Variant position: 163 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 317 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human MLGQSTEELRVRLASHLRKL RKRLLRDADDLQKRLAVYQAG
Gorilla MLGQSTEELRARLASHLRKL RKRLLRDADDLQKRLAVYQAG
Chimpanzee MLGQSTEELRARLASHLRKL RKRLLRDADDLQKRLAVYQAG
Mouse MLGQSTEEIRARLSTHLRKM RKRLMRDAEDLQKRLAVYKAG
Rat MLGQSTEELRSRLSTHLRKM RKRLMRDADDLQKRLAVYKAG
Pig MLGQTTEELRSRLASHLRNV RKRLVRDTEDLQKRLAVYQAG
Bovine MLGQSTEELRARMASHLRKL PKRLLRDADDLKKRLAVYQAG
Rabbit MLGQSTEELARAFSSHLRKL RKRLLRDAEDLQKRMAVYGAG
Sheep MLGQSTEELRARMASHLRKL RKRLLRDADDLKKRLAVYQAG
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
19 – 317 Apolipoprotein E
146 – 167 4
80 – 255 8 X 22 AA approximate tandem repeats
158 – 168 LDL and other lipoprotein receptors binding
162 – 165 Heparin-binding
143 – 143 Methionine sulfoxide
147 – 147 Phosphoserine; by FAM20C
157 – 157 S -> R. Increased binding to LDL receptor; when associated with A-167.
158 – 158 H -> A. Decreased binding to LDL receptor.
161 – 161 K -> A. Decreased binding to LDL receptor.
162 – 162 L -> P. Decreased binding to LDL receptor.
167 – 167 L -> A. Increased binding to LDL receptor; when associated with R-157.
168 – 168 R -> A. Decreased binding to LDL receptor.
172 – 172 D -> A. Restores the LDL receptor binding activity of ApoE2.
149 – 179
Apolipoprotein E Sendai (arginine 145-->proline): a new variant associated with lipoprotein glomerulopathy.
Oikawa S.; Matsunaga A.; Saito T.; Sato H.; Seki T.; Hoshi K.; Hayasaka K.; Kotake H.; Midorikawa H.; Sekikawa A.; Hara S.; Abe K.; Toyota T.; Jingami H.; Nakamura H.; Sasaki J.;
J. Am. Soc. Nephrol. 8:820-823(1997)
Cited for: VARIANT LPG PRO-163;
Virus-mediated transduction of apolipoprotein E (ApoE)-sendai develops lipoprotein glomerulopathy in ApoE-deficient mice.
Ishigaki Y.; Oikawa S.; Suzuki T.; Usui S.; Magoori K.; Kim D.H.; Suzuki H.; Sasaki J.; Sasano H.; Okazaki M.; Toyota T.; Saito T.; Yamamoto T.T.;
J. Biol. Chem. 275:31269-31273(2000)
Cited for: CHARACTERIZATION OF VARIANT LPG PRO-163; CHARACTERIZATION OF VARIANT AD2 ARG-130;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.