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Conserved domains on  [gi|1958661668|ref|XP_038943036|]
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lipase maturation factor 1 isoform X3 [Rattus norvegicus]

Protein Classification

lipase maturation factor family protein( domain architecture ID 10535984)

lipase maturation factor family protein similar to vertebrate lipase maturation factor, which is involved in the maturation of specific proteins in the endoplasmic reticulum, and may be required for maturation and transport of active lipoprotein lipase through the secretory pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LMF1 pfam06762
Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation ...
 2-297 7.19e-116

Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation factor, LMF1. Lipoprotein lipase and hepatic lipase require LMF1 to fold into their active states. It acts as a chaperone required for maturation and transport of active lipoprotein lipase (LPL), through the secretory pathway.


:

Pssm-ID: 462004  Cd Length: 419  Bit Score: 341.24  E-value: 7.19e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661668   2 AYYLHRSPRWFHRFETLSNHFLELLVPFFLFLG-RRMCVLHGVLQILFQVVLIISGNLSFLNWLTIVPSLACFDDATLGF 80
Cdd:pfam06762  84 SWYAHQLPSWFHKLETLGNHVVELVVPFLFFAPiRRLRIVAFFIQVLLQLLIILTGNYGFLNLLTIVLSLSLLDDAFLYF 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661668  81 LFPSGPRGLKKRVLE--------------MQREDAQRVQPKPRYLGCVVRQAANISLGI-LVAWLSVPVVINLLSSK--- 142
Cdd:pfam06762 164 WTPESRKKPPRTRLLsvietllsllvyglLIYGTVSLFGLKISENGTFLRRVTLPSIVLgLVSLLSVPVCALLRSNKliq 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661668 143 ----------------------------QVMNTSFNPLRIVNTYGAFGSITKERTEVILQGTANPNasapdAVWEDYEFK 194
Cdd:pfam06762 244 siqlaivtlaavllfalslvpfsvrnllSRMNASFNPLHLVNSYGLFGSMTGGRPEVVIEGSNDGE-----GPWKEYEFK 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661668 195 CKPGDPWRRPCLISPYHYRLDWLMWFAAFQTYEQNEWIIHLTGKLLADDAEALSLLALNPFEGRaPPRWIRGEHYRYKFS 274
Cdd:pfam06762 319 YKPGDVNRRPPFVAPYHPRLDWQMWFAALGTYQQNPWFLSLLYRLLQNDPEVLGLLDHNPFPDK-PPKYVRAELYRYRFT 397

                         330       340
                  ....*....|....*....|...
gi 1958661668 275 LPgGQHAAQGKWWIRKRIGPYFP 297
Cdd:pfam06762 398 TP-GERRATGAWWKRERVGEYFP 419
 
Name Accession Description Interval E-value
LMF1 pfam06762
Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation ...
 2-297 7.19e-116

Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation factor, LMF1. Lipoprotein lipase and hepatic lipase require LMF1 to fold into their active states. It acts as a chaperone required for maturation and transport of active lipoprotein lipase (LPL), through the secretory pathway.


Pssm-ID: 462004  Cd Length: 419  Bit Score: 341.24  E-value: 7.19e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661668   2 AYYLHRSPRWFHRFETLSNHFLELLVPFFLFLG-RRMCVLHGVLQILFQVVLIISGNLSFLNWLTIVPSLACFDDATLGF 80
Cdd:pfam06762  84 SWYAHQLPSWFHKLETLGNHVVELVVPFLFFAPiRRLRIVAFFIQVLLQLLIILTGNYGFLNLLTIVLSLSLLDDAFLYF 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661668  81 LFPSGPRGLKKRVLE--------------MQREDAQRVQPKPRYLGCVVRQAANISLGI-LVAWLSVPVVINLLSSK--- 142
Cdd:pfam06762 164 WTPESRKKPPRTRLLsvietllsllvyglLIYGTVSLFGLKISENGTFLRRVTLPSIVLgLVSLLSVPVCALLRSNKliq 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661668 143 ----------------------------QVMNTSFNPLRIVNTYGAFGSITKERTEVILQGTANPNasapdAVWEDYEFK 194
Cdd:pfam06762 244 siqlaivtlaavllfalslvpfsvrnllSRMNASFNPLHLVNSYGLFGSMTGGRPEVVIEGSNDGE-----GPWKEYEFK 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661668 195 CKPGDPWRRPCLISPYHYRLDWLMWFAAFQTYEQNEWIIHLTGKLLADDAEALSLLALNPFEGRaPPRWIRGEHYRYKFS 274
Cdd:pfam06762 319 YKPGDVNRRPPFVAPYHPRLDWQMWFAALGTYQQNPWFLSLLYRLLQNDPEVLGLLDHNPFPDK-PPKYVRAELYRYRFT 397

                         330       340
                  ....*....|....*....|...
gi 1958661668 275 LPgGQHAAQGKWWIRKRIGPYFP 297
Cdd:pfam06762 398 TP-GERRATGAWWKRERVGEYFP 419
 
Name Accession Description Interval E-value
LMF1 pfam06762
Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation ...
 2-297 7.19e-116

Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation factor, LMF1. Lipoprotein lipase and hepatic lipase require LMF1 to fold into their active states. It acts as a chaperone required for maturation and transport of active lipoprotein lipase (LPL), through the secretory pathway.


Pssm-ID: 462004  Cd Length: 419  Bit Score: 341.24  E-value: 7.19e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661668   2 AYYLHRSPRWFHRFETLSNHFLELLVPFFLFLG-RRMCVLHGVLQILFQVVLIISGNLSFLNWLTIVPSLACFDDATLGF 80
Cdd:pfam06762  84 SWYAHQLPSWFHKLETLGNHVVELVVPFLFFAPiRRLRIVAFFIQVLLQLLIILTGNYGFLNLLTIVLSLSLLDDAFLYF 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661668  81 LFPSGPRGLKKRVLE--------------MQREDAQRVQPKPRYLGCVVRQAANISLGI-LVAWLSVPVVINLLSSK--- 142
Cdd:pfam06762 164 WTPESRKKPPRTRLLsvietllsllvyglLIYGTVSLFGLKISENGTFLRRVTLPSIVLgLVSLLSVPVCALLRSNKliq 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661668 143 ----------------------------QVMNTSFNPLRIVNTYGAFGSITKERTEVILQGTANPNasapdAVWEDYEFK 194
Cdd:pfam06762 244 siqlaivtlaavllfalslvpfsvrnllSRMNASFNPLHLVNSYGLFGSMTGGRPEVVIEGSNDGE-----GPWKEYEFK 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661668 195 CKPGDPWRRPCLISPYHYRLDWLMWFAAFQTYEQNEWIIHLTGKLLADDAEALSLLALNPFEGRaPPRWIRGEHYRYKFS 274
Cdd:pfam06762 319 YKPGDVNRRPPFVAPYHPRLDWQMWFAALGTYQQNPWFLSLLYRLLQNDPEVLGLLDHNPFPDK-PPKYVRAELYRYRFT 397

                         330       340
                  ....*....|....*....|...
gi 1958661668 275 LPgGQHAAQGKWWIRKRIGPYFP 297
Cdd:pfam06762 398 TP-GERRATGAWWKRERVGEYFP 419
 
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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