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APOE_TAPTE
ID   APOE_TAPTE              Reviewed;         310 AA.
AC   P0DUP8;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=Apolipoprotein E;
DE            Short=Apo-E;
DE   Flags: Precursor;
GN   Name=APOE;
OS   Tapirus terrestris (Lowland tapir) (Brazilian tapir).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Tapiridae; Tapirus.
OX   NCBI_TaxID=9801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Johnson J., Muren E., Swofford R., Turner-Maier J., Marinescu V.D.,
RA   Genereux D.P., Alfoldi J., Birren B., Karlsson E.K., Lindblad-Toh K.;
RT   "The 200 mammals project: sequencing genomes by a novel cost-effective
RT   method, yielding a high resolution annotation of the human genome.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (MAR-2021).
CC   -!- FUNCTION: APOE is an apolipoprotein, a protein associating with lipid
CC       particles, that mainly functions in lipoprotein-mediated lipid
CC       transport between organs via the plasma and interstitial fluids. APOE
CC       is a core component of plasma lipoproteins and is involved in their
CC       production, conversion and clearance. Apoliproteins are amphipathic
CC       molecules that interact both with lipids of the lipoprotein particle
CC       core and the aqueous environment of the plasma. As such, APOE
CC       associates with chylomicrons, chylomicron remnants, very low density
CC       lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but
CC       shows a preferential binding to high-density lipoproteins (HDL). It
CC       also binds a wide range of cellular receptors including the LDL
CC       receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8
CC       and the very low-density lipoprotein receptor/VLDLR that mediate the
CC       cellular uptake of the APOE-containing lipoprotein particles. Finally,
CC       APOE has also a heparin-binding activity and binds heparan-sulfate
CC       proteoglycans on the surface of cells, a property that supports the
CC       capture and the receptor-mediated uptake of APOE-containing
CC       lipoproteins by cells. A main function of APOE is to mediate
CC       lipoprotein clearance through the uptake of chylomicrons, VLDLs, and
CC       HDLs by hepatocytes. APOE is also involved in the biosynthesis by the
CC       liver of VLDLs as well as their uptake by peripheral tissues ensuring
CC       the delivery of triglycerides and energy storage in muscle, heart and
CC       adipose tissues. By participating in the lipoprotein-mediated
CC       distribution of lipids among tissues, APOE plays a critical role in
CC       plasma and tissues lipid homeostasis. APOE is also involved in two
CC       steps of reverse cholesterol transport, the HDLs-mediated transport of
CC       cholesterol from peripheral tissues to the liver, and thereby plays an
CC       important role in cholesterol homeostasis. First, it is functionally
CC       associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it
CC       is enriched in circulating HDLs and mediates their uptake by
CC       hepatocytes. APOE also plays an important role in lipid transport in
CC       the central nervous system, regulating neuron survival and sprouting.
CC       {ECO:0000250|UniProtKB:P02649}.
CC   -!- SUBUNIT: Homotetramer. May interact with ABCA1; functionally associated
CC       with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-
CC       beta peptide; the interaction is extremely stable in vitro but its
CC       physiological significance is unclear. May interact with MAPT. May
CC       interact with MAP2. In the cerebrospinal fluid, interacts with secreted
CC       SORL1. {ECO:0000250|UniProtKB:P02649}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}.
CC       Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted,
CC       extracellular space, extracellular matrix
CC       {ECO:0000250|UniProtKB:P02649}. Note=In the plasma, APOE is associated
CC       with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL
CC       lipoproteins. Lipid poor oligomeric APOE is associated with the
CC       extracellular matrix in a calcium- and heparan-sulfate proteoglycans-
CC       dependent manner. Lipidation induces the release from the extracellular
CC       matrix. {ECO:0000250|UniProtKB:P02649}.
CC   -!- PTM: APOE exists as multiple glycosylated and sialylated glycoforms
CC       within cells and in plasma. The extent of glycosylation and sialylation
CC       are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.
CC   -!- PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000250|UniProtKB:P02649}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC       {ECO:0000305}.
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DR   EMBL; PVID01019406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DUP8; -.
DR   SMR; P0DUP8; -.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR   InterPro; IPR000074; ApoA_E.
DR   Pfam; PF01442; Apolipoprotein; 1.
PE   3: Inferred from homology;
KW   Chylomicron; Extracellular matrix; Glycoprotein; HDL; Heparin-binding;
KW   Lipid transport; Lipid-binding; Oxidation; Phosphoprotein; Repeat;
KW   Secreted; Signal; Transport; VLDL.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..310
FT                   /note="Apolipoprotein E"
FT                   /id="PRO_0000452911"
FT   REPEAT          77..98
FT                   /note="1"
FT   REPEAT          99..120
FT                   /note="2"
FT   REPEAT          121..142
FT                   /note="3"
FT   REPEAT          143..164
FT                   /note="4"
FT   REPEAT          165..186
FT   REPEAT          187..204
FT                   /note="6"
FT   REPEAT          205..226
FT                   /note="7"
FT   REPEAT          227..248
FT                   /note="8"
FT   REGION          77..248
FT                   /note="8 X 22 AA approximate tandem repeats"
FT   REGION          155..165
FT                   /note="LDL and other lipoprotein receptors binding"
FT                   /evidence="ECO:0000250|UniProtKB:P02649"
FT   REGION          203..283
FT                   /note="Lipid-binding and lipoprotein association"
FT                   /evidence="ECO:0000250|UniProtKB:P02649"
FT   REGION          259..310
FT                   /note="Homooligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P02649"
FT   REGION          271..283
FT                   /note="Specificity for association with VLDL"
FT                   /evidence="ECO:0000250|UniProtKB:P02649"
FT   BINDING         159..162
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250|UniProtKB:P02649"
FT   BINDING         222..229
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250|UniProtKB:P02649"
FT   MOD_RES         140
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P08226"
FT   MOD_RES         144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02649"
SQ   SEQUENCE   310 AA;  35638 MW;  5ECF6640CC052AA1 CRC64;
     MKVLWAALVV TLLAGCQADV EPEPEVQLGN EWAKWQAGQP WEQALGRFWN YLRWVQTLSD
     QVQEELLSTQ ATQELTALME ETMKEVKTYK AQLEQQLGPT AQETQARVSK ELQAAQARLG
     ADMEDVRNRL VQYRSELQAM MGQSTEELRG RLNSHLRKLR KRLLRDAEDL QKRLAVYQAG
     IREGAERSVN TLRERLRPLV EQAATVRSLI SKPLQERAEA WGQRLRGRLE KVGTQAGDRL
     DEVREQVQEV RAKVEEQANQ MRLQAEAFHA RLKSWFEPLV QDMQQKWAEL VEKVQLAVGT
     SPTSESSEKQ
 
 
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