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Apolipoprotein A-V (Apo-AV) (ApoA-V) (Apolipoprotein A5) (Regeneration-associated protein 3)

 APOA5_HUMAN             Reviewed;         366 AA.
Q6Q788; B0YIV9; Q3MIK6; Q6UWK9; Q9UBJ3;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
12-SEP-2018, entry version 136.
RecName: Full=Apolipoprotein A-V;
Short=Apo-AV;
Short=ApoA-V;
AltName: Full=Apolipoprotein A5;
AltName: Full=Regeneration-associated protein 3;
Flags: Precursor;
Name=APOA5; Synonyms=RAP3; ORFNames=UNQ411/PRO773;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=11577099; DOI=10.1074/jbc.M106888200;
van Der Vliet H.N., Sammels M.G., Leegwater A.C.J., Levels J.H.M.,
Reitsma P.H., Boers W., Chamuleau R.A.F.M.;
"Apolipoprotein A-V. A novel apolipoprotein associated with an early
phase of liver regeneration.";
J. Biol. Chem. 276:44512-44520(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-19 AND MET-153.
PubMed=15108119; DOI=10.1007/s00439-004-1106-x;
Fullerton S.M., Buchanan A.V., Sonpar V.A., Taylor S.L., Smith J.D.,
Carlson C.S., Salomaa V., Stengaard J.H., Boerwinkle E., Clark A.G.,
Nickerson D.A., Weiss K.M.;
"The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster.";
Hum. Genet. 115:36-56(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11588264; DOI=10.1126/science.1064852;
Pennacchio L.A., Olivier M., Hubacek J.A., Cohen J.C., Cox D.R.,
Fruchart J.-C., Krauss R.M., Rubin E.M.;
"An apolipoprotein influencing triglycerides in humans and mice
revealed by comparative sequencing.";
Science 294:169-173(2001).
[7]
FUNCTION.
PubMed=12899628; DOI=10.1021/bi034509t;
Beckstead J.A., Oda M.N., Martin D.D.O., Forte T.M., Bielicki J.K.,
Berger T., Luty R., Kay C.M., Ryan R.O.;
"Structure-function studies of human apolipoprotein A-V: a regulator
of plasma lipid homeostasis.";
Biochemistry 42:9416-9423(2003).
[8]
INDUCTION.
PubMed=12709436; DOI=10.1074/jbc.M301302200;
Prieur X., Coste H., Rodriguez J.C.;
"The human apolipoprotein AV gene is regulated by peroxisome
proliferator-activated receptor-alpha and contains a novel farnesoid
X-activated receptor response element.";
J. Biol. Chem. 278:25468-25480(2003).
[9]
SUBCELLULAR LOCATION.
PubMed=12810715; DOI=10.1074/jbc.M303784200;
Weinberg R.B., Cook V.R., Beckstead J.A., Martin D.D.O.,
Gallagher J.W., Shelness G.S., Ryan R.O.;
"Structure and interfacial properties of human apolipoprotein A-V.";
J. Biol. Chem. 278:34438-34444(2003).
[10]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15528295; DOI=10.1373/clinchem.2004.040824;
O'Brien P.J., Alborn W.E., Sloan J.H., Ulmer M., Boodhoo A.,
Knierman M.D., Schultze A.E., Konrad R.J.;
"The novel apolipoprotein A5 is present in human serum, is associated
with VLDL, HDL, and chylomicrons, and circulates at very low
concentrations compared with other apolipoproteins.";
Clin. Chem. 51:351-359(2005).
[11]
INTERACTION WITH GPIHBP1.
PubMed=17997385; DOI=10.1016/j.bbalip.2007.10.005;
Gin P., Beigneux A.P., Davies B., Young M.F., Ryan R.O., Bensadoun A.,
Fong L.G., Young S.G.;
"Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to
GPIHBP1 containing a G56R amino acid substitution.";
Biochim. Biophys. Acta 1771:1464-1468(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
PHOSPHORYLATION AT THR-55.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[14]
POLYMORPHISM, AND VARIANT TRP-19.
PubMed=12417524; DOI=10.1093/hmg/11.24.3031;
Pennacchio L.A., Olivier M., Hubacek J.A., Krauss R.M., Rubin E.M.,
Cohen J.C.;
"Two independent apolipoprotein A5 haplotypes influence human plasma
triglyceride levels.";
Hum. Mol. Genet. 11:3031-3038(2002).
[15]
VARIANT TRP-19.
PubMed=12920097; DOI=10.1136/jmg.40.8.e105;
Vrablik M., Horinek A., Ceska R., Adamkova V., Poledne R.,
Hubacek J.A.;
"Ser19Trp polymorphism within the apolipoprotein AV gene in
hypertriglyceridaemic people.";
J. Med. Genet. 40:E105-E105(2003).
[16]
VARIANT CYS-185.
PubMed=12915450; DOI=10.1093/hmg/ddg255;
Kao J.-T., Wen H.-C., Chien K.-L., Hsu H.-C., Lin S.-W.;
"A novel genetic variant in the apolipoprotein A5 gene is associated
with hypertriglyceridemia.";
Hum. Mol. Genet. 12:2533-2539(2003).
[17]
INVOLVEMENT IN HLPP5.
PubMed=16200213; DOI=10.1172/JCI24471;
Marcais C., Verges B., Charriere S., Pruneta V., Merlin M., Billon S.,
Perrot L., Drai J., Sassolas A., Pennacchio L.A., Fruchart-Najib J.,
Fruchart J.C., Durlach V., Moulin P.;
"Apoa5 Q139X truncation predisposes to late-onset hyperchylomicronemia
due to lipoprotein lipase impairment.";
J. Clin. Invest. 115:2862-2869(2005).
-!- FUNCTION: Minor apolipoprotein mainly associated with HDL and to a
lesser extent with VLDL. May also be associated with chylomicrons.
Important determinant of plasma triglyceride (TG) levels by both
being a potent stimulator of apo-CII lipoprotein lipase (LPL) TG
hydrolysis and a inhibitor of the hepatic VLDL-TG production rate
(without affecting the VLDL-apoB production rate) (By similarity).
Activates poorly lecithin:cholesterol acyltransferase (LCAT) and
does not enhance efflux of cholesterol from macrophages.
{ECO:0000250, ECO:0000269|PubMed:11588264,
ECO:0000269|PubMed:12899628, ECO:0000269|PubMed:15528295}.
-!- SUBUNIT: Interacts with GPIHBP1. {ECO:0000269|PubMed:17997385}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12810715}.
-!- TISSUE SPECIFICITY: Liver and plasma.
{ECO:0000269|PubMed:11577099, ECO:0000269|PubMed:11588264,
ECO:0000269|PubMed:15528295}.
-!- INDUCTION: Up-regulated by PPARA agonists, which are used
clinically to lower serum TG (such as fibrates).
{ECO:0000269|PubMed:12709436}.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000269|PubMed:26091039}.
-!- POLYMORPHISM: Three common alleles are known: allele APOA5*1,
APOA5*2 and APOA5*3. The APOA5*2 haplotype, which consists of 3
non-coding SNPs, is present in approximately 16% of Caucasians and
is associated with increased plasma triglyceride concentrations.
APOA5*3 haplotype is defined by the rare Ser-19-Trp substitution.
Together, the APOA5*2 and APOA5*3 haplotypes are found in 25 to
50% of African Americans, Hispanics, and Caucasians.
{ECO:0000269|PubMed:12417524}.
-!- DISEASE: Hypertriglyceridemia, familial (FHTR) [MIM:145750]: A
common inherited disorder in which the concentration of very low
density lipoprotein (VLDL) is elevated in the plasma. This leads
to increased risk of heart disease, obesity, and pancreatitis.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Hyperlipoproteinemia 5 (HLPP5) [MIM:144650]:
Characterized by increased amounts of chylomicrons and very low
density lipoprotein (VLDL) and decreased low density lipoprotein
(LDL) and high density lipoprotein (HDL) in the plasma after a
fast. Numerous conditions cause this phenotype, including insulin-
dependent diabetes mellitus, contraceptive steroids, alcohol
abuse, and glycogen storage disease type 1A (GSD1A).
{ECO:0000269|PubMed:16200213}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Induced in early phase of liver regeneration.
-!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF25661.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAF25662.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAQ89109.1; Type=Erroneous termination; Positions=275; Note=Translated as Gln.; Evidence={ECO:0000305};
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EMBL; AF202889; AAF25661.1; ALT_INIT; mRNA.
EMBL; AF202890; AAF25662.1; ALT_INIT; mRNA.
EMBL; AY555191; AAS68229.1; -; Genomic_DNA.
EMBL; AY422949; AAQ91808.1; -; Genomic_DNA.
EMBL; AY358749; AAQ89109.1; ALT_SEQ; mRNA.
EMBL; EF444949; ACA05937.1; -; Genomic_DNA.
EMBL; EF444949; ACA05938.1; -; Genomic_DNA.
EMBL; BC101787; AAI01788.1; -; mRNA.
EMBL; BC101789; AAI01790.1; -; mRNA.
CCDS; CCDS8376.2; -.
RefSeq; NP_001160070.1; NM_001166598.1.
RefSeq; NP_443200.2; NM_052968.4.
RefSeq; XP_016872658.1; XM_017017169.1.
UniGene; Hs.283923; -.
ProteinModelPortal; Q6Q788; -.
SMR; Q6Q788; -.
BioGrid; 125518; 3.
IntAct; Q6Q788; 22.
STRING; 9606.ENSP00000227665; -.
iPTMnet; Q6Q788; -.
PhosphoSitePlus; Q6Q788; -.
BioMuta; APOA5; -.
DMDM; 60391728; -.
MaxQB; Q6Q788; -.
PaxDb; Q6Q788; -.
PeptideAtlas; Q6Q788; -.
PRIDE; Q6Q788; -.
ProteomicsDB; 67276; -.
Ensembl; ENST00000227665; ENSP00000227665; ENSG00000110243.
Ensembl; ENST00000542499; ENSP00000445002; ENSG00000110243.
GeneID; 116519; -.
KEGG; hsa:116519; -.
UCSC; uc001ppr.4; human.
CTD; 116519; -.
DisGeNET; 116519; -.
EuPathDB; HostDB:ENSG00000110243.11; -.
GeneCards; APOA5; -.
HGNC; HGNC:17288; APOA5.
MalaCards; APOA5; -.
MIM; 144650; phenotype.
MIM; 145750; phenotype.
MIM; 606368; gene.
neXtProt; NX_Q6Q788; -.
OpenTargets; ENSG00000110243; -.
Orphanet; 413; Hyperlipoproteinemia type 4.
Orphanet; 70470; Hyperlipoproteinemia type 5.
PharmGKB; PA24888; -.
eggNOG; ENOG410IKFF; Eukaryota.
eggNOG; ENOG410YHUG; LUCA.
GeneTree; ENSGT00530000063081; -.
HOGENOM; HOG000253942; -.
HOVERGEN; HBG050545; -.
InParanoid; Q6Q788; -.
KO; K09025; -.
OMA; HRSVAPH; -.
OrthoDB; EOG091G0IA5; -.
PhylomeDB; Q6Q788; -.
TreeFam; TF334458; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
Reactome; R-HSA-8963901; Chylomicron remodeling.
SIGNOR; Q6Q788; -.
GeneWiki; APOA5; -.
GenomeRNAi; 116519; -.
PRO; PR:Q6Q788; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110243; Expressed in 31 organ(s), highest expression level in right lobe of liver.
CleanEx; HS_APOA5; -.
ExpressionAtlas; Q6Q788; baseline and differential.
Genevisible; Q6Q788; HS.
GO; GO:0072562; C:blood microparticle; IBA:GO_Central.
GO; GO:0042627; C:chylomicron; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
GO; GO:0017127; F:cholesterol transporter activity; IBA:GO_Central.
GO; GO:0008047; F:enzyme activator activity; IDA:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IDA:BHF-UCL.
GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
GO; GO:0060229; F:lipase activator activity; IMP:BHF-UCL.
GO; GO:0035473; F:lipase binding; IPI:BHF-UCL.
GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
GO; GO:0060230; F:lipoprotein lipase activator activity; IDA:BHF-UCL.
GO; GO:0070325; F:lipoprotein particle receptor binding; IPI:BHF-UCL.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:BHF-UCL.
GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IBA:GO_Central.
GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
GO; GO:0055090; P:acylglycerol homeostasis; IDA:BHF-UCL.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
GO; GO:0033344; P:cholesterol efflux; IBA:GO_Central.
GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
GO; GO:0006869; P:lipid transport; IDA:BHF-UCL.
GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
GO; GO:0031102; P:neuron projection regeneration; IBA:GO_Central.
GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
GO; GO:0033700; P:phospholipid efflux; IBA:GO_Central.
GO; GO:0010873; P:positive regulation of cholesterol esterification; IBA:GO_Central.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IDA:BHF-UCL.
GO; GO:0050996; P:positive regulation of lipid catabolic process; IDA:BHF-UCL.
GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:BHF-UCL.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; TAS:BHF-UCL.
GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:BHF-UCL.
GO; GO:0010902; P:positive regulation of very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IBA:GO_Central.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0043691; P:reverse cholesterol transport; IBA:GO_Central.
GO; GO:0042246; P:tissue regeneration; IEP:UniProtKB.
GO; GO:0019433; P:triglyceride catabolic process; IMP:BHF-UCL.
GO; GO:0070328; P:triglyceride homeostasis; IDA:BHF-UCL.
GO; GO:0006641; P:triglyceride metabolic process; IDA:BHF-UCL.
GO; GO:0034370; P:triglyceride-rich lipoprotein particle remodeling; IEA:Ensembl.
InterPro; IPR000074; ApoA_E.
Pfam; PF01442; Apolipoprotein; 2.
1: Evidence at protein level;
Chylomicron; Coiled coil; Complete proteome; Disease mutation; HDL;
Lipid transport; Phosphoprotein; Polymorphism; Reference proteome;
Secreted; Signal; Transport; VLDL.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 366 Apolipoprotein A-V.
/FTId=PRO_0000001981.
COILED 54 157 {ECO:0000255}.
COILED 236 262 {ECO:0000255}.
MOD_RES 55 55 Phosphothreonine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 59 59 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VARIANT 19 19 S -> W (in allele APOA5*3; associated
with high plasma triglyceride levels;
dbSNP:rs3135506).
{ECO:0000269|PubMed:12417524,
ECO:0000269|PubMed:12920097,
ECO:0000269|PubMed:15108119}.
/FTId=VAR_021165.
VARIANT 37 37 D -> E (in dbSNP:rs34282181).
/FTId=VAR_035124.
VARIANT 153 153 V -> M (in dbSNP:rs3135507).
{ECO:0000269|PubMed:15108119}.
/FTId=VAR_021166.
VARIANT 185 185 G -> C (associated with high plasma
triglyceride levels; dbSNP:rs2075291).
{ECO:0000269|PubMed:12915450}.
/FTId=VAR_021167.
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


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