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P02650

- APOE_RAT

UniProt

P02650 - APOE_RAT

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Protein

Apolipoprotein E

Gene
Apoe
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 transporter activity Source: Ensembl
  4. heparin binding Source: UniProtKB-KW
  5. hydroxyapatite binding Source: RGD
  6. lipid transporter activity Source: RGD
  7. lipoprotein particle binding Source: Ensembl
  8. metal chelating activity Source: Ensembl
  9. phosphatidylcholine-sterol O-acyltransferase activator activity Source: Ensembl
  10. phospholipid binding Source: RGD
  11. receptor binding Source: UniProt

GO - Biological processi

  1. aging Source: RGD
  2. artery morphogenesis Source: Ensembl
  3. cellular calcium ion homeostasis Source: Ensembl
  4. cellular response to cholesterol Source: RGD
  5. cellular response to growth factor stimulus Source: RGD
  6. cellular response to interleukin-1 Source: RGD
  7. cGMP-mediated signaling Source: Ensembl
  8. cholesterol catabolic process Source: Ensembl
  9. cholesterol efflux Source: Ensembl
  10. cholesterol homeostasis Source: Ensembl
  11. chylomicron remnant clearance Source: Ensembl
  12. G-protein coupled receptor signaling pathway Source: Ensembl
  13. high-density lipoprotein particle assembly Source: Ensembl
  14. high-density lipoprotein particle clearance Source: Ensembl
  15. high-density lipoprotein particle remodeling Source: Ensembl
  16. lipid transport Source: RGD
  17. lipoprotein biosynthetic process Source: Ensembl
  18. lipoprotein catabolic process Source: Ensembl
  19. lipoprotein metabolic process Source: RGD
  20. low-density lipoprotein particle remodeling Source: Ensembl
  21. maintenance of location in cell Source: Ensembl
  22. negative regulation of blood vessel endothelial cell migration Source: Ensembl
  23. negative regulation of cholesterol biosynthetic process Source: Ensembl
  24. negative regulation of endothelial cell proliferation Source: Ensembl
  25. negative regulation of inflammatory response Source: Ensembl
  26. negative regulation of MAP kinase activity Source: Ensembl
  27. negative regulation of neuron apoptotic process Source: RGD
  28. negative regulation of platelet activation Source: Ensembl
  29. neuron projection regeneration Source: RGD
  30. nitric oxide mediated signal transduction Source: Ensembl
  31. oligodendrocyte differentiation Source: RGD
  32. peripheral nervous system axon regeneration Source: RGD
  33. phospholipid efflux Source: Ensembl
  34. positive regulation of axon extension Source: RGD
  35. positive regulation of cGMP biosynthetic process Source: Ensembl
  36. positive regulation of cholesterol efflux Source: Ensembl
  37. positive regulation of cholesterol esterification Source: Ensembl
  38. positive regulation of low-density lipoprotein particle receptor catabolic process Source: Ensembl
  39. positive regulation of membrane protein ectodomain proteolysis Source: Ensembl
  40. positive regulation of nitric-oxide synthase activity Source: Ensembl
  41. receptor-mediated endocytosis Source: Ensembl
  42. regulation of Cdc42 protein signal transduction Source: Ensembl
  43. response to dietary excess Source: Ensembl
  44. response to ethanol Source: RGD
  45. response to insulin Source: RGD
  46. response to oxidative stress Source: Ensembl
  47. response to retinoic acid Source: RGD
  48. reverse cholesterol transport Source: Ensembl
  49. triglyceride metabolic process Source: Ensembl
  50. vasodilation Source: Ensembl
  51. very-low-density lipoprotein particle clearance Source: Ensembl
  52. very-low-density lipoprotein particle remodeling Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_198733. Scavenging by Class A Receptors.
REACT_199015. Retinoid metabolism and 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: Chromosome 1

Organism-specific databases

RGDi2138. Apoe.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: RGD
  2. chylomicron Source: UniProtKB-KW
  3. cytoplasm Source: RGD
  4. dendrite Source: RGD
  5. discoidal high-density lipoprotein particle Source: RGD
  6. endoplasmic reticulum Source: RGD
  7. endosome Source: RGD
  8. extracellular space Source: RGD
  9. extrinsic component of external side of plasma membrane Source: RGD
  10. Golgi apparatus Source: RGD
  11. intermediate-density lipoprotein particle Source: Ensembl
  12. late endosome Source: RGD
  13. low-density lipoprotein particle Source: Ensembl
  14. lysosome Source: RGD
  15. neuronal cell body Source: RGD
  16. nuclear envelope Source: RGD
  17. plasma membrane Source: RGD
  18. 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 sulfoxide By 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.

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 binding Reviewed predictionAdd
BLAST
Regioni154 – 1574Heparin-binding By similarity
Regioni221 – 2288Heparin-binding By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

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

Family and domain databases

InterProiIPR000074. ApoA1_A4_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

MKALWALLLV PLLTGCLAEG ELEVTDQLPG QSDQPWEQAL NRFWDYLRWV    50
QTLSDQVQEE LQSSQVTQEL TVLMEDTMTE VKAYKKELEE QLGPVAEETR 100
ARLAKEVQAA QARLGADMED LRNRLGQYRN EVNTMLGQST EELRSRLSTH 150
LRKMRKRLMR DADDLQKRLA VYKAGAQEGA ERGVSAIRER LGPLVEQGRQ 200
RTANLGAGAA QPLRDRAQAL SDRIRGRLEE VGNQARDRLE EVREQMEEVR 250
SKMEEQTQQI RLQAEIFQAR IKGWFEPLVE DMQRQWANLM EKIQASVATN 300
SIASTTVPLE NQ 312
Length:312
Mass (Da):35,753
Last modified:October 1, 1996 - v2
Checksum:i8180EEE933378D92
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041A → T in CAA28650. 1 Publication
Sequence conflicti110 – 1101A → T no nucleotide entry 1 Publication
Sequence conflicti110 – 1101A → T in AAC60703. 1 Publication
Sequence conflicti141 – 1411E → D no nucleotide entry 1 Publication
Sequence conflicti141 – 1411E → D in AAC60703. 1 Publication
Sequence conflicti206 – 2138GAGAAQPL → RWRRPAP in CAA28650. 1 Publication
Sequence conflicti206 – 2138GAGAAQPL → RWRRPAP no nucleotide entry 1 Publication
Sequence conflicti309 – 3102LE → WR no nucleotide entry 1 Publication
Sequence conflicti309 – 3102LE → WR in AAC60703. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X04979 Genomic DNA. Translation: CAA28650.1 .
J02582 Genomic DNA. Translation: AAA40755.1 .
S76779 mRNA. Translation: AAC60703.1 .
BC086581 mRNA. Translation: AAH86581.1 .
PIRi A26189. LPRTE.
RefSeqi NP_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.
UniGenei Rn.32351.

3D structure databases

ProteinModelPortali P02650.
SMRi P02650. Positions 23-195.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247757. 1 interaction.
IntActi P02650. 3 interactions.
MINTi MINT-4585732.
STRINGi 10116.ENSRNOP00000050968.

PTM databases

PhosphoSitei P02650.

Proteomic databases

PaxDbi P02650.
PRIDEi P02650.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000041891 ; ENSRNOP00000050968 ; ENSRNOG00000018454 .
GeneIDi 25728.
KEGGi rno:25728.
UCSCi RGD:2138. rat.

Organism-specific databases

CTDi 348.
RGDi 2138. Apoe.

Phylogenomic databases

eggNOGi NOG44867.
GeneTreei ENSGT00730000111315.
HOGENOMi HOG000034006.
HOVERGENi HBG010582.
InParanoidi P02650.
KOi K04524.
OMAi PLQERAQ.
OrthoDBi EOG793B87.
PhylomeDBi P02650.
TreeFami TF334458.

Enzyme and pathway databases

Reactomei REACT_198733. Scavenging by Class A Receptors.
REACT_199015. Retinoid metabolism and transport.

Miscellaneous databases

NextBioi 607845.
PROi P02650.

Gene expression databases

Genevestigatori P02650.

Family and domain databases

InterProi IPR000074. ApoA1_A4_E.
[Graphical view ]
Pfami PF01442. Apolipoprotein. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 123 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