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Apolipoprotein E (Apo-E)

 APOE_RAT                Reviewed;         312 AA.
P02650;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
23-MAY-2018, entry version 155.
RecName: Full=Apolipoprotein E;
Short=Apo-E;
Flags: Precursor;
Name=Apoe;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3797247; DOI=10.1093/nar/14.23.9527;
Fukazawa C., Matsumoto A., Taylor L.M.;
"Complete nucleotide sequence of the gene encoding the rat
apolipoprotein E.";
Nucleic Acids Res. 14:9527-9528(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3020048;
Fung W.-P., Howlett G.J., Schreiber G.;
"Structure and expression of the rat apolipoprotein E gene.";
J. Biol. Chem. 261:13777-13783(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6190813;
McLean J.W., Fukazawa C., Taylor J.M.;
"Rat apolipoprotein E mRNA. Cloning and sequencing of double-stranded
cDNA.";
J. Biol. Chem. 258:8993-9000(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=7766086; DOI=10.1007/BF00191183;
Nomura N., Yamada H., Matsubara N., Horinouchi S., Beppu T.;
"Secretion by Saccharomyces cerevisiae of rat apolipoprotein E as a
fusion to Mucor rennin.";
Appl. Microbiol. Biotechnol. 42:865-870(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 87-100; 114-122; 130-144; 191-199; 202-216;
226-236 AND 262-270, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Mediates the binding, internalization, and catabolism of
lipoprotein particles. It can serve as a ligand for the LDL (apo
B/E) receptor and for the specific apo-E receptor (chylomicron
remnant) of hepatic tissues. {ECO:0000250|UniProtKB:P02649}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}.
-!- TISSUE SPECIFICITY: Secreted in plasma.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P02649}.
-!- MISCELLANEOUS: The mature protein has no cysteine residues;
however, in different allelic variants where cysteine residues
replace arginine at positions 155 or 168, binding of Apo-E to cell
membrane receptors is decreased. The amino end of this protein is
therefore thought to interact with the receptor.
-!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X04979; CAA28650.1; -; Genomic_DNA.
EMBL; J02582; AAA40755.1; -; Genomic_DNA.
EMBL; S76779; AAC60703.1; -; mRNA.
EMBL; BC086581; AAH86581.1; -; mRNA.
PIR; A26189; LPRTE.
RefSeq; NP_001257610.1; NM_001270681.1.
RefSeq; NP_001257611.1; NM_001270682.1.
RefSeq; NP_001257612.1; NM_001270683.1.
RefSeq; NP_001257613.1; NM_001270684.1.
RefSeq; NP_620183.2; NM_138828.3.
UniGene; Rn.32351; -.
ProteinModelPortal; P02650; -.
SMR; P02650; -.
BioGrid; 247757; 2.
IntAct; P02650; 3.
STRING; 10116.ENSRNOP00000050968; -.
iPTMnet; P02650; -.
PhosphoSitePlus; P02650; -.
PaxDb; P02650; -.
PRIDE; P02650; -.
Ensembl; ENSRNOT00000041891; ENSRNOP00000050968; ENSRNOG00000018454.
Ensembl; ENSRNOT00000091574; ENSRNOP00000068937; ENSRNOG00000018454.
GeneID; 25728; -.
KEGG; rno:25728; -.
UCSC; RGD:2138; rat.
CTD; 348; -.
RGD; 2138; Apoe.
eggNOG; ENOG410IVK0; Eukaryota.
eggNOG; ENOG4111MYC; LUCA.
GeneTree; ENSGT00730000111315; -.
HOGENOM; HOG000034006; -.
HOVERGEN; HBG010582; -.
InParanoid; P02650; -.
KO; K04524; -.
PhylomeDB; P02650; -.
TreeFam; TF334458; -.
Reactome; R-RNO-3000480; Scavenging by Class A Receptors.
Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
Reactome; R-RNO-8963888; Chylomicron assembly.
Reactome; R-RNO-8963901; Chylomicron remodeling.
Reactome; R-RNO-8964026; Chylomicron clearance.
Reactome; R-RNO-8964058; HDL remodeling.
Reactome; R-RNO-975634; Retinoid metabolism and transport.
PRO; PR:P02650; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000018454; -.
ExpressionAtlas; P02650; baseline and differential.
Genevisible; P02650; RN.
GO; GO:0072562; C:blood microparticle; IBA:GO_Central.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0042627; C:chylomicron; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0034365; C:discoidal high-density lipoprotein particle; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0005768; C:endosome; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0034364; C:high-density lipoprotein particle; IDA:ARUK-UCL.
GO; GO:0034363; C:intermediate-density lipoprotein particle; IDA:ARUK-UCL.
GO; GO:0005770; C:late endosome; IDA:RGD.
GO; GO:0034362; C:low-density lipoprotein particle; IDA:ARUK-UCL.
GO; GO:0005764; C:lysosome; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005635; C:nuclear envelope; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:ARUK-UCL.
GO; GO:0001540; F:amyloid-beta binding; IDA:RGD.
GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
GO; GO:0017127; F:cholesterol transporter activity; IBA:GO_Central.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0046848; F:hydroxyapatite binding; IDA:RGD.
GO; GO:0005319; F:lipid transporter activity; IDA:RGD.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IBA:GO_Central.
GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IBA:GO_Central.
GO; GO:0005543; F:phospholipid binding; IDA:RGD.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0070326; F:very-low-density lipoprotein particle receptor binding; IBA:GO_Central.
GO; GO:0007568; P:aging; IDA:RGD.
GO; GO:0071397; P:cellular response to cholesterol; IEP:RGD.
GO; GO:0071361; P:cellular response to ethanol; IEP:RGD.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0006707; P:cholesterol catabolic process; IBA:GO_Central.
GO; GO:0033344; P:cholesterol efflux; IBA:GO_Central.
GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
GO; GO:0006869; P:lipid transport; IDA:RGD.
GO; GO:0042159; P:lipoprotein catabolic process; IBA:GO_Central.
GO; GO:0042157; P:lipoprotein metabolic process; IDA:RGD.
GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IDA:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD.
GO; GO:0031102; P:neuron projection regeneration; TAS:RGD.
GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
GO; GO:0014012; P:peripheral nervous system axon regeneration; IEP:RGD.
GO; GO:0033700; P:phospholipid efflux; IBA:GO_Central.
GO; GO:0045773; P:positive regulation of axon extension; IDA:RGD.
GO; GO:0010873; P:positive regulation of cholesterol esterification; IBA:GO_Central.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IBA:GO_Central.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IBA:GO_Central.
GO; GO:1900221; P:regulation of amyloid-beta clearance; IBA:GO_Central.
GO; GO:0032374; P:regulation of cholesterol transport; IBA:GO_Central.
GO; GO:0090207; P:regulation of triglyceride metabolic process; IDA:RGD.
GO; GO:1904421; P:response to D-galactosamine; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
GO; GO:0034612; P:response to tumor necrosis factor; IEP:RGD.
GO; GO:0010043; P:response to zinc ion; IEP:RGD.
GO; GO:0043691; P:reverse cholesterol transport; IBA:GO_Central.
GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IBA:GO_Central.
InterPro; IPR000074; ApoA_E.
Pfam; PF01442; Apolipoprotein; 1.
1: Evidence at protein level;
Chylomicron; Complete proteome; Direct protein sequencing;
Glycoprotein; HDL; Heparin-binding; Lipid transport; Oxidation;
Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
Transport; VLDL.
SIGNAL 1 18
CHAIN 19 312 Apolipoprotein E.
/FTId=PRO_0000001996.
REPEAT 72 93 1.
REPEAT 94 115 2.
REPEAT 116 137 3.
REPEAT 138 159 4.
REPEAT 160 181 5.
REPEAT 182 203 6.
REPEAT 204 225 7.
REPEAT 226 247 8.
REGION 72 247 8 X 22 AA approximate tandem repeats.
REGION 150 160 LDL receptor binding.
{ECO:0000250|UniProtKB:P02649}.
REGION 154 157 Heparin-binding.
{ECO:0000250|UniProtKB:P02649}.
REGION 221 228 Heparin-binding.
{ECO:0000250|UniProtKB:P02649}.
MOD_RES 135 135 Methionine sulfoxide.
{ECO:0000250|UniProtKB:P08226}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 25 25 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:Q03247}.
CARBOHYD 305 305 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:Q03247}.
CONFLICT 104 104 A -> T (in Ref. 1; CAA28650).
{ECO:0000305}.
CONFLICT 110 110 A -> T (in Ref. 3; no nucleotide entry
and 4; AAC60703). {ECO:0000305}.
CONFLICT 141 141 E -> D (in Ref. 3; no nucleotide entry
and 4; AAC60703). {ECO:0000305}.
CONFLICT 206 213 GAGAAQPL -> RWRRPAP (in Ref. 1; CAA28650
and 3; no nucleotide entry).
{ECO:0000305}.
CONFLICT 309 310 LE -> WR (in Ref. 3; no nucleotide entry
and 4; AAC60703). {ECO:0000305}.
SEQUENCE 312 AA; 35753 MW; 8180EEE933378D92 CRC64;
MKALWALLLV PLLTGCLAEG ELEVTDQLPG QSDQPWEQAL NRFWDYLRWV QTLSDQVQEE
LQSSQVTQEL TVLMEDTMTE VKAYKKELEE QLGPVAEETR ARLAKEVQAA QARLGADMED
LRNRLGQYRN EVNTMLGQST EELRSRLSTH LRKMRKRLMR DADDLQKRLA VYKAGAQEGA
ERGVSAIRER LGPLVEQGRQ RTANLGAGAA QPLRDRAQAL SDRIRGRLEE VGNQARDRLE
EVREQMEEVR SKMEEQTQQI RLQAEIFQAR IKGWFEPLVE DMQRQWANLM EKIQASVATN
SIASTTVPLE NQ


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