APOE_RAT
ID APOE_RAT Reviewed; 312 AA.
AC P02650;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Apolipoprotein E;
DE Short=Apo-E;
DE Flags: Precursor;
GN Name=Apoe;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3797247; DOI=10.1093/nar/14.23.9527;
RA Fukazawa C., Matsumoto A., Taylor L.M.;
RT "Complete nucleotide sequence of the gene encoding the rat apolipoprotein
RT E.";
RL Nucleic Acids Res. 14:9527-9528(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3020048; DOI=10.1016/s0021-9258(18)67087-5;
RA Fung W.-P., Howlett G.J., Schreiber G.;
RT "Structure and expression of the rat apolipoprotein E gene.";
RL J. Biol. Chem. 261:13777-13783(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6190813; DOI=10.1016/s0021-9258(18)32155-0;
RA McLean J.W., Fukazawa C., Taylor J.M.;
RT "Rat apolipoprotein E mRNA. Cloning and sequencing of double-stranded
RT cDNA.";
RL J. Biol. Chem. 258:8993-9000(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=7766086; DOI=10.1007/bf00191183;
RA Nomura N., Yamada H., Matsubara N., Horinouchi S., Beppu T.;
RT "Secretion by Saccharomyces cerevisiae of rat apolipoprotein E as a fusion
RT to Mucor rennin.";
RL Appl. Microbiol. Biotechnol. 42:865-870(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 87-100; 114-122; 130-144; 191-199; 202-216; 226-236 AND
RP 262-270, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 and the very low-density lipoprotein receptor/VLDLR that
CC mediate the cellular uptake of the APOE-containing lipoprotein
CC particles. Finally, APOE has also a heparin-binding activity and binds
CC heparan-sulfate proteoglycans on the surface of cells, a property that
CC supports the capture and the receptor-mediated uptake of APOE-
CC containing lipoproteins by cells. {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 -!- MISCELLANEOUS: The mature protein has no cysteine residues; however, in
CC different allelic variants where cysteine residues replace arginine at
CC positions 155 or 168, binding of Apo-E to cell membrane receptors is
CC decreased. The amino end of this protein is therefore thought to
CC interact with the receptor.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; X04979; CAA28650.1; -; Genomic_DNA.
DR EMBL; J02582; AAA40755.1; -; Genomic_DNA.
DR EMBL; S76779; AAC60703.1; -; mRNA.
DR EMBL; BC086581; AAH86581.1; -; mRNA.
DR PIR; A26189; LPRTE.
DR RefSeq; NP_001257610.1; NM_001270681.1.
DR RefSeq; NP_001257611.1; NM_001270682.1.
DR RefSeq; NP_001257612.1; NM_001270683.1.
DR RefSeq; NP_001257613.1; NM_001270684.1.
DR RefSeq; NP_620183.2; NM_138828.3.
DR AlphaFoldDB; P02650; -.
DR SMR; P02650; -.
DR BioGRID; 247757; 3.
DR IntAct; P02650; 4.
DR STRING; 10116.ENSRNOP00000050968; -.
DR iPTMnet; P02650; -.
DR PhosphoSitePlus; P02650; -.
DR PaxDb; P02650; -.
DR PRIDE; P02650; -.
DR GeneID; 25728; -.
DR KEGG; rno:25728; -.
DR UCSC; RGD:2138; rat.
DR CTD; 348; -.
DR RGD; 2138; Apoe.
DR VEuPathDB; HostDB:ENSRNOG00000018454; -.
DR eggNOG; ENOG502QVD6; Eukaryota.
DR InParanoid; P02650; -.
DR OrthoDB; 1314660at2759; -.
DR PhylomeDB; P02650; -.
DR TreeFam; TF334458; -.
DR Reactome; R-RNO-3000480; Scavenging by Class A Receptors.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR Reactome; R-RNO-8963888; Chylomicron assembly.
DR Reactome; R-RNO-8963901; Chylomicron remodeling.
DR Reactome; R-RNO-8964026; Chylomicron clearance.
DR Reactome; R-RNO-8964058; HDL remodeling.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:P02650; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018454; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; P02650; baseline and differential.
DR Genevisible; P02650; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0042627; C:chylomicron; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0034365; C:discoidal high-density lipoprotein particle; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:ARUK-UCL.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; IDA:ARUK-UCL.
DR GO; GO:0005770; C:late endosome; IDA:RGD.
DR GO; GO:1990777; C:lipoprotein particle; ISO:RGD.
DR GO; GO:0034362; C:low-density lipoprotein particle; IDA:ARUK-UCL.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0043083; C:synaptic cleft; ISO:RGD.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:ARUK-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:RGD.
DR GO; GO:0016209; F:antioxidant activity; ISO:RGD.
DR GO; GO:0120020; F:cholesterol transfer activity; ISO:RGD.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0046848; F:hydroxyapatite binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; ISO:RGD.
DR GO; GO:0005319; F:lipid transporter activity; IDA:RGD.
DR GO; GO:0071813; F:lipoprotein particle binding; ISO:RGD.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISS:UniProtKB.
DR GO; GO:0046911; F:metal chelating activity; ISO:RGD.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; IDA:RGD.
DR GO; GO:0046983; F:protein dimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0048156; F:tau protein binding; ISO:RGD.
DR GO; GO:0070326; F:very-low-density lipoprotein particle receptor binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IDA:RGD.
DR GO; GO:0097113; P:AMPA glutamate receptor clustering; ISO:RGD.
DR GO; GO:0042982; P:amyloid precursor protein metabolic process; ISO:RGD.
DR GO; GO:0048844; P:artery morphogenesis; ISO:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0071397; P:cellular response to cholesterol; IEP:RGD.
DR GO; GO:0071361; P:cellular response to ethanol; IEP:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0019934; P:cGMP-mediated signaling; ISO:RGD.
DR GO; GO:0006707; P:cholesterol catabolic process; ISO:RGD.
DR GO; GO:0033344; P:cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR GO; GO:0034382; P:chylomicron remnant clearance; ISS:UniProtKB.
DR GO; GO:0072359; P:circulatory system development; ISO:RGD.
DR GO; GO:0055089; P:fatty acid homeostasis; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; ISS:UniProtKB.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0071831; P:intermediate-density lipoprotein particle clearance; ISS:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR GO; GO:0006869; P:lipid transport; IDA:RGD.
DR GO; GO:0010877; P:lipid transport involved in lipid storage; ISO:RGD.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; ISS:UniProtKB.
DR GO; GO:0042159; P:lipoprotein catabolic process; ISO:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; IDA:RGD.
DR GO; GO:0035641; P:locomotory exploration behavior; ISO:RGD.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISO:RGD.
DR GO; GO:0007616; P:long-term memory; ISO:RGD.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0051651; P:maintenance of location in cell; ISO:RGD.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISS:UniProtKB.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISO:RGD.
DR GO; GO:0030195; P:negative regulation of blood coagulation; ISO:RGD.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IDA:RGD.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:0010544; P:negative regulation of platelet activation; ISO:RGD.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISO:RGD.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0090209; P:negative regulation of triglyceride metabolic process; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0031102; P:neuron projection regeneration; TAS:RGD.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; ISO:RGD.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; ISO:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEP:RGD.
DR GO; GO:0033700; P:phospholipid efflux; ISO:RGD.
DR GO; GO:0044794; P:positive regulation by host of viral process; ISO:RGD.
DR GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISS:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; IDA:RGD.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:RGD.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; ISO:RGD.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:RGD.
DR GO; GO:1902952; P:positive regulation of dendritic spine maintenance; ISO:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:1905855; P:positive regulation of heparan sulfate binding; ISO:RGD.
DR GO; GO:1905860; P:positive regulation of heparan sulfate proteoglycan binding; ISO:RGD.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISO:RGD.
DR GO; GO:1903002; P:positive regulation of lipid transport across blood-brain barrier; ISO:RGD.
DR GO; GO:0032805; P:positive regulation of low-density lipoprotein particle receptor catabolic process; ISO:RGD.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISO:RGD.
DR GO; GO:1902995; P:positive regulation of phospholipid efflux; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0017038; P:protein import; ISO:RGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
DR GO; GO:1905906; P:regulation of amyloid fibril formation; ISO:RGD.
DR GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; ISO:RGD.
DR GO; GO:1900221; P:regulation of amyloid-beta clearance; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR GO; GO:2000822; P:regulation of behavioral fear response; ISO:RGD.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:RGD.
DR GO; GO:1905890; P:regulation of cellular response to very-low-density lipoprotein particle stimulus; ISO:RGD.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0045088; P:regulation of innate immune response; ISO:RGD.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; ISO:RGD.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:RGD.
DR GO; GO:0051246; P:regulation of protein metabolic process; ISO:RGD.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:RGD.
DR GO; GO:0090207; P:regulation of triglyceride metabolic process; IDA:RGD.
DR GO; GO:0061771; P:response to caloric restriction; ISO:RGD.
DR GO; GO:1904421; P:response to D-galactosamine; IEP:RGD.
DR GO; GO:0002021; P:response to dietary excess; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0034612; P:response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:RGD.
DR GO; GO:0070328; P:triglyceride homeostasis; ISO:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR GO; GO:0071830; P:triglyceride-rich lipoprotein particle clearance; ISS:UniProtKB.
DR GO; GO:0042311; P:vasodilation; ISO:RGD.
DR GO; GO:0034447; P:very-low-density lipoprotein particle clearance; ISS:UniProtKB.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0019068; P:virion assembly; ISO:RGD.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 1.
PE 1: Evidence at protein level;
KW Chylomicron; Direct protein sequencing; Extracellular matrix; Glycoprotein;
KW HDL; Heparin-binding; Lipid transport; Lipid-binding; Oxidation;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal; Transport;
KW VLDL.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..312
FT /note="Apolipoprotein E"
FT /id="PRO_0000001996"
FT REPEAT 72..93
FT /note="1"
FT REPEAT 94..115
FT /note="2"
FT REPEAT 116..137
FT /note="3"
FT REPEAT 138..159
FT /note="4"
FT REPEAT 160..181
FT /note="5"
FT REPEAT 182..203
FT /note="6"
FT REPEAT 204..225
FT /note="7"
FT REPEAT 226..247
FT /note="8"
FT REGION 72..247
FT /note="8 X 22 AA approximate tandem repeats"
FT REGION 150..160
FT /note="LDL and other lipoprotein receptors binding"
FT /evidence="ECO:0000250|UniProtKB:P02649"
FT REGION 150..160
FT /note="LDL receptor binding"
FT /evidence="ECO:0000250|UniProtKB:P02649"
FT REGION 202..282
FT /note="Lipid-binding and lipoprotein association"
FT /evidence="ECO:0000250|UniProtKB:P02649"
FT REGION 258..312
FT /note="Homooligomerization"
FT /evidence="ECO:0000250|UniProtKB:P02649"
FT REGION 270..282
FT /note="Specificity for association with VLDL"
FT /evidence="ECO:0000250|UniProtKB:P02649"
FT BINDING 154..157
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:P02649"
FT BINDING 221..228
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:P02649"
FT MOD_RES 135
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P08226"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 104
FT /note="A -> T (in Ref. 1; CAA28650)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="A -> T (in Ref. 3; no nucleotide entry and 4;
FT AAC60703)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="E -> D (in Ref. 3; no nucleotide entry and 4;
FT AAC60703)"
FT /evidence="ECO:0000305"
FT CONFLICT 206..213
FT /note="GAGAAQPL -> RWRRPAP (in Ref. 1; CAA28650 and 3; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 309..310
FT /note="LE -> WR (in Ref. 3; no nucleotide entry and 4;
FT AAC60703)"
FT /evidence="ECO:0000305"
SQ 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
