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Protein

Apolipoprotein E

Gene

Apoe

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • cellular response to cholesterol Source: RGD
  • cellular response to growth factor stimulus Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cholesterol biosynthetic process Source: GO_Central
  • cholesterol catabolic process Source: GO_Central
  • cholesterol efflux Source: GO_Central
  • cholesterol homeostasis Source: GO_Central
  • high-density lipoprotein particle assembly Source: GO_Central
  • lipid transport Source: RGD
  • lipoprotein catabolic process Source: GO_Central
  • lipoprotein metabolic process Source: RGD
  • negative regulation of neuron apoptotic process Source: RGD
  • neuron projection regeneration Source: RGD
  • oligodendrocyte differentiation Source: RGD
  • peripheral nervous system axon regeneration Source: RGD
  • phospholipid efflux Source: GO_Central
  • positive regulation of axon extension Source: RGD
  • positive regulation of cholesterol esterification Source: GO_Central
  • positive regulation of lipid biosynthetic process Source: GO_Central
  • positive regulation of nitric-oxide synthase activity Source: GO_Central
  • regulation of beta-amyloid clearance Source: GO_Central
  • regulation of cholesterol transport Source: GO_Central
  • response to ethanol Source: RGD
  • response to insulin Source: RGD
  • response to retinoic acid Source: RGD
  • reverse cholesterol transport Source: GO_Central
  • triglyceride catabolic process Source: GO_Central
  • very-low-density lipoprotein particle remodeling Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_302011. Scavenging by Class A Receptors.
REACT_319671. Retinoid metabolism and transport.
REACT_345465. Chylomicron-mediated lipid transport.
REACT_346849. HDL-mediated lipid transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipoprotein E
Short name:
Apo-E
Gene namesi
Name:Apoe
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2138. Apoe.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: GO_Central
  • cell surface Source: RGD
  • chylomicron Source: GO_Central
  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • discoidal high-density lipoprotein particle Source: RGD
  • endoplasmic reticulum Source: RGD
  • endosome Source: RGD
  • extracellular space Source: RGD
  • extrinsic component of external side of plasma membrane Source: RGD
  • Golgi apparatus Source: RGD
  • intermediate-density lipoprotein particle Source: GO_Central
  • late endosome Source: RGD
  • lysosome Source: RGD
  • neuronal cell body Source: RGD
  • nuclear envelope Source: RGD
  • plasma membrane Source: RGD
  • very-low-density lipoprotein particle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chylomicron, HDL, Secreted, VLDL

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 312294Apolipoprotein EPRO_0000001996Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251O-linked (GalNAc...)By similarity
Modified residuei135 – 1351Methionine sulfoxideBy similarity
Modified residuei139 – 1391PhosphoserineBy similarity
Glycosylationi305 – 3051O-linked (GalNAc...)By similarity

Post-translational modificationi

Phosphorylation sites are present in the extracellular medium.By similarity

Keywords - PTMi

Glycoprotein, Oxidation, Phosphoprotein

Proteomic databases

PaxDbiP02650.
PRIDEiP02650.

PTM databases

PhosphoSiteiP02650.

Expressioni

Tissue specificityi

Secreted in plasma.

Gene expression databases

GenevisibleiP02650. RN.

Interactioni

Protein-protein interaction databases

BioGridi247757. 1 interaction.
IntActiP02650. 3 interactions.
MINTiMINT-4585732.
STRINGi10116.ENSRNOP00000050968.

Structurei

3D structure databases

ProteinModelPortaliP02650.
SMRiP02650. Positions 23-195.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati72 – 93221Add
BLAST
Repeati94 – 115222Add
BLAST
Repeati116 – 137223Add
BLAST
Repeati138 – 159224Add
BLAST
Repeati160 – 181225Add
BLAST
Repeati182 – 203226Add
BLAST
Repeati204 – 225227Add
BLAST
Repeati226 – 247228Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni72 – 2471768 X 22 AA approximate tandem repeatsAdd
BLAST
Regioni150 – 16011LDL receptor bindingSequence AnalysisAdd
BLAST
Regioni154 – 1574Heparin-bindingBy similarity
Regioni221 – 2288Heparin-bindingBy similarity

Sequence similaritiesi

Belongs to the apolipoprotein A1/A4/E family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG44867.
GeneTreeiENSGT00730000111315.
HOGENOMiHOG000034006.
HOVERGENiHBG010582.
InParanoidiP02650.
KOiK04524.
OMAiPLQERAQ.
OrthoDBiEOG793B87.
PhylomeDBiP02650.
TreeFamiTF334458.

Family and domain databases

InterProiIPR000074. ApoA_E.
[Graphical view]
PfamiPF01442. Apolipoprotein. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02650-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALWALLLV PLLTGCLAEG ELEVTDQLPG QSDQPWEQAL NRFWDYLRWV
60 70 80 90 100
QTLSDQVQEE LQSSQVTQEL TVLMEDTMTE VKAYKKELEE QLGPVAEETR
110 120 130 140 150
ARLAKEVQAA QARLGADMED LRNRLGQYRN EVNTMLGQST EELRSRLSTH
160 170 180 190 200
LRKMRKRLMR DADDLQKRLA VYKAGAQEGA ERGVSAIRER LGPLVEQGRQ
210 220 230 240 250
RTANLGAGAA QPLRDRAQAL SDRIRGRLEE VGNQARDRLE EVREQMEEVR
260 270 280 290 300
SKMEEQTQQI RLQAEIFQAR IKGWFEPLVE DMQRQWANLM EKIQASVATN
310
SIASTTVPLE NQ
Length:312
Mass (Da):35,753
Last modified:October 1, 1996 - v2
Checksum:i8180EEE933378D92
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041A → T in CAA28650 (PubMed:3797247).Curated
Sequence conflicti110 – 1101A → T no nucleotide entry (PubMed:6190813).Curated
Sequence conflicti110 – 1101A → T in AAC60703 (PubMed:7766086).Curated
Sequence conflicti141 – 1411E → D no nucleotide entry (PubMed:6190813).Curated
Sequence conflicti141 – 1411E → D in AAC60703 (PubMed:7766086).Curated
Sequence conflicti206 – 2138GAGAAQPL → RWRRPAP in CAA28650 (PubMed:3797247).Curated
Sequence conflicti206 – 2138GAGAAQPL → RWRRPAP no nucleotide entry (PubMed:6190813).Curated
Sequence conflicti309 – 3102LE → WR no nucleotide entry (PubMed:6190813).Curated
Sequence conflicti309 – 3102LE → WR in AAC60703 (PubMed:7766086).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04979 Genomic DNA. Translation: CAA28650.1.
J02582 Genomic DNA. Translation: AAA40755.1.
S76779 mRNA. Translation: AAC60703.1.
BC086581 mRNA. Translation: AAH86581.1.
PIRiA26189. LPRTE.
RefSeqiNP_001257610.1. NM_001270681.1.
NP_001257611.1. NM_001270682.1.
NP_001257612.1. NM_001270683.1.
NP_001257613.1. NM_001270684.1.
NP_620183.2. NM_138828.3.
UniGeneiRn.32351.

Genome annotation databases

EnsembliENSRNOT00000041891; ENSRNOP00000050968; ENSRNOG00000018454.
ENSRNOT00000091574; ENSRNOP00000068937; ENSRNOG00000018454.
GeneIDi25728.
KEGGirno:25728.
UCSCiRGD:2138. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04979 Genomic DNA. Translation: CAA28650.1.
J02582 Genomic DNA. Translation: AAA40755.1.
S76779 mRNA. Translation: AAC60703.1.
BC086581 mRNA. Translation: AAH86581.1.
PIRiA26189. LPRTE.
RefSeqiNP_001257610.1. NM_001270681.1.
NP_001257611.1. NM_001270682.1.
NP_001257612.1. NM_001270683.1.
NP_001257613.1. NM_001270684.1.
NP_620183.2. NM_138828.3.
UniGeneiRn.32351.

3D structure databases

ProteinModelPortaliP02650.
SMRiP02650. Positions 23-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247757. 1 interaction.
IntActiP02650. 3 interactions.
MINTiMINT-4585732.
STRINGi10116.ENSRNOP00000050968.

PTM databases

PhosphoSiteiP02650.

Proteomic databases

PaxDbiP02650.
PRIDEiP02650.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000041891; ENSRNOP00000050968; ENSRNOG00000018454.
ENSRNOT00000091574; ENSRNOP00000068937; ENSRNOG00000018454.
GeneIDi25728.
KEGGirno:25728.
UCSCiRGD:2138. rat.

Organism-specific databases

CTDi348.
RGDi2138. Apoe.

Phylogenomic databases

eggNOGiNOG44867.
GeneTreeiENSGT00730000111315.
HOGENOMiHOG000034006.
HOVERGENiHBG010582.
InParanoidiP02650.
KOiK04524.
OMAiPLQERAQ.
OrthoDBiEOG793B87.
PhylomeDBiP02650.
TreeFamiTF334458.

Enzyme and pathway databases

ReactomeiREACT_302011. Scavenging by Class A Receptors.
REACT_319671. Retinoid metabolism and transport.
REACT_345465. Chylomicron-mediated lipid transport.
REACT_346849. HDL-mediated lipid transport.

Miscellaneous databases

NextBioi607845.
PROiP02650.

Gene expression databases

GenevisibleiP02650. RN.

Family and domain databases

InterProiIPR000074. ApoA_E.
[Graphical view]
PfamiPF01442. Apolipoprotein. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence of the gene encoding the rat apolipoprotein E."
    Fukazawa C., Matsumoto A., Taylor L.M.
    Nucleic Acids Res. 14:9527-9528(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structure and expression of the rat apolipoprotein E gene."
    Fung W.-P., Howlett G.J., Schreiber G.
    J. Biol. Chem. 261:13777-13783(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Rat apolipoprotein E mRNA. Cloning and sequencing of double-stranded cDNA."
    McLean J.W., Fukazawa C., Taylor J.M.
    J. Biol. Chem. 258:8993-9000(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Secretion by Saccharomyces cerevisiae of rat apolipoprotein E as a fusion to Mucor rennin."
    Nomura N., Yamada H., Matsubara N., Horinouchi S., Beppu T.
    Appl. Microbiol. Biotechnol. 42:865-870(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  6. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 87-100; 114-122; 130-144; 191-199; 202-216; 226-236 AND 262-270, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.

Entry informationi

Entry nameiAPOE_RAT
AccessioniPrimary (citable) accession number: P02650
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.