ID APOA4_HUMAN Reviewed; 396 AA. AC P06727; A8MSL6; Q14CW8; Q6Q787; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 17-JUN-2020, sequence version 4. DT 02-OCT-2024, entry version 237. DE RecName: Full=Apolipoprotein A-IV; DE Short=Apo-AIV; DE Short=ApoA-IV; DE AltName: Full=Apolipoprotein A4; DE Flags: Precursor; GN Name=APOA4; 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 VARIANTS ASN-147 AND LYS-279. RX PubMed=3755616; DOI=10.1021/bi00361a034; RA Karathanasis S.K., Yunis I.; RT "Structure, evolution, and tissue-specific synthesis of human RT apolipoprotein AIV."; RL Biochemistry 25:3962-3970(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-147 AND LYS-279. RX PubMed=3095836; DOI=10.1073/pnas.83.22.8457; RA Karathanasis S.K., Oettgen P., Haddad I.A., Antonarakis S.E.; RT "Structure, evolution, and polymorphisms of the human apolipoprotein A4 RT gene (APOA4)."; RL Proc. Natl. Acad. Sci. U.S.A. 83:8457-8461(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, AND VARIANTS ASN-147 AND RP HIS-380. RX PubMed=3036793; DOI=10.1016/s0021-9258(18)47513-8; RA Elshourbagy N.A., Walker D.W., Paik Y.K., Boguski M.S., Freeman M., RA Gordon J.I., Taylor J.M.; RT "Structure and expression of the human apolipoprotein A-IV gene."; RL J. Biol. Chem. 262:7973-7981(1987). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-147. RC TISSUE=Intestine; RX PubMed=2930771; DOI=10.1016/0005-2760(89)90292-0; RA Yang C., Gu Z.W., Xiong W., Rosseneu M., Yang H.X., Lee B.M., RA Gotto A.M. Jr., Chan L.; RT "The primary structure of human apolipoprotein A-IV."; RL Biochim. Biophys. Acta 1002:231-237(1989). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-13; HIS-77; ASN-147; RP SER-161; SER-367 AND HIS-380. 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-147. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-147. RC TISSUE=Brain, and Colon; 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-396, AND VARIANTS ASN-147 AND HIS-380. RX PubMed=3080432; DOI=10.1016/s0021-9258(17)35888-x; RA Elshourbagy N.A., Walker D.W., Boguski M.S., Gordon J.I., Taylor J.M.; RT "The nucleotide and derived amino acid sequence of human apolipoprotein A- RT IV mRNA and the close linkage of its gene to the genes of apolipoproteins RT A-I and C-III."; RL J. Biol. Chem. 261:1998-2002(1986). RN [9] RP SIGNAL SEQUENCE CLEAVAGE SITE. RX PubMed=6706947; DOI=10.1016/s0021-9258(17)43684-2; RA Gordon J.I., Bisgaier C.L., Sims H.F., Sachdev O.P., Glickman R.M., RA Strauss A.W.; RT "Biosynthesis of human preapolipoprotein A-IV."; RL J. Biol. Chem. 259:468-474(1984). RN [10] RP REVIEW ON POLYMORPHISM. RA Lohse P., Brewer H.B. Jr.; RT "Genetic polymorphism of apolipoprotein A-IV."; RL Curr. Opin. Lipidol. 2:90-95(1991). RN [11] RP POLYMORPHISM, ALLELES APOA-IV*1 AND APOA-IV*2, AND VARIANT HIS-380. RX PubMed=2351649; DOI=10.1016/s0021-9258(19)38779-4; RA Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.; RT "Genetic polymorphism of human plasma apolipoprotein A-IV is due to RT nucleotide substitutions in the apolipoprotein A-IV gene."; RL J. Biol. Chem. 265:10061-10064(1990). RN [12] RP POLYMORPHISM, ALLELES A-IV*0 AND A-IV*3, AND VARIANTS LYS-250 AND RP GLU-GLN-GLN-GLN-381 INS. RX PubMed=1973689; DOI=10.1016/s0021-9258(19)38406-6; RA Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.; RT "Human plasma apolipoproteins A-IV-0 and A-IV-3. Molecular basis for two RT rare variants of apolipoprotein A-IV-1."; RL J. Biol. Chem. 265:12734-12739(1990). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 84-355, AND SUBUNIT. RX PubMed=22579246; DOI=10.1016/j.str.2012.02.020; RA Deng X., Morris J., Dressmen J., Tubb M.R., Tso P., Jerome W.G., RA Davidson W.S., Thompson T.B.; RT "The structure of dimeric apolipoprotein A-IV and its mechanism of self- RT association."; RL Structure 20:767-779(2012). RN [15] RP VARIANT HIS-380. RX PubMed=2065039; DOI=10.1161/01.atv.11.4.851; RA Tenkanen H., Lukka M., Jauhiainen M., Metso J., Baumann M., Peltonen L., RA Ehnholm C.; RT "The mutation causing the common apolipoprotein A-IV polymorphism is a RT glutamine to histidine substitution of amino acid 360."; RL Arterioscler. Thromb. 11:851-856(1991). RN [16] RP POLYMORPHISM, ALLELES A-IV*0; A-IV*1; A-IV*2 AND A-IV*3, AND VARIANTS RP LYS-185; GLU-187; SER-367 AND HIS-380. RX PubMed=1677358; DOI=10.1016/s0021-9258(18)92728-6; RA Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.; RT "Three genetic variants of human plasma apolipoprotein A-IV: apoA-IV-1(Thr- RT 347-->Ser), apoA-IV-0(Lys-167-->Glu,Gln-360-->His), and apoA-IV-3(Glu- RT 165-->Lys)."; RL J. Biol. Chem. 266:13513-13518(1991). RN [17] RP ERRATUM OF PUBMED:1677358. RA Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.; RL J. Biol. Chem. 266:19866-19866(1991). RN [18] RP VARIANT MET-13. RX PubMed=1349197; RA von Eckardstein A., Funke H., Schulte M., Erren M., Schulte H., Assmann G.; RT "Nonsynonymous polymorphic sites in the apolipoprotein (apo) A-IV gene are RT associated with changes in the concentration of apo B- and apo A-I- RT containing lipoproteins in a normal population."; RL Am. J. Hum. Genet. 50:1115-1128(1992). RN [19] RP VARIANT ASN-147. RX PubMed=1737067; DOI=10.1016/0925-4439(92)90147-f; RA Tenkanen H., Koskinen P., Metso J., Baumann M., Lukka M., RA Kauppinen-Makelin R., Kontula K., Taskinen M.R., Manttari M., Manninen V., RA Ehnholm C.; RT "A novel polymorphism of apolipoprotein A-IV is the result of an asparagine RT to serine substitution at residue 127."; RL Biochim. Biophys. Acta 1138:27-33(1992). RN [20] RP POLYMORPHISM, ALLELE A-IV*5, AND VARIANT GLU-GLN-GLN-GLN-381 INS. RX PubMed=1487136; DOI=10.1002/gepi.1370090602; RA Kamboh M.I., Williams E.R., Law J.C., Aston C.E., Bunker C.H., RA Ferrell R.E., Pollitzer W.S.; RT "Molecular basis of a unique African variant (A-IV 5) of human RT apolipoprotein A-IV and its significance in lipid metabolism."; RL Genet. Epidemiol. 9:379-388(1992). RN [21] RP VARIANT BUDAPEST-2 LYS-44, AND VARIANTS BUDAPEST-1 CYS-305 AND SER-367. RX PubMed=7728150; DOI=10.1002/humu.1380050108; RA Menzel H.J., Dieplinger H., Sandholzer C., Karadi I., Utermann G., RA Csaszar A.; RT "Apolipoprotein A-IV polymorphism in the Hungarian population: gene RT frequencies, effect on lipid levels, and sequence of two new variants."; RL Hum. Mutat. 5:58-65(1995). RN [22] RP VARIANT SEATTLE-3 SER-161, VARIANT SEATTLE-1 LEU-178, AND VARIANT SEATTLE-2 RP GLN-264. RX PubMed=8956036; RX DOI=10.1002/(sici)1098-1004(1996)8:4<319::aid-humu4>3.0.co;2-2; RA Deeb S.S., Nevin D.N., Iwasaki L., Brunzell J.D.; RT "Two novel apolipoprotein A-IV variants in individuals with familial RT combined hyperlipidemia and diminished levels of lipoprotein lipase RT activity."; RL Hum. Mutat. 8:319-325(1996). RN [23] RP VARIANT HIS-380. RX PubMed=10391210; DOI=10.1038/10297; RA Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., RA Cooper R., Lipshutz R., Chakravarti A.; RT "Patterns of single-nucleotide polymorphisms in candidate genes for blood- RT pressure homeostasis."; RL Nat. Genet. 22:239-247(1999). CC -!- FUNCTION: May have a role in chylomicrons and VLDL secretion and CC catabolism. Required for efficient activation of lipoprotein lipase by CC ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL CC and chylomicrons. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22579246}. CC -!- INTERACTION: CC P06727; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-1222447, EBI-11522760; CC P06727; P06727: APOA4; NbExp=10; IntAct=EBI-1222447, EBI-1222447; CC P06727; P55212: CASP6; NbExp=3; IntAct=EBI-1222447, EBI-718729; CC P06727; Q8IZR5-2: CMTM4; NbExp=3; IntAct=EBI-1222447, EBI-17278014; CC P06727; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-1222447, EBI-11522780; CC P06727; P43360: MAGEA6; NbExp=3; IntAct=EBI-1222447, EBI-1045155; CC P06727; P20393: NR1D1; NbExp=3; IntAct=EBI-1222447, EBI-2811738; CC P06727; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-1222447, EBI-2623095; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Synthesized primarily in the intestine and secreted CC in plasma. CC -!- DOMAIN: Nine of the thirteen 22-amino acid tandem repeats (each 22-mer CC is actually a tandem array of two, A and B, related 11-mers) occurring CC in this sequence are predicted to be highly alpha-helical, and many of CC these helices are amphipathic. They may therefore serve as lipid- CC binding domains with lecithin:cholesterol acyltransferase (LCAT) CC activating abilities. CC -!- PTM: Phosphorylation sites are present in the extracellular medium. CC -!- POLYMORPHISM: Eight alleles have been characterized (APOA-IV*0 to APOA- CC IV*7). APOA-IV*1 is the major allele (90%), APOA-IV*2 is also common CC (8%), the others are rare alleles. {ECO:0000269|PubMed:1487136, CC ECO:0000269|PubMed:1677358, ECO:0000269|PubMed:1973689, CC ECO:0000269|PubMed:2351649, ECO:0000269|PubMed:3036793, CC ECO:0000269|Ref.10}. CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family. CC {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; M13654; AAA51744.1; -; mRNA. DR EMBL; M14642; AAA51745.1; -; Genomic_DNA. DR EMBL; J02758; AAA96731.1; -; Genomic_DNA. DR EMBL; X13629; CAA31955.1; -; mRNA. DR EMBL; AY422950; AAQ91809.1; -; Genomic_DNA. DR EMBL; AY555191; AAS68228.1; -; Genomic_DNA. DR EMBL; AP006216; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC074764; AAH74764.1; -; mRNA. DR EMBL; BC113594; AAI13595.1; -; mRNA. DR EMBL; BC113596; AAI13597.1; -; mRNA. DR EMBL; M14566; AAA51748.1; -; mRNA. DR CCDS; CCDS31681.1; -. DR PIR; A94137; LPHUA4. DR RefSeq; NP_000473.2; NM_000482.3. DR PDB; 3S84; X-ray; 2.40 A; A/B=84-355. DR PDBsum; 3S84; -. DR AlphaFoldDB; P06727; -. DR SMR; P06727; -. DR DIP; DIP-38333N; -. DR IntAct; P06727; 20. DR STRING; 9606.ENSP00000350425; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB11886; Infigratinib. DR DrugBank; DB00877; Sirolimus. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR CarbonylDB; P06727; -. DR GlyGen; P06727; 1 site, 2 O-linked glycans (1 site). DR iPTMnet; P06727; -. DR PhosphoSitePlus; P06727; -. DR BioMuta; APOA4; -. DR DMDM; 93163358; -. DR REPRODUCTION-2DPAGE; IPI00304273; -. DR CPTAC; non-CPTAC-1077; -. DR CPTAC; non-CPTAC-1078; -. DR CPTAC; non-CPTAC-1079; -. DR jPOST; P06727; -. DR MassIVE; P06727; -. DR PaxDb; 9606-ENSP00000350425; -. DR PeptideAtlas; P06727; -. DR ProteomicsDB; 51912; -. DR Antibodypedia; 18421; 537 antibodies from 37 providers. DR DNASU; 337; -. DR Ensembl; ENST00000357780.5; ENSP00000350425.3; ENSG00000110244.7. DR GeneID; 337; -. DR KEGG; hsa:337; -. DR MANE-Select; ENST00000357780.5; ENSP00000350425.3; NM_000482.4; NP_000473.2. DR UCSC; uc001pps.2; human. DR AGR; HGNC:602; -. DR CTD; 337; -. DR DisGeNET; 337; -. DR GeneCards; APOA4; -. DR HGNC; HGNC:602; APOA4. DR HPA; ENSG00000110244; Tissue enriched (intestine). DR MIM; 107690; gene. DR neXtProt; NX_P06727; -. DR OpenTargets; ENSG00000110244; -. DR VEuPathDB; HostDB:ENSG00000110244; -. DR eggNOG; ENOG502QSC5; Eukaryota. DR GeneTree; ENSGT00950000182929; -. DR HOGENOM; CLU_058447_0_0_1; -. DR InParanoid; P06727; -. DR OMA; VIWKYFT; -. DR OrthoDB; 4637112at2759; -. DR PhylomeDB; P06727; -. DR TreeFam; TF334458; -. DR PathwayCommons; P06727; -. DR Reactome; R-HSA-8963888; Chylomicron assembly. DR Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes. DR Reactome; R-HSA-8963901; Chylomicron remodeling. DR Reactome; R-HSA-975634; Retinoid metabolism and transport. DR Reactome; R-HSA-977225; Amyloid fiber formation. DR SignaLink; P06727; -. DR SIGNOR; P06727; -. DR EvolutionaryTrace; P06727; -. DR Pharos; P06727; Tbio. DR PRO; PR:P06727; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P06727; protein. DR Bgee; ENSG00000110244; Expressed in jejunal mucosa and 106 other cell types or tissues. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0042627; C:chylomicron; IDA:BHF-UCL. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005769; C:early endosome; TAS:Reactome. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:1903561; C:extracellular vesicle; IBA:GO_Central. DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL. DR GO; GO:0034362; C:low-density lipoprotein particle; IBA:GO_Central. DR GO; GO:0045202; C:synapse; IEA:Ensembl. DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL. DR GO; GO:0016209; F:antioxidant activity; IDA:HGNC-UCL. DR GO; GO:0120020; F:cholesterol transfer activity; IDA:BHF-UCL. DR GO; GO:0005507; F:copper ion binding; IDA:HGNC-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008289; F:lipid binding; IMP:BHF-UCL. DR GO; GO:0005319; F:lipid transporter activity; TAS:ProtInc. DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL. DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IDA:BHF-UCL. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL. DR GO; GO:0055090; P:acylglycerol homeostasis; IBA:GO_Central. DR GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL. DR GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL. DR GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL. DR GO; GO:0034378; P:chylomicron assembly; TAS:BHF-UCL. DR GO; GO:0034371; P:chylomicron remodeling; IC:BHF-UCL. DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:BHF-UCL. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:HGNC-UCL. DR GO; GO:0002227; P:innate immune response in mucosa; IDA:BHF-UCL. DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL. DR GO; GO:0016042; P:lipid catabolic process; IDA:BHF-UCL. DR GO; GO:0055088; P:lipid homeostasis; IDA:BHF-UCL. DR GO; GO:0006869; P:lipid transport; IDA:BHF-UCL. DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro. DR GO; GO:0034445; P:negative regulation of plasma lipoprotein oxidation; IDA:BHF-UCL. DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEA:Ensembl. DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:BHF-UCL. DR GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL. DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IDA:ARUK-UCL. DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IDA:BHF-UCL. DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:BHF-UCL. DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:BHF-UCL. DR GO; GO:0065005; P:protein-lipid complex assembly; IMP:BHF-UCL. DR GO; GO:0032374; P:regulation of cholesterol transport; IDA:BHF-UCL. DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IEA:Ensembl. DR GO; GO:0019430; P:removal of superoxide radicals; IDA:HGNC-UCL. DR GO; GO:0006982; P:response to lipid hydroperoxide; IDA:HGNC-UCL. DR GO; GO:0035634; P:response to stilbenoid; IEA:Ensembl. DR GO; GO:0034014; P:response to triglyceride; IEA:Ensembl. DR GO; GO:0043691; P:reverse cholesterol transport; IDA:BHF-UCL. DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:BHF-UCL. DR Gene3D; 1.20.120.20; Apolipoprotein; 2. DR InterPro; IPR000074; ApoA_E. DR InterPro; IPR050163; Apolipoprotein_A1/A4/E. DR PANTHER; PTHR18976; APOLIPOPROTEIN; 1. DR PANTHER; PTHR18976:SF1; APOLIPOPROTEIN A-IV; 1. DR Pfam; PF01442; Apolipoprotein; 1. DR SUPFAM; SSF58113; Apolipoprotein A-I; 2. PE 1: Evidence at protein level; KW 3D-structure; Chylomicron; HDL; Lipid transport; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; Secreted; Signal; KW Transport. FT SIGNAL 1..20 FT /evidence="ECO:0000269|PubMed:6706947" FT CHAIN 21..396 FT /note="Apolipoprotein A-IV" FT /id="PRO_0000001975" FT REPEAT 33..54 FT /note="1" FT REPEAT 60..81 FT /note="2" FT REPEAT 82..103 FT /note="3" FT REPEAT 115..136 FT /note="4" FT REPEAT 137..158 FT /note="5" FT REPEAT 159..180 FT /note="6" FT REPEAT 181..202 FT /note="7" FT REPEAT 203..224 FT /note="8" FT REPEAT 225..246 FT /note="9" FT REPEAT 247..268 FT /note="10" FT REPEAT 269..286 FT /note="11" FT REPEAT 287..308 FT /note="12" FT REPEAT 309..330 FT /note="13" FT REGION 33..330 FT /note="13 X 22 AA approximate tandem repeats" FT REGION 361..396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 369..396 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 13 FT /note="V -> M (in allele APOA-IV*1D; dbSNP:rs12721041)" FT /evidence="ECO:0000269|PubMed:1349197, FT ECO:0000269|PubMed:15108119" FT /id="VAR_000626" FT VARIANT 44 FT /note="E -> K (in Budapest-2)" FT /evidence="ECO:0000269|PubMed:7728150" FT /id="VAR_000627" FT VARIANT 74 FT /note="G -> S (in dbSNP:rs5102)" FT /id="VAR_014610" FT VARIANT 77 FT /note="Q -> H (in dbSNP:rs12721042)" FT /evidence="ECO:0000269|PubMed:15108119" FT /id="VAR_025444" FT VARIANT 147 FT /note="S -> N (in dbSNP:rs5104)" FT /evidence="ECO:0000269|PubMed:15108119, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16554811, FT ECO:0000269|PubMed:1737067, ECO:0000269|PubMed:2930771, FT ECO:0000269|PubMed:3036793, ECO:0000269|PubMed:3080432, FT ECO:0000269|PubMed:3095836, ECO:0000269|PubMed:3755616" FT /id="VAR_000628" FT VARIANT 161 FT /note="A -> S (in Seattle-3; dbSNP:rs12721043)" FT /evidence="ECO:0000269|PubMed:15108119, FT ECO:0000269|PubMed:8956036" FT /id="VAR_000629" FT VARIANT 178 FT /note="S -> L (in Seattle-1; may contribute to the FT development of familial combined hyperlipidemia; FT dbSNP:rs1181852696)" FT /evidence="ECO:0000269|PubMed:8956036" FT /id="VAR_000630" FT VARIANT 185 FT /note="E -> K (in allele APOA-IV*3; dbSNP:rs201861136)" FT /evidence="ECO:0000269|PubMed:1677358" FT /id="VAR_000631" FT VARIANT 187 FT /note="K -> E (in allele APOA-IV*0A; associated with H-380; FT dbSNP:rs773492545)" FT /evidence="ECO:0000269|PubMed:1677358" FT /id="VAR_000632" FT VARIANT 250 FT /note="E -> K (in allele APOA-IV*3A; dbSNP:rs121909576)" FT /evidence="ECO:0000269|PubMed:1973689" FT /id="VAR_000633" FT VARIANT 264 FT /note="R -> Q (in Seattle-2; may contribute to the FT development of familial combined hyperlipidemia; FT dbSNP:rs2238008)" FT /evidence="ECO:0000269|PubMed:8956036" FT /id="VAR_000634" FT VARIANT 279 FT /note="R -> K (in dbSNP:rs1042372)" FT /evidence="ECO:0000269|PubMed:3095836, FT ECO:0000269|PubMed:3755616" FT /id="VAR_025443" FT VARIANT 305 FT /note="R -> C (in allele Budapest-1; dbSNP:rs150264487)" FT /evidence="ECO:0000269|PubMed:7728150" FT /id="VAR_000635" FT VARIANT 307 FT /note="V -> L (in dbSNP:rs5108)" FT /id="VAR_014611" FT VARIANT 367 FT /note="T -> S (in allele APOA-IV*1A and allele Budapest-1; FT dbSNP:rs675)" FT /evidence="ECO:0000269|PubMed:15108119, FT ECO:0000269|PubMed:1677358, ECO:0000269|PubMed:7728150" FT /id="VAR_000636" FT VARIANT 380 FT /note="Q -> H (in allele APOA-IV*2 and allele APOA-IV*0A; FT associated with E-187 in allele APOA-IV*0A; dbSNP:rs5110)" FT /evidence="ECO:0000269|PubMed:10391210, FT ECO:0000269|PubMed:15108119, ECO:0000269|PubMed:1677358, FT ECO:0000269|PubMed:2065039, ECO:0000269|PubMed:2351649, FT ECO:0000269|PubMed:3036793, ECO:0000269|PubMed:3080432" FT /id="VAR_000637" FT VARIANT 381 FT /note="Q -> QEQQQ (in allele APOA-IV*0 and allele FT APOA-IV*5; allele APOA-IV*5 is further defined by a silent FT nucleotide substitution)" FT /evidence="ECO:0000269|PubMed:1487136" FT /id="VAR_000638" FT CONFLICT 158..160 FT /note="TPY -> DPL (in Ref. 1; AAA51744 and 2; AAA51745)" FT /evidence="ECO:0000305" FT CONFLICT 327 FT /note="Q -> T (in Ref. 3; AAA96731 and 8; AAA51748)" FT /evidence="ECO:0000305" FT HELIX 97..113 FT /evidence="ECO:0007829|PDB:3S84" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:3S84" FT HELIX 117..223 FT /evidence="ECO:0007829|PDB:3S84" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:3S84" FT HELIX 231..276 FT /evidence="ECO:0007829|PDB:3S84" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:3S84" FT HELIX 282..307 FT /evidence="ECO:0007829|PDB:3S84" FT HELIX 310..329 FT /evidence="ECO:0007829|PDB:3S84" SQ SEQUENCE 396 AA; 45372 MW; 19307A196CAE0A4A CRC64; MFLKAVVLTL ALVAVAGARA EVSADQVATV MWDYFSQLSN NAKEAVEHLQ KSELTQQLNA LFQDKLGEVN TYAGDLQKKL VPFATELHER LAKDSEKLKE EIGKELEELR ARLLPHANEV SQKIGDNLRE LQQRLEPYAD QLRTQVSTQA 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 //