFLFNMIFLYRYCRMLEEGSFRGRTADFVFMFLFGGFLMTLFGLFVSLVFLGQ---A 204
Cdd:pfam01694   1 PVQPGQLWRLITsMFLHAGW--LHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPLSTPSVGAsgaI 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217312251 205 FTIMLVYvwSRRNPYVRMNFFGLLNFQAPFLPWVLMGFSLLLGNSIIVD----LLGIAVGHIYFFL 266
Cdd:pfam01694  79 FGLLGAL--LVLGPRNRILLFGLIGALLALLLFILLNLVLGLLPGNGVSnlahLGGLLVGLLLGFI 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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