SMART: Pfam domain ELO

The domain within your query sequence starts at position 27 and ends at position 262; the E-value for the ELO domain shown below is 2.3e-68.

FLLDNYIPTFVCSVIYLLIVWLGPKYMKNRQPFSCRGILQLYNLGLTLLSLYMFYELVTG
VWEGKYNFFCQGTRSAGESDMKIIRVLWWYYFSKLIEFMDTFFFILRKNNHQITVLHVYH
HATMLNIWWFVMNWVPCGHSYFGATLNSFIHVLMYSYYGLSSIPSMRPYLWWKKYITQGQ
LVQFVLTIIQTTCGVFWPCSFPLGWLFFQIGYMISLIALFTNFYIQTYNKKGASRR

ELO

PFAM accession number:	PF01151
Interpro abstract (IPR002076):	This group of eukaryotic integral membrane proteins are evolutionary related, but exact function has not yet clearly been established. The proteins have from 290 to 435 amino acid residues. Structurally, they seem to be formed of three sections: a N-terminal region with two transmembrane domains, a central hydrophilic loop and a C-terminal region that contains from one to three transmembrane domains. Members of this family are involved in long chain fatty acid elongation systems that produce the 26-carbon precursors for ceramide and sphingolipid synthesis [ (PUBMED:8027068) ]. Predicted to be integral membrane proteins, in eukaryotes they are probably located on the endoplasmic reticulum. Yeast ELO3 ( P40319 ) affects plasma membrane H+-ATPase activity, and may act on a glucose-signalling pathway that controls the expression of several genes that are transcriptionally regulated by glucose such as PMA1 [ (PUBMED:7768822) ]. The ELO family consist of eukaryotic integral membrane proteins involved in fatty acid elongation. This family consist of: Mammalian proteins ELOVL1 to ELOVL4 [ (PUBMED:10791983) ]. These proteins all seem to be involved in the synthesis of very long chain fatty acids. Yeast ELO1, ELO2 and ELO3 [ (PUBMED:9211877) ]. They seem to be components of membrane-bound fatty acid elongation systems. Caenorhabditis elegans hypothetical protein C40H1.4. Caenorhabditis elegans hypothetical protein D2024.3.
GO component:	integral component of membrane (GO:0016021)

PFAM accession number:

PF01151

Interpro abstract (IPR002076):

This group of eukaryotic integral membrane proteins are evolutionary related, but exact function has not yet clearly been established. The proteins have from 290 to 435 amino acid residues. Structurally, they seem to be formed of three sections: a N-terminal region with two transmembrane domains, a central hydrophilic loop and a C-terminal region that contains from one to three transmembrane domains. Members of this family are involved in long chain fatty acid elongation systems that produce the 26-carbon precursors for ceramide and sphingolipid synthesis [ (PUBMED:8027068) ]. Predicted to be integral membrane proteins, in eukaryotes they are probably located on the endoplasmic reticulum. Yeast ELO3 ( P40319 ) affects plasma membrane H+-ATPase activity, and may act on a glucose-signalling pathway that controls the expression of several genes that are transcriptionally regulated by glucose such as PMA1 [ (PUBMED:7768822) ].

The ELO family consist of eukaryotic integral membrane proteins involved in fatty acid elongation. This family consist of:

Mammalian proteins ELOVL1 to ELOVL4 [ (PUBMED:10791983) ]. These proteins all seem to be involved in the synthesis of very long chain fatty acids.
Yeast ELO1, ELO2 and ELO3 [ (PUBMED:9211877) ]. They seem to be components of membrane-bound fatty acid elongation systems.
Caenorhabditis elegans hypothetical protein C40H1.4.
Caenorhabditis elegans hypothetical protein D2024.3.

GO component:

integral component of membrane (GO:0016021)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ELO