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Conserved domains on  [gi|569001991|ref|XP_006525160|]
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lipase maturation factor 1 isoform X3 [Mus musculus]

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 ...
 1-261 1.28e-98

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: 295.40  E-value: 1.28e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001991    1 MRILHGVLQILFQVILIISGNLSFLNWLTIVPSLACFDDAALGFLFPSGPQGLKKQVLEIQREDT--------------Q 66
Cdd:pfam06762 120 LRIVAFFIQVLLQLLIILTGNYGFLNLLTIVLSLSLLDDAFLYFWTPESRKKPPRTRLLSVIETLlsllvyglliygtvS 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001991   67 RVQPKPRDRGCLVRQVVNISLGI-LVAWLSVPVVINLLSSRQI-------------------------------MNTSFN 114
Cdd:pfam06762 200 LFGLKISENGTFLRRVTLPSIVLgLVSLLSVPVCALLRSNKLIqsiqlaivtlaavllfalslvpfsvrnllsrMNASFN 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001991  115 PLRIVNTYGAFGSVTKERTEVILQGTvspnaSAPDAVWEDYEFKCKPGDPWRQPCLISPYHYRLDWLMWFAAFQTYEQNE 194
Cdd:pfam06762 280 PLHLVNSYGLFGSMTGGRPEVVIEGS-----NDGEGPWKEYEFKYKPGDVNRRPPFVAPYHPRLDWQMWFAALGTYQQNP 354

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569001991  195 WILHLAGKLLAGDSEALALLAVNPFEGRtPPRWIRGEHYRYKFSLPgGQHATQGKWWIRKRIGPYFP 261
Cdd:pfam06762 355 WFLSLLYRLLQNDPEVLGLLDHNPFPDK-PPKYVRAELYRYRFTTP-GERRATGAWWKRERVGEYFP 419
 
Name Accession Description Interval E-value
LMF1 pfam06762
Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation ...
 1-261 1.28e-98

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: 295.40  E-value: 1.28e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001991    1 MRILHGVLQILFQVILIISGNLSFLNWLTIVPSLACFDDAALGFLFPSGPQGLKKQVLEIQREDT--------------Q 66
Cdd:pfam06762 120 LRIVAFFIQVLLQLLIILTGNYGFLNLLTIVLSLSLLDDAFLYFWTPESRKKPPRTRLLSVIETLlsllvyglliygtvS 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001991   67 RVQPKPRDRGCLVRQVVNISLGI-LVAWLSVPVVINLLSSRQI-------------------------------MNTSFN 114
Cdd:pfam06762 200 LFGLKISENGTFLRRVTLPSIVLgLVSLLSVPVCALLRSNKLIqsiqlaivtlaavllfalslvpfsvrnllsrMNASFN 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001991  115 PLRIVNTYGAFGSVTKERTEVILQGTvspnaSAPDAVWEDYEFKCKPGDPWRQPCLISPYHYRLDWLMWFAAFQTYEQNE 194
Cdd:pfam06762 280 PLHLVNSYGLFGSMTGGRPEVVIEGS-----NDGEGPWKEYEFKYKPGDVNRRPPFVAPYHPRLDWQMWFAALGTYQQNP 354

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569001991  195 WILHLAGKLLAGDSEALALLAVNPFEGRtPPRWIRGEHYRYKFSLPgGQHATQGKWWIRKRIGPYFP 261
Cdd:pfam06762 355 WFLSLLYRLLQNDPEVLGLLDHNPFPDK-PPKYVRAELYRYRFTTP-GERRATGAWWKRERVGEYFP 419
 
Name Accession Description Interval E-value
LMF1 pfam06762
Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation ...
 1-261 1.28e-98

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: 295.40  E-value: 1.28e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001991    1 MRILHGVLQILFQVILIISGNLSFLNWLTIVPSLACFDDAALGFLFPSGPQGLKKQVLEIQREDT--------------Q 66
Cdd:pfam06762 120 LRIVAFFIQVLLQLLIILTGNYGFLNLLTIVLSLSLLDDAFLYFWTPESRKKPPRTRLLSVIETLlsllvyglliygtvS 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001991   67 RVQPKPRDRGCLVRQVVNISLGI-LVAWLSVPVVINLLSSRQI-------------------------------MNTSFN 114
Cdd:pfam06762 200 LFGLKISENGTFLRRVTLPSIVLgLVSLLSVPVCALLRSNKLIqsiqlaivtlaavllfalslvpfsvrnllsrMNASFN 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001991  115 PLRIVNTYGAFGSVTKERTEVILQGTvspnaSAPDAVWEDYEFKCKPGDPWRQPCLISPYHYRLDWLMWFAAFQTYEQNE 194
Cdd:pfam06762 280 PLHLVNSYGLFGSMTGGRPEVVIEGS-----NDGEGPWKEYEFKYKPGDVNRRPPFVAPYHPRLDWQMWFAALGTYQQNP 354

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569001991  195 WILHLAGKLLAGDSEALALLAVNPFEGRtPPRWIRGEHYRYKFSLPgGQHATQGKWWIRKRIGPYFP 261
Cdd:pfam06762 355 WFLSLLYRLLQNDPEVLGLLDHNPFPDK-PPKYVRAELYRYRFTTP-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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