Abstract
Supernatant protein factor (SPF) and alpha-tocopherol-associated protein (TAP) both belong to a widespread lipid-binding Sec 14-like protein family. All the members of the family have the lipid-binding motif called CRAL_TRIO. SPF is showed to stimulate the conversion of squalene to lanosterol and enhance cholesterol biosynthesis. TAP is identified to be involved in the intracellular distribution of alpha-tocopherol. Recently TAP is identified as SPF though they have very different functions. Here we report a human SPF/TAP homology SEC14L3 with 2082 base pairs in length and contains an open reading frame encoding a 400 amino acids protein. Analysis shows that SEC14L3 is mapped to 22q12 and expresses only in the liver among the used sixteen tissues in the test.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
ATP-Binding Cassette Transporters
-
Amino Acid Sequence
-
Binding Sites
-
Carrier Proteins / genetics*
-
Carrier Proteins / metabolism*
-
Chromosomes, Human, Pair 22
-
DNA, Complementary / genetics
-
Gene Expression Regulation*
-
Histocompatibility Antigens Class I / metabolism
-
Humans
-
Lipid Metabolism
-
Lipoproteins / metabolism*
-
Liver / physiology
-
Molecular Sequence Data
-
Proteins / genetics*
-
Proteins / metabolism*
-
Sequence Analysis
-
Sequence Homology, Amino Acid
-
Trans-Activators / metabolism*
Substances
-
ATP-Binding Cassette Transporters
-
Carrier Proteins
-
DNA, Complementary
-
Histocompatibility Antigens Class I
-
Lipoproteins
-
Proteins
-
SEC14L2 protein, human
-
SEC14L3 protein, human
-
Trans-Activators
-
transporter associated with antigen processing (TAP)