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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

  1. antioxidant activity Source: Ensembl
  2. beta-amyloid binding Source: UniProtKB
  3. cholesterol binding Source: GO_Central
  4. cholesterol transporter activity Source: GO_Central
  5. heparin binding Source: UniProtKB-KW
  6. hydroxyapatite binding Source: RGD
  7. lipid transporter activity Source: RGD
  8. lipoprotein particle binding Source: Ensembl
  9. low-density lipoprotein particle receptor binding Source: GO_Central
  10. metal chelating activity Source: Ensembl
  11. phosphatidylcholine-sterol O-acyltransferase activator activity Source: GO_Central
  12. phospholipid binding Source: RGD
  13. receptor binding Source: UniProtKB
  14. very-low-density lipoprotein particle receptor binding Source: GO_Central

GO - Biological processi

  1. aging Source: RGD
  2. alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering Source: Ensembl
  3. artery morphogenesis Source: Ensembl
  4. cellular calcium ion homeostasis Source: Ensembl
  5. cellular response to cholesterol Source: RGD
  6. cellular response to growth factor stimulus Source: RGD
  7. cellular response to interleukin-1 Source: RGD
  8. cGMP-mediated signaling Source: Ensembl
  9. cholesterol biosynthetic process Source: GO_Central
  10. cholesterol catabolic process Source: GO_Central
  11. cholesterol efflux Source: GO_Central
  12. cholesterol homeostasis Source: GO_Central
  13. chylomicron remnant clearance Source: Ensembl
  14. fatty acid homeostasis Source: Ensembl
  15. G-protein coupled receptor signaling pathway Source: Ensembl
  16. high-density lipoprotein particle assembly Source: GO_Central
  17. high-density lipoprotein particle clearance Source: Ensembl
  18. high-density lipoprotein particle remodeling Source: Ensembl
  19. lipid transport Source: RGD
  20. lipoprotein biosynthetic process Source: Ensembl
  21. lipoprotein catabolic process Source: GO_Central
  22. lipoprotein metabolic process Source: RGD
  23. long-chain fatty acid transport Source: Ensembl
  24. low-density lipoprotein particle remodeling Source: Ensembl
  25. maintenance of location in cell Source: Ensembl
  26. negative regulation of beta-amyloid formation Source: Ensembl
  27. negative regulation of blood vessel endothelial cell migration Source: Ensembl
  28. negative regulation of cholesterol biosynthetic process Source: Ensembl
  29. negative regulation of cholesterol efflux Source: Ensembl
  30. negative regulation of dendritic spine development Source: Ensembl
  31. negative regulation of dendritic spine maintenance Source: Ensembl
  32. negative regulation of endothelial cell proliferation Source: Ensembl
  33. negative regulation of inflammatory response Source: Ensembl
  34. negative regulation of lipid transport across blood brain barrier Source: Ensembl
  35. negative regulation of MAP kinase activity Source: Ensembl
  36. negative regulation of neuron apoptotic process Source: RGD
  37. negative regulation of phospholipid efflux Source: Ensembl
  38. negative regulation of platelet activation Source: Ensembl
  39. negative regulation of postsynaptic membrane organization Source: Ensembl
  40. negative regulation of presynaptic membrane organization Source: Ensembl
  41. neuron projection regeneration Source: RGD
  42. nitric oxide mediated signal transduction Source: Ensembl
  43. N-methyl-D-aspartate receptor clustering Source: Ensembl
  44. oligodendrocyte differentiation Source: RGD
  45. peripheral nervous system axon regeneration Source: RGD
  46. phospholipid efflux Source: GO_Central
  47. positive regulation of axon extension Source: RGD
  48. positive regulation of beta-amyloid formation Source: Ensembl
  49. positive regulation of cGMP biosynthetic process Source: Ensembl
  50. positive regulation of cholesterol efflux Source: Ensembl
  51. positive regulation of cholesterol esterification Source: GO_Central
  52. positive regulation of dendritic spine development Source: Ensembl
  53. positive regulation of dendritic spine maintenance Source: Ensembl
  54. positive regulation of lipid biosynthetic process Source: GO_Central
  55. positive regulation of lipid transport across blood brain barrier Source: Ensembl
  56. positive regulation of low-density lipoprotein particle receptor catabolic process Source: Ensembl
  57. positive regulation of membrane protein ectodomain proteolysis Source: Ensembl
  58. positive regulation of neurofibrillary tangle assembly Source: Ensembl
  59. positive regulation of neuron death Source: Ensembl
  60. positive regulation of nitric-oxide synthase activity Source: GO_Central
  61. positive regulation of phospholipid efflux Source: Ensembl
  62. positive regulation of postsynaptic membrane organization Source: Ensembl
  63. positive regulation of presynaptic membrane organization Source: Ensembl
  64. protein import Source: Ensembl
  65. receptor-mediated endocytosis Source: Ensembl
  66. regulation of beta-amyloid clearance Source: GO_Central
  67. regulation of Cdc42 protein signal transduction Source: Ensembl
  68. regulation of cholesterol transport Source: GO_Central
  69. regulation of gene expression Source: Ensembl
  70. regulation of tau-protein kinase activity Source: Ensembl
  71. response to dietary excess Source: Ensembl
  72. response to ethanol Source: RGD
  73. response to insulin Source: RGD
  74. response to oxidative stress Source: Ensembl
  75. response to retinoic acid Source: RGD
  76. reverse cholesterol transport Source: GO_Central
  77. triglyceride catabolic process Source: GO_Central
  78. vasodilation Source: Ensembl
  79. very-low-density lipoprotein particle clearance Source: Ensembl
  80. 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

  1. blood microparticle Source: GO_Central
  2. cell surface Source: RGD
  3. chylomicron Source: GO_Central
  4. cytoplasm Source: RGD
  5. dendrite Source: RGD
  6. discoidal high-density lipoprotein particle Source: RGD
  7. endoplasmic reticulum Source: RGD
  8. endosome Source: RGD
  9. extracellular matrix Source: Ensembl
  10. extracellular space Source: RGD
  11. extracellular vesicular exosome Source: Ensembl
  12. extrinsic component of external side of plasma membrane Source: RGD
  13. Golgi apparatus Source: RGD
  14. intermediate-density lipoprotein particle Source: GO_Central
  15. late endosome Source: RGD
  16. low-density lipoprotein particle Source: Ensembl
  17. lysosome Source: RGD
  18. neuronal cell body Source: RGD
  19. nuclear envelope Source: RGD
  20. plasma membrane Source: RGD
  21. 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
Modified residuei135 – 1351Methionine sulfoxideBy similarity
Modified residuei139 – 1391PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation sites are present in the extracellular medium.By similarity

Keywords - PTMi

Oxidation, Phosphoprotein

Proteomic databases

PaxDbiP02650.
PRIDEiP02650.

PTM databases

PhosphoSiteiP02650.

Expressioni

Tissue specificityi

Secreted in plasma.

Gene expression databases

GenevestigatoriP02650.

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:September 30, 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.
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.
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

GenevestigatoriP02650.

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(1985) [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(1985) [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(1982) [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(1994) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  6. Lubec G., Chen W.-Q.
    Submitted (MAR-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 20, 1986
Last sequence update: September 30, 1996
Last modified: March 31, 2015
This is version 130 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.