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Apolipoprotein A-IV (Apo-AIV) (ApoA-IV) (Apolipoprotein A4)

 APOA4_HUMAN             Reviewed;         396 AA.
P06727; A8MSL6; Q14CW8; Q6Q787;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 3.
18-JUL-2018, entry version 200.
RecName: Full=Apolipoprotein A-IV;
Short=Apo-AIV;
Short=ApoA-IV;
AltName: Full=Apolipoprotein A4;
Flags: Precursor;
Name=APOA4;
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 VARIANT LYS-279.
PubMed=3755616; DOI=10.1021/bi00361a034;
Karathanasis S.K., Yunis I.;
"Structure, evolution, and tissue-specific synthesis of human
apolipoprotein AIV.";
Biochemistry 25:3962-3970(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-279.
PubMed=3095836; DOI=10.1073/pnas.83.22.8457;
Karathanasis S.K., Oettgen P., Haddad I.A., Antonarakis S.E.;
"Structure, evolution, and polymorphisms of the human apolipoprotein
A4 gene (APOA4).";
Proc. Natl. Acad. Sci. U.S.A. 83:8457-8461(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, AND VARIANT APOA-IV*2
HIS-380.
PubMed=3036793;
Elshourbagy N.A., Walker D.W., Paik Y.K., Boguski M.S., Freeman M.,
Gordon J.I., Taylor J.M.;
"Structure and expression of the human apolipoprotein A-IV gene.";
J. Biol. Chem. 262:7973-7981(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Intestine;
PubMed=2930771; DOI=10.1016/0005-2760(89)90292-0;
Yang C., Gu Z.W., Xiong W., Rosseneu M., Yang H.X., Lee B.M.,
Gotto A.M. Jr., Chan L.;
"The primary structure of human apolipoprotein A-IV.";
Biochim. Biophys. Acta 1002:231-237(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-13; HIS-77;
SER-147; SER-161; SER-367 AND HIS-380.
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-147.
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Colon;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-396, AND VARIANT APOA-IV*2 HIS-380.
PubMed=3080432;
Elshourbagy N.A., Walker D.W., Boguski M.S., Gordon J.I., Taylor J.M.;
"The nucleotide and derived amino acid sequence of human
apolipoprotein A-IV mRNA and the close linkage of its gene to the
genes of apolipoproteins A-I and C-III.";
J. Biol. Chem. 261:1998-2002(1986).
[9]
SIGNAL SEQUENCE CLEAVAGE SITE.
PubMed=6706947;
Gordon J.I., Bisgaier C.L., Sims H.F., Sachdev O.P., Glickman R.M.,
Strauss A.W.;
"Biosynthesis of human preapolipoprotein A-IV.";
J. Biol. Chem. 259:468-474(1984).
[10]
REVIEW ON POLYMORPHISM.
Lohse P., Brewer H.B. Jr.;
"Genetic polymorphism of apolipoprotein A-IV.";
Curr. Opin. Lipidol. 2:90-95(1991).
[11]
POLYMORPHISM, ALLELES APOA-IV*1 AND APOA-IV*2, AND VARIANT HIS-380.
PubMed=2351649;
Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.;
"Genetic polymorphism of human plasma apolipoprotein A-IV is due to
nucleotide substitutions in the apolipoprotein A-IV gene.";
J. Biol. Chem. 265:10061-10064(1990).
[12]
POLYMORPHISM, ALLELES A-IV*0 AND A-IV*3, AND VARIANTS LYS-250 AND
GLU-GLN-GLN-GLN-381 INS.
PubMed=1973689;
Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.;
"Human plasma apolipoproteins A-IV-0 and A-IV-3. Molecular basis for
two rare variants of apolipoprotein A-IV-1.";
J. Biol. Chem. 265:12734-12739(1990).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 84-355, AND SUBUNIT.
PubMed=22579246; DOI=10.1016/j.str.2012.02.020;
Deng X., Morris J., Dressmen J., Tubb M.R., Tso P., Jerome W.G.,
Davidson W.S., Thompson T.B.;
"The structure of dimeric apolipoprotein A-IV and its mechanism of
self-association.";
Structure 20:767-779(2012).
[15]
VARIANT HIS-380.
PubMed=2065039;
Tenkanen H., Lukka M., Jauhiainen M., Metso J., Baumann M.,
Peltonen L., Ehnholm C.;
"The mutation causing the common apolipoprotein A-IV polymorphism is a
glutamine to histidine substitution of amino acid 360.";
Arterioscler. Thromb. 11:851-856(1991).
[16]
POLYMORPHISM, ALLELES A-IV*0; A-IV*1; A-IV*2 AND A-IV*3, AND VARIANTS
LYS-185; GLU-187; SER-367 AND HIS-380.
PubMed=1677358;
Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.;
"Three genetic variants of human plasma apolipoprotein A-IV: apoA-IV-
1(Thr-347-->Ser), apoA-IV-0(Lys-167-->Glu,Gln-360-->His), and apoA-IV-
3(Glu-165-->Lys).";
J. Biol. Chem. 266:13513-13518(1991).
[17]
ERRATUM.
Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.;
J. Biol. Chem. 266:19866-19866(1991).
[18]
VARIANT MET-13.
PubMed=1349197;
von Eckardstein A., Funke H., Schulte M., Erren M., Schulte H.,
Assmann G.;
"Nonsynonymous polymorphic sites in the apolipoprotein (apo) A-IV gene
are associated with changes in the concentration of apo B- and apo A-
I-containing lipoproteins in a normal population.";
Am. J. Hum. Genet. 50:1115-1128(1992).
[19]
VARIANT SER-147.
PubMed=1737067; DOI=10.1016/0925-4439(92)90147-F;
Tenkanen H., Koskinen P., Metso J., Baumann M., Lukka M.,
Kauppinen-Makelin R., Kontula K., Taskinen M.R., Manttari M.,
Manninen V., Ehnholm C.;
"A novel polymorphism of apolipoprotein A-IV is the result of an
asparagine to serine substitution at residue 127.";
Biochim. Biophys. Acta 1138:27-33(1992).
[20]
POLYMORPHISM, ALLELE A-IV*5, AND VARIANT GLU-GLN-GLN-GLN-381 INS.
PubMed=1487136; DOI=10.1002/gepi.1370090602;
Kamboh M.I., Williams E.R., Law J.C., Aston C.E., Bunker C.H.,
Ferrell R.E., Pollitzer W.S.;
"Molecular basis of a unique African variant (A-IV 5) of human
apolipoprotein A-IV and its significance in lipid metabolism.";
Genet. Epidemiol. 9:379-388(1992).
[21]
VARIANTS BUDAPEST-2 LYS-44; BUDAPEST-1 CYS-305 AND SER-367.
PubMed=7728150; DOI=10.1002/humu.1380050108;
Menzel H.J., Dieplinger H., Sandholzer C., Karadi I., Utermann G.,
Csaszar A.;
"Apolipoprotein A-IV polymorphism in the Hungarian population: gene
frequencies, effect on lipid levels, and sequence of two new
variants.";
Hum. Mutat. 5:58-65(1995).
[22]
VARIANTS SEATTLE-3 SER-161; SEATTLE-1 LEU-178 AND SEATTLE-2 GLN-264.
PubMed=8956036;
DOI=10.1002/(SICI)1098-1004(1996)8:4<319::AID-HUMU4>3.3.CO;2-T;
Deeb S.S., Nevin D.N., Iwasaki L., Brunzell J.D.;
"Two novel apolipoprotein A-IV variants in individuals with familial
combined hyperlipidemia and diminished levels of lipoprotein lipase
activity.";
Hum. Mutat. 8:319-325(1996).
[23]
VARIANT HIS-380.
PubMed=10391210; DOI=10.1038/10297;
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
Cooper R., Lipshutz R., Chakravarti A.;
"Patterns of single-nucleotide polymorphisms in candidate genes for
blood-pressure homeostasis.";
Nat. Genet. 22:239-247(1999).
[24]
VARIANT [LARGE SCALE ANALYSIS] SER-147, 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).
-!- FUNCTION: May have a role in chylomicrons and VLDL secretion and
catabolism. Required for efficient activation of lipoprotein
lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major
component of HDL and chylomicrons.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22579246}.
-!- INTERACTION:
Self; NbExp=10; IntAct=EBI-1222447, EBI-1222447;
P20393:NR1D1; NbExp=3; IntAct=EBI-1222447, EBI-2811738;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Synthesized primarily in the intestine and
secreted in plasma.
-!- DOMAIN: Nine of the thirteen 22-amino acid tandem repeats (each
22-mer is actually a tandem array of two, A and B, related 11-
mers) occurring in this sequence are predicted to be highly alpha-
helical, and many of these helices are amphipathic. They may
therefore serve as lipid-binding domains with lecithin:cholesterol
acyltransferase (LCAT) activating abilities.
-!- PTM: Phosphorylation sites are present in the extracellular
medium.
-!- POLYMORPHISM: Eight alleles have been characterized (APOA-IV*0 to
APOA-IV*7). APOA-IV*1 is the major allele (90%), APOA-IV*2 is also
common (8%), the others are rare alleles. The sequence shown
represents allele APOA-IV*1. {ECO:0000269|PubMed:1487136,
ECO:0000269|PubMed:1677358, ECO:0000269|PubMed:1973689,
ECO:0000269|PubMed:2351649, ECO:0000269|PubMed:3036793,
ECO:0000269|Ref.10}.
-!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=APOA4";
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EMBL; M13654; AAA51744.1; -; mRNA.
EMBL; M14642; AAA51745.1; -; Genomic_DNA.
EMBL; J02758; AAA96731.1; -; Genomic_DNA.
EMBL; X13629; CAA31955.1; -; mRNA.
EMBL; AY422950; AAQ91809.1; -; Genomic_DNA.
EMBL; AY555191; AAS68228.1; -; Genomic_DNA.
EMBL; AP006216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC074764; AAH74764.1; -; mRNA.
EMBL; BC113594; AAI13595.1; -; mRNA.
EMBL; BC113596; AAI13597.1; -; mRNA.
EMBL; M14566; AAA51748.1; -; mRNA.
CCDS; CCDS31681.1; -.
PIR; A94137; LPHUA4.
UniGene; Hs.1247; -.
PDB; 3S84; X-ray; 2.40 A; A/B=84-355.
PDBsum; 3S84; -.
ProteinModelPortal; P06727; -.
SMR; P06727; -.
DIP; DIP-38333N; -.
IntAct; P06727; 6.
STRING; 9606.ENSP00000350425; -.
CarbonylDB; P06727; -.
iPTMnet; P06727; -.
PhosphoSitePlus; P06727; -.
DMDM; 93163358; -.
DOSAC-COBS-2DPAGE; P06727; -.
REPRODUCTION-2DPAGE; IPI00304273; -.
SWISS-2DPAGE; P06727; -.
EPD; P06727; -.
MaxQB; P06727; -.
PaxDb; P06727; -.
PeptideAtlas; P06727; -.
PRIDE; P06727; -.
ProteomicsDB; 51912; -.
Ensembl; ENST00000357780; ENSP00000350425; ENSG00000110244.
UCSC; uc001pps.2; human.
DisGeNET; 337; -.
EuPathDB; HostDB:ENSG00000110244.6; -.
GeneCards; APOA4; -.
HGNC; HGNC:602; APOA4.
HPA; CAB068250; -.
HPA; CAB068251; -.
HPA; CAB068252; -.
HPA; HPA001352; -.
HPA; HPA002549; -.
MIM; 107690; gene.
neXtProt; NX_P06727; -.
eggNOG; ENOG410IKU1; Eukaryota.
eggNOG; ENOG41119VI; LUCA.
HOGENOM; HOG000037942; -.
HOVERGEN; HBG105707; -.
InParanoid; P06727; -.
OrthoDB; EOG091G0IA5; -.
PhylomeDB; P06727; -.
TreeFam; TF334458; -.
Reactome; R-HSA-8963888; Chylomicron assembly.
Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
Reactome; R-HSA-8963901; Chylomicron remodeling.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
Reactome; R-HSA-977225; Amyloid fiber formation.
PMAP-CutDB; A8MSL6; -.
PRO; PR:P06727; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110244; -.
CleanEx; HS_APOA4; -.
Genevisible; P06727; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0042627; C:chylomicron; IDA:BHF-UCL.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005769; C:early endosome; TAS:Reactome.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
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:0016209; F:antioxidant activity; IDA:HGNC.
GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
GO; GO:0017127; F:cholesterol transporter activity; IDA:BHF-UCL.
GO; GO:0005507; F:copper ion binding; IDA:HGNC.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008289; F:lipid binding; IMP:BHF-UCL.
GO; GO:0005319; F:lipid transporter activity; TAS:ProtInc.
GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; 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; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
GO; GO:0034378; P:chylomicron assembly; TAS:BHF-UCL.
GO; GO:0034371; P:chylomicron remodeling; TAS:Reactome.
GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; IC:BHF-UCL.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:HGNC.
GO; GO:0002227; P:innate immune response in mucosa; IDA:BHF-UCL.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0016042; P:lipid catabolic process; IDA:BHF-UCL.
GO; GO:0055088; P:lipid homeostasis; IDA:BHF-UCL.
GO; GO:0006869; P:lipid transport; IDA:BHF-UCL.
GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
GO; GO:0034445; P:negative regulation of plasma lipoprotein oxidation; IDA:BHF-UCL.
GO; GO:0031102; P:neuron projection regeneration; IBA:GO_Central.
GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:BHF-UCL.
GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL.
GO; GO:0010873; P:positive regulation of cholesterol esterification; IDA:BHF-UCL.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IDA:BHF-UCL.
GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:BHF-UCL.
GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:BHF-UCL.
GO; GO:0065005; P:protein-lipid complex assembly; IMP:BHF-UCL.
GO; GO:0032374; P:regulation of cholesterol transport; IDA:BHF-UCL.
GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IBA:GO_Central.
GO; GO:0019430; P:removal of superoxide radicals; IDA:HGNC.
GO; GO:0006982; P:response to lipid hydroperoxide; IDA:HGNC.
GO; GO:0035634; P:response to stilbenoid; IEA:Ensembl.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0043691; P:reverse cholesterol transport; IDA:BHF-UCL.
GO; GO:0070328; P:triglyceride homeostasis; IBA:GO_Central.
GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
InterPro; IPR000074; ApoA_E.
Pfam; PF01442; Apolipoprotein; 3.
1: Evidence at protein level;
3D-structure; Chylomicron; Complete proteome; HDL; Lipid transport;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted;
Signal; Transport.
SIGNAL 1 20 {ECO:0000269|PubMed:6706947}.
CHAIN 21 396 Apolipoprotein A-IV.
/FTId=PRO_0000001975.
REPEAT 33 54 1.
REPEAT 60 81 2.
REPEAT 82 103 3.
REPEAT 115 136 4.
REPEAT 137 158 5.
REPEAT 159 180 6.
REPEAT 181 202 7.
REPEAT 203 224 8.
REPEAT 225 246 9.
REPEAT 247 268 10.
REPEAT 269 286 11.
REPEAT 287 308 12.
REPEAT 309 330 13.
REGION 33 330 13 X 22 AA approximate tandem repeats.
COMPBIAS 372 389 Gln/Glu-rich.
VARIANT 13 13 V -> M (in allele APOA-IV*1D).
{ECO:0000269|PubMed:1349197,
ECO:0000269|PubMed:15108119}.
/FTId=VAR_000626.
VARIANT 44 44 E -> K (in Budapest-2).
{ECO:0000269|PubMed:7728150}.
/FTId=VAR_000627.
VARIANT 74 74 G -> S (in dbSNP:rs5102).
/FTId=VAR_014610.
VARIANT 77 77 Q -> H. {ECO:0000269|PubMed:15108119}.
/FTId=VAR_025444.
VARIANT 147 147 N -> S (in allele APOA-IV*1B;
dbSNP:rs5104).
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:15108119,
ECO:0000269|PubMed:16554811,
ECO:0000269|PubMed:1737067}.
/FTId=VAR_000628.
VARIANT 161 161 A -> S (in Seattle-3).
{ECO:0000269|PubMed:15108119,
ECO:0000269|PubMed:8956036}.
/FTId=VAR_000629.
VARIANT 178 178 S -> L (in Seattle-1; may contribute to
the development of familial combined
hyperlipidemia).
{ECO:0000269|PubMed:8956036}.
/FTId=VAR_000630.
VARIANT 185 185 E -> K (in allele APOA-IV*3).
{ECO:0000269|PubMed:1677358}.
/FTId=VAR_000631.
VARIANT 187 187 K -> E (in allele APOA-IV*0A; associated
with H-380).
{ECO:0000269|PubMed:1677358}.
/FTId=VAR_000632.
VARIANT 250 250 E -> K (in allele APOA-IV*3A).
{ECO:0000269|PubMed:1973689}.
/FTId=VAR_000633.
VARIANT 264 264 R -> Q (in Seattle-2; may contribute to
the development of familial combined
hyperlipidemia; dbSNP:rs2238008).
{ECO:0000269|PubMed:8956036}.
/FTId=VAR_000634.
VARIANT 279 279 R -> K (in dbSNP:rs1042372).
{ECO:0000269|PubMed:3095836,
ECO:0000269|PubMed:3755616}.
/FTId=VAR_025443.
VARIANT 305 305 R -> C (in Budapest-1).
{ECO:0000269|PubMed:7728150}.
/FTId=VAR_000635.
VARIANT 307 307 V -> L (in dbSNP:rs5108).
/FTId=VAR_014611.
VARIANT 367 367 T -> S (in allele APOA-IV*1A and allele
Budapest-1; dbSNP:rs675).
{ECO:0000269|PubMed:15108119,
ECO:0000269|PubMed:1677358,
ECO:0000269|PubMed:7728150}.
/FTId=VAR_000636.
VARIANT 380 380 Q -> H (in allele APOA-IV*2 and allele
APOA-IV*0A; associated with E-187 in
allele APOA-IV*0A; dbSNP:rs5110).
{ECO:0000269|PubMed:10391210,
ECO:0000269|PubMed:15108119,
ECO:0000269|PubMed:1677358,
ECO:0000269|PubMed:2065039,
ECO:0000269|PubMed:2351649,
ECO:0000269|PubMed:3036793,
ECO:0000269|PubMed:3080432}.
/FTId=VAR_000637.
VARIANT 381 381 Q -> QEQQQ (in allele APOA-IV*0 and
allele APOA-IV*5; allele APOA-IV*5 is
further defined by a silent nucleotide
substitution).
{ECO:0000269|PubMed:1487136}.
/FTId=VAR_000638.
CONFLICT 158 160 TPY -> DPL (in Ref. 1; AAA51744 and 2;
AAA51745). {ECO:0000305}.
CONFLICT 327 327 Q -> T (in Ref. 3; AAA96731 and 8;
AAA51748). {ECO:0000305}.
HELIX 97 113 {ECO:0000244|PDB:3S84}.
HELIX 114 116 {ECO:0000244|PDB:3S84}.
HELIX 117 223 {ECO:0000244|PDB:3S84}.
HELIX 224 226 {ECO:0000244|PDB:3S84}.
HELIX 231 276 {ECO:0000244|PDB:3S84}.
STRAND 278 280 {ECO:0000244|PDB:3S84}.
HELIX 282 307 {ECO:0000244|PDB:3S84}.
HELIX 310 329 {ECO:0000244|PDB:3S84}.
SEQUENCE 396 AA; 45399 MW; 193753196CA2FA4A CRC64;
MFLKAVVLTL ALVAVAGARA EVSADQVATV MWDYFSQLSN NAKEAVEHLQ KSELTQQLNA
LFQDKLGEVN TYAGDLQKKL VPFATELHER LAKDSEKLKE EIGKELEELR ARLLPHANEV
SQKIGDNLRE LQQRLEPYAD QLRTQVNTQA EQLRRQLTPY AQRMERVLRE NADSLQASLR
PHADELKAKI DQNVEELKGR LTPYADEFKV KIDQTVEELR RSLAPYAQDT QEKLNHQLEG
LTFQMKKNAE ELKARISASA EELRQRLAPL AEDVRGNLRG NTEGLQKSLA ELGGHLDQQV
EEFRRRVEPY GENFNKALVQ QMEQLRQKLG PHAGDVEGHL SFLEKDLRDK VNSFFSTFKE
KESQDKTLSL PELEQQQEQQ QEQQQEQVQM LAPLES


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