APOA5_HUMAN
ID APOA5_HUMAN Reviewed; 366 AA.
AC Q6Q788; B0YIV9; Q3MIK6; Q6UWK9; Q9UBJ3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Apolipoprotein A-V;
DE Short=Apo-AV;
DE Short=ApoA-V;
DE AltName: Full=Apolipoprotein A5;
DE AltName: Full=Regeneration-associated protein 3;
DE Flags: Precursor;
GN Name=APOA5; Synonyms=RAP3; ORFNames=UNQ411/PRO773;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11577099; DOI=10.1074/jbc.m106888200;
RA van Der Vliet H.N., Sammels M.G., Leegwater A.C.J., Levels J.H.M.,
RA Reitsma P.H., Boers W., Chamuleau R.A.F.M.;
RT "Apolipoprotein A-V. A novel apolipoprotein associated with an early phase
RT of liver regeneration.";
RL J. Biol. Chem. 276:44512-44520(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-19 AND MET-153.
RX PubMed=15108119; DOI=10.1007/s00439-004-1106-x;
RA Fullerton S.M., Buchanan A.V., Sonpar V.A., Taylor S.L., Smith J.D.,
RA Carlson C.S., Salomaa V., Stengaard J.H., Boerwinkle E., Clark A.G.,
RA Nickerson D.A., Weiss K.M.;
RT "The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster.";
RL Hum. Genet. 115:36-56(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11588264; DOI=10.1126/science.1064852;
RA Pennacchio L.A., Olivier M., Hubacek J.A., Cohen J.C., Cox D.R.,
RA Fruchart J.-C., Krauss R.M., Rubin E.M.;
RT "An apolipoprotein influencing triglycerides in humans and mice revealed by
RT comparative sequencing.";
RL Science 294:169-173(2001).
RN [7]
RP FUNCTION.
RX PubMed=12899628; DOI=10.1021/bi034509t;
RA Beckstead J.A., Oda M.N., Martin D.D.O., Forte T.M., Bielicki J.K.,
RA Berger T., Luty R., Kay C.M., Ryan R.O.;
RT "Structure-function studies of human apolipoprotein A-V: a regulator of
RT plasma lipid homeostasis.";
RL Biochemistry 42:9416-9423(2003).
RN [8]
RP INDUCTION.
RX PubMed=12709436; DOI=10.1074/jbc.m301302200;
RA Prieur X., Coste H., Rodriguez J.C.;
RT "The human apolipoprotein AV gene is regulated by peroxisome proliferator-
RT activated receptor-alpha and contains a novel farnesoid X-activated
RT receptor response element.";
RL J. Biol. Chem. 278:25468-25480(2003).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12810715; DOI=10.1074/jbc.m303784200;
RA Weinberg R.B., Cook V.R., Beckstead J.A., Martin D.D.O., Gallagher J.W.,
RA Shelness G.S., Ryan R.O.;
RT "Structure and interfacial properties of human apolipoprotein A-V.";
RL J. Biol. Chem. 278:34438-34444(2003).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15528295; DOI=10.1373/clinchem.2004.040824;
RA O'Brien P.J., Alborn W.E., Sloan J.H., Ulmer M., Boodhoo A., Knierman M.D.,
RA Schultze A.E., Konrad R.J.;
RT "The novel apolipoprotein A5 is present in human serum, is associated with
RT VLDL, HDL, and chylomicrons, and circulates at very low concentrations
RT compared with other apolipoproteins.";
RL Clin. Chem. 51:351-359(2005).
RN [11]
RP INTERACTION WITH SORL1, BINDING TO HEPARIN, AND MUTAGENESIS OF
RP 233-ARG-LYS-234.
RX PubMed=17326667; DOI=10.1021/bi7000533;
RA Nilsson S.K., Lookene A., Beckstead J.A., Gliemann J., Ryan R.O.,
RA Olivecrona G.;
RT "Apolipoprotein A-V interaction with members of the low density lipoprotein
RT receptor gene family.";
RL Biochemistry 46:3896-3904(2007).
RN [12]
RP INTERACTION WITH GPIHBP1.
RX PubMed=17997385; DOI=10.1016/j.bbalip.2007.10.005;
RA Gin P., Beigneux A.P., Davies B., Young M.F., Ryan R.O., Bensadoun A.,
RA Fong L.G., Young S.G.;
RT "Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1
RT containing a G56R amino acid substitution.";
RL Biochim. Biophys. Acta 1771:1464-1468(2007).
RN [13]
RP INTERACTION WITH SORL1, AND SUBCELLULAR LOCATION.
RX PubMed=18603531; DOI=10.1074/jbc.m802721200;
RA Nilsson S.K., Christensen S., Raarup M.K., Ryan R.O., Nielsen M.S.,
RA Olivecrona G.;
RT "Endocytosis of apolipoprotein A-V by members of the low density
RT lipoprotein receptor and the VPS10p domain receptor families.";
RL J. Biol. Chem. 283:25920-25927(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP PHOSPHORYLATION AT THR-55.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [16]
RP POLYMORPHISM, AND VARIANT TRP-19.
RX PubMed=12417524; DOI=10.1093/hmg/11.24.3031;
RA Pennacchio L.A., Olivier M., Hubacek J.A., Krauss R.M., Rubin E.M.,
RA Cohen J.C.;
RT "Two independent apolipoprotein A5 haplotypes influence human plasma
RT triglyceride levels.";
RL Hum. Mol. Genet. 11:3031-3038(2002).
RN [17]
RP VARIANT TRP-19.
RX PubMed=12920097; DOI=10.1136/jmg.40.8.e105;
RA Vrablik M., Horinek A., Ceska R., Adamkova V., Poledne R., Hubacek J.A.;
RT "Ser19Trp polymorphism within the apolipoprotein AV gene in
RT hypertriglyceridaemic people.";
RL J. Med. Genet. 40:E105-E105(2003).
RN [18]
RP VARIANT CYS-185.
RX PubMed=12915450; DOI=10.1093/hmg/ddg255;
RA Kao J.-T., Wen H.-C., Chien K.-L., Hsu H.-C., Lin S.-W.;
RT "A novel genetic variant in the apolipoprotein A5 gene is associated with
RT hypertriglyceridemia.";
RL Hum. Mol. Genet. 12:2533-2539(2003).
RN [19]
RP INVOLVEMENT IN HLPP5.
RX PubMed=16200213; DOI=10.1172/jci24471;
RA Marcais C., Verges B., Charriere S., Pruneta V., Merlin M., Billon S.,
RA Perrot L., Drai J., Sassolas A., Pennacchio L.A., Fruchart-Najib J.,
RA Fruchart J.C., Durlach V., Moulin P.;
RT "Apoa5 Q139X truncation predisposes to late-onset hyperchylomicronemia due
RT to lipoprotein lipase impairment.";
RL J. Clin. Invest. 115:2862-2869(2005).
CC -!- FUNCTION: Minor apolipoprotein mainly associated with HDL and to a
CC lesser extent with VLDL. May also be associated with chylomicrons.
CC Important determinant of plasma triglyceride (TG) levels by both being
CC a potent stimulator of apo-CII lipoprotein lipase (LPL) TG hydrolysis
CC and an inhibitor of the hepatic VLDL-TG production rate (without
CC affecting the VLDL-apoB production rate) (By similarity). Activates
CC poorly lecithin:cholesterol acyltransferase (LCAT) and does not enhance
CC efflux of cholesterol from macrophages. Binds heparin
CC (PubMed:17326667). {ECO:0000250|UniProtKB:Q8C7G5,
CC ECO:0000269|PubMed:11588264, ECO:0000269|PubMed:12899628,
CC ECO:0000269|PubMed:15528295, ECO:0000269|PubMed:17326667}.
CC -!- SUBUNIT: Interacts with GPIHBP1 (PubMed:17997385). Interacts with
CC SORL1; this interaction leads to APOA5 internalization and sorting
CC either to lysosomes and degradation, or to the trans-Golgi network
CC (PubMed:17326667, PubMed:18603531). {ECO:0000269|PubMed:17326667,
CC ECO:0000269|PubMed:17997385, ECO:0000269|PubMed:18603531}.
CC -!- INTERACTION:
CC Q6Q788; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-3936819, EBI-2876502;
CC Q6Q788; O95393: BMP10; NbExp=3; IntAct=EBI-3936819, EBI-3922513;
CC Q6Q788; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-3936819, EBI-7247651;
CC Q6Q788; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-3936819, EBI-11522780;
CC Q6Q788; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-3936819, EBI-1054315;
CC Q6Q788; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-3936819, EBI-10269566;
CC Q6Q788; Q9HB07: MYG1; NbExp=3; IntAct=EBI-3936819, EBI-709754;
CC Q6Q788; Q9BQE4: SELENOS; NbExp=3; IntAct=EBI-3936819, EBI-398970;
CC Q6Q788; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-3936819, EBI-10171534;
CC Q6Q788; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-3936819, EBI-741829;
CC Q6Q788; Q9BTV4: TMEM43; NbExp=3; IntAct=EBI-3936819, EBI-721293;
CC Q6Q788; P49638: TTPA; NbExp=3; IntAct=EBI-3936819, EBI-10210710;
CC Q6Q788; O95070: YIF1A; NbExp=3; IntAct=EBI-3936819, EBI-2799703;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12810715}. Early
CC endosome {ECO:0000269|PubMed:18603531}. Late endosome
CC {ECO:0000269|PubMed:18603531}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:18603531}. Note=In the presence of SORL1,
CC internalized to early endosomes, sorted in a retrograde fashion to late
CC endosomes, from which a portion is sent to lysosomes and degradation,
CC another portion is sorted to the trans-Golgi network.
CC {ECO:0000269|PubMed:18603531}.
CC -!- TISSUE SPECIFICITY: Liver and plasma. {ECO:0000269|PubMed:11577099,
CC ECO:0000269|PubMed:11588264, ECO:0000269|PubMed:15528295}.
CC -!- INDUCTION: Up-regulated by PPARA agonists, which are used clinically to
CC lower serum TG (such as fibrates). {ECO:0000269|PubMed:12709436}.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000269|PubMed:26091039}.
CC -!- POLYMORPHISM: Three common alleles are known: allele APOA5*1, APOA5*2
CC and APOA5*3. The APOA5*2 haplotype, which consists of 3 non-coding
CC SNPs, is present in approximately 16% of Caucasians and is associated
CC with increased plasma triglyceride concentrations. APOA5*3 haplotype is
CC defined by the rare Ser-19-Trp substitution. Together, the APOA5*2 and
CC APOA5*3 haplotypes are found in 25 to 50% of African Americans,
CC Hispanics, and Caucasians. {ECO:0000269|PubMed:12417524}.
CC -!- DISEASE: Hypertriglyceridemia, familial (FHTR) [MIM:145750]: A common
CC inherited disorder in which the concentration of very low density
CC lipoprotein (VLDL) is elevated in the plasma. This leads to increased
CC risk of heart disease, obesity, and pancreatitis. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- DISEASE: Hyperlipoproteinemia 5 (HLPP5) [MIM:144650]: Characterized by
CC increased amounts of chylomicrons and very low density lipoprotein
CC (VLDL) and decreased low density lipoprotein (LDL) and high density
CC lipoprotein (HDL) in the plasma after a fast. Numerous conditions cause
CC this phenotype, including insulin-dependent diabetes mellitus,
CC contraceptive steroids, alcohol abuse, and glycogen storage disease
CC type 1A (GSD1A). {ECO:0000269|PubMed:16200213}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Induced in early phase of liver regeneration.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF25661.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAF25662.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAQ89109.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF202889; AAF25661.1; ALT_INIT; mRNA.
DR EMBL; AF202890; AAF25662.1; ALT_INIT; mRNA.
DR EMBL; AY555191; AAS68229.1; -; Genomic_DNA.
DR EMBL; AY422949; AAQ91808.1; -; Genomic_DNA.
DR EMBL; AY358749; AAQ89109.1; ALT_SEQ; mRNA.
DR EMBL; EF444949; ACA05937.1; -; Genomic_DNA.
DR EMBL; EF444949; ACA05938.1; -; Genomic_DNA.
DR EMBL; BC101787; AAI01788.1; -; mRNA.
DR EMBL; BC101789; AAI01790.1; -; mRNA.
DR CCDS; CCDS8376.2; -.
DR RefSeq; NP_001160070.1; NM_001166598.1.
DR RefSeq; NP_443200.2; NM_052968.4.
DR RefSeq; XP_016872658.1; XM_017017169.1.
DR AlphaFoldDB; Q6Q788; -.
DR SMR; Q6Q788; -.
DR BioGRID; 125518; 16.
DR IntAct; Q6Q788; 22.
DR STRING; 9606.ENSP00000445002; -.
DR iPTMnet; Q6Q788; -.
DR PhosphoSitePlus; Q6Q788; -.
DR BioMuta; APOA5; -.
DR DMDM; 60391728; -.
DR MassIVE; Q6Q788; -.
DR MaxQB; Q6Q788; -.
DR PaxDb; Q6Q788; -.
DR PeptideAtlas; Q6Q788; -.
DR PRIDE; Q6Q788; -.
DR ProteomicsDB; 67276; -.
DR Antibodypedia; 32277; 773 antibodies from 33 providers.
DR DNASU; 116519; -.
DR Ensembl; ENST00000227665.9; ENSP00000227665.4; ENSG00000110243.12.
DR Ensembl; ENST00000433069.2; ENSP00000399701.2; ENSG00000110243.12.
DR Ensembl; ENST00000542499.5; ENSP00000445002.1; ENSG00000110243.12.
DR GeneID; 116519; -.
DR KEGG; hsa:116519; -.
DR MANE-Select; ENST00000227665.9; ENSP00000227665.4; NM_001371904.1; NP_001358833.1.
DR UCSC; uc001ppr.4; human.
DR CTD; 116519; -.
DR DisGeNET; 116519; -.
DR GeneCards; APOA5; -.
DR HGNC; HGNC:17288; APOA5.
DR HPA; ENSG00000110243; Tissue enriched (liver).
DR MalaCards; APOA5; -.
DR MIM; 144650; phenotype.
DR MIM; 145750; phenotype.
DR MIM; 606368; gene.
DR neXtProt; NX_Q6Q788; -.
DR OpenTargets; ENSG00000110243; -.
DR Orphanet; 530849; Familial apolipoprotein A5 deficiency.
DR Orphanet; 413; NON RARE IN EUROPE: Hyperlipoproteinemia type 4.
DR PharmGKB; PA24888; -.
DR VEuPathDB; HostDB:ENSG00000110243; -.
DR eggNOG; ENOG502S33P; Eukaryota.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_747959_0_0_1; -.
DR InParanoid; Q6Q788; -.
DR OMA; AFRQDTF; -.
DR OrthoDB; 813395at2759; -.
DR PhylomeDB; Q6Q788; -.
DR TreeFam; TF334458; -.
DR PathwayCommons; Q6Q788; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
DR Reactome; R-HSA-8963901; Chylomicron remodeling.
DR SignaLink; Q6Q788; -.
DR SIGNOR; Q6Q788; -.
DR BioGRID-ORCS; 116519; 9 hits in 1069 CRISPR screens.
DR GeneWiki; APOA5; -.
DR GenomeRNAi; 116519; -.
DR Pharos; Q6Q788; Tbio.
DR PRO; PR:Q6Q788; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6Q788; protein.
DR Bgee; ENSG00000110243; Expressed in right lobe of liver and 50 other tissues.
DR ExpressionAtlas; Q6Q788; baseline and differential.
DR Genevisible; Q6Q788; HS.
DR GO; GO:0042627; C:chylomicron; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IDA:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
DR GO; GO:0060229; F:lipase activator activity; IMP:BHF-UCL.
DR GO; GO:0035473; F:lipase binding; IPI:BHF-UCL.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR GO; GO:0060230; F:lipoprotein lipase activator activity; IDA:BHF-UCL.
DR GO; GO:0070325; F:lipoprotein particle receptor binding; IPI:BHF-UCL.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:BHF-UCL.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
DR GO; GO:0055090; P:acylglycerol homeostasis; IDA:BHF-UCL.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IDA:BHF-UCL.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
DR GO; GO:0033700; P:phospholipid efflux; IBA:GO_Central.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; IBA:GO_Central.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IDA:BHF-UCL.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:BHF-UCL.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; TAS:BHF-UCL.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:BHF-UCL.
DR GO; GO:0010902; P:positive regulation of very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IBA:GO_Central.
DR GO; GO:0042246; P:tissue regeneration; IEP:UniProtKB.
DR GO; GO:0019433; P:triglyceride catabolic process; IMP:BHF-UCL.
DR GO; GO:0070328; P:triglyceride homeostasis; IDA:BHF-UCL.
DR GO; GO:0006641; P:triglyceride metabolic process; IDA:BHF-UCL.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IBA:GO_Central.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 2.
PE 1: Evidence at protein level;
KW Chylomicron; Coiled coil; Disease variant; Endosome; Golgi apparatus; HDL;
KW Lipid transport; Phosphoprotein; Reference proteome; Secreted; Signal;
KW Transport; VLDL.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..366
FT /note="Apolipoprotein A-V"
FT /id="PRO_0000001981"
FT COILED 54..157
FT /evidence="ECO:0000255"
FT COILED 236..262
FT /evidence="ECO:0000255"
FT MOD_RES 55
FT /note="Phosphothreonine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 19
FT /note="S -> W (in allele APOA5*3; associated with high
FT plasma triglyceride levels; dbSNP:rs3135506)"
FT /evidence="ECO:0000269|PubMed:12417524,
FT ECO:0000269|PubMed:12920097, ECO:0000269|PubMed:15108119"
FT /id="VAR_021165"
FT VARIANT 37
FT /note="D -> E (in dbSNP:rs34282181)"
FT /id="VAR_035124"
FT VARIANT 153
FT /note="V -> M (in dbSNP:rs3135507)"
FT /evidence="ECO:0000269|PubMed:15108119"
FT /id="VAR_021166"
FT VARIANT 185
FT /note="G -> C (associated with high plasma triglyceride
FT levels; dbSNP:rs2075291)"
FT /evidence="ECO:0000269|PubMed:12915450"
FT /id="VAR_021167"
FT MUTAGEN 233..234
FT /note="RK->EQ: Decreased heparin-binding."
FT /evidence="ECO:0000269|PubMed:17326667"
SQ SEQUENCE 366 AA; 41213 MW; A1C9C207024D0DAF CRC64;
MASMAAVLTW ALALLSAFSA TQARKGFWDY FSQTSGDKGR VEQIHQQKMA REPATLKDSL
EQDLNNMNKF LEKLRPLSGS EAPRLPQDPV GMRRQLQEEL EEVKARLQPY MAEAHELVGW
NLEGLRQQLK PYTMDLMEQV ALRVQELQEQ LRVVGEDTKA QLLGGVDEAW ALLQGLQSRV
VHHTGRFKEL FHPYAESLVS GIGRHVQELH RSVAPHAPAS PARLSRCVQV LSRKLTLKAK
ALHARIQQNL DQLREELSRA FAGTGTEEGA GPDPQMLSEE VRQRLQAFRQ DTYLQIAAFT
RAIDQETEEV QQQLAPPPPG HSAFAPEFQQ TDSGKVLSKL QARLDDLWED ITHSLHDQGH
SHLGDP
