ID APOB_HUMAN Reviewed; 4563 AA. AC P04114; O00502; P78479; P78480; P78481; Q13779; Q13785; Q13786; Q13787; AC Q13788; Q4ZG63; Q53QC8; Q7Z600; Q9UMN0; DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2024, sequence version 3. DT 27-MAR-2024, entry version 254. DE RecName: Full=Apolipoprotein B-100; DE Short=Apo B-100; DE Contains: DE RecName: Full=Apolipoprotein B-48; DE Short=Apo B-48; DE Flags: Precursor; GN Name=APOB; 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-273; GLU-1218; VAL-2092; RP VAL-2313; THR-2365; GLN-2680; HIS-3319; LYS-3427; GLU-3432; THR-3732; RP LEU-3949; PHE-3964; LYS-4181 AND ASN-4338. RX PubMed=3763409; DOI=10.1093/nar/14.18.7501; RA Knott T.C., Wallis S.C., Powell L.M., Pease R.J., Lusis A.J., Blackhart B., RA McCarthy B.J., Mahley R.W., Levy-Wilson B., Scott J.; RT "Complete cDNA and derived protein sequence of human apolipoprotein RT B-100."; RL Nucleic Acids Res. 14:7501-7503(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-2313; HIS-3319; RP LYS-3427; GLU-3432 AND ASN-4338. RX PubMed=3652907; DOI=10.1089/dna.1987.6.363; RA Ludwig E.H., Blackhart B.D., Pierotti V.R., Caiati L., Fortier C., RA Knott T., Scott J., Mahley R.W., Levy-Wilson B., McCarthy B.J.; RT "DNA sequence of the human apolipoprotein B gene."; RL DNA 6:363-372(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ILE-98; VAL-618; VAL-2313; RP HIS-3319; LYS-3427; GLU-3432 AND ASN-4338. RX PubMed=3759943; DOI=10.1016/s0021-9258(18)69248-8; RA Chen S.-H., Yang C.-Y., Chen P.-F., Setzer D., Tanimura M., Li W.-H., RA Gotto A.M. Jr., Chan L.; RT "The complete cDNA and amino acid sequence of human apolipoprotein B-100."; RL J. Biol. Chem. 261:12918-12921(1986). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-2037; VAL-2313; HIS-3319; RP LYS-3427; GLU-3432; LEU-3949; LYS-4181 AND ASN-4338. RX PubMed=3464946; DOI=10.1073/pnas.83.21.8142; RA Law S.W., Grant S.M., Higuchi K., Hospattankar A.V., Lackner K.J., Lee N., RA Brewer H.B. Jr.; RT "Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived RT amino acid sequence."; RL Proc. Natl. Acad. Sci. U.S.A. 83:8142-8146(1986). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40, AND RP VARIANTS VAL-618; VAL-2313; HIS-3319; LYS-3427; GLU-3432; THR-3732; RP LEU-3949; PHE-3964; LYS-4181 AND ASN-4338. RX PubMed=3030729; DOI=10.1002/j.1460-2075.1986.tb04675.x; RA Cladaras C., Hadzopoulou-Cladaras M., Nolte R.T., Atkinson D., Zannis V.I.; RT "The complete sequence and structural analysis of human apolipoprotein B- RT 100: relationship between apoB-100 and apoB-48 forms."; RL EMBO J. 5:3495-3507(1986). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-2313 AND ASN-4338. RG SeattleSNPs variation discovery resource; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TYR-1422. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1670, AND VARIANTS ILE-98 AND ASP-1670. RX PubMed=3461454; DOI=10.1073/pnas.83.15.5678; RA Protter A.A., Hardman D.A., Sato K.Y., Schilling J.W., Yamanaka M., RA Hort Y.J., Hjerrild K.A., Chen G.C., Kane J.P.; RT "Analysis of cDNA clones encoding the entire B-26 region of human RT apolipoprotein B."; RL Proc. Natl. Acad. Sci. U.S.A. 83:5678-5682(1986). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-291. RX PubMed=3513177; DOI=10.1073/pnas.83.5.1467; RA Protter A.A., Hardman D.A., Schilling J.W., Miller J., Appleby V., RA Chen G.C., Kirsher S.W., McEnroe G., Kane J.P.; RT "Isolation of a cDNA clone encoding the amino-terminal region of human RT apolipoprotein B."; RL Proc. Natl. Acad. Sci. U.S.A. 83:1467-1471(1986). RN [10] RP PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND VARIANT ILE-98. RX PubMed=2115173; DOI=10.1073/pnas.87.14.5523; RA Yang C.Y., Kim T.W., Weng S.A., Lee B.R., Yang M.L., Gotto A.M. Jr.; RT "Isolation and characterization of sulfhydryl and disulfide peptides of RT human apolipoprotein B-100."; RL Proc. Natl. Acad. Sci. U.S.A. 87:5523-5527(1990). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 485-1044. RC TISSUE=Liver; RX PubMed=3001697; DOI=10.1073/pnas.82.24.8340; RA Law S.W., Lackner K.J., Hospattankar A.V., Anchors J.M., Sakaguchi A.Y., RA Naylor S.L., Brewer H.B. Jr.; RT "Human apolipoprotein B-100: cloning, analysis of liver mRNA, and RT assignment of the gene to chromosome 2."; RL Proc. Natl. Acad. Sci. U.S.A. 82:8340-8344(1985). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 709-906. RX PubMed=3860836; DOI=10.1073/pnas.82.15.4983; RA Deeb S.S., Motulsky A.G., Albers J.J.; RT "A partial cDNA clone for human apolipoprotein B."; RL Proc. Natl. Acad. Sci. U.S.A. 82:4983-4986(1985). RN [13] RP PROTEIN SEQUENCE OF 873-896 AND 3113-3137. RX PubMed=6373369; DOI=10.1016/0014-5793(84)81378-2; RA LeBoeuf R.C., Miller C., Shively J.E., Schumaker V.N., Balla M.A., RA Lusis A.J.; RT "Human apolipoprotein B: partial amino acid sequence."; RL FEBS Lett. 170:105-108(1984). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1042-1232. RX PubMed=2567736; DOI=10.1016/s0021-9258(18)60477-6; RA Huang L.S., Ripps M.E., Korman S.H., Deckelbaum R.J., Breslow J.L.; RT "Hypobetalipoproteinemia due to an apolipoprotein B gene exon 21 deletion RT derived by Alu-Alu recombination."; RL J. Biol. Chem. 264:11394-11400(1989). RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1282-4503, AND VARIANTS VAL-2313; HIS-3319; RP LYS-3427; GLU-3432; THR-3732 AND ASN-4338. RX PubMed=2883086; DOI=10.1016/0378-1119(86)90383-5; RA Carlsson P., Darnfors C., Olofsson S.O., Bjursell G.; RT "Analysis of the human apolipoprotein B gene; complete structure of the B- RT 74 region."; RL Gene 49:29-51(1986). RN [16] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1671-2398, AND VARIANT VAL-2313. RX PubMed=3676265; DOI=10.1021/bi00391a040; RA Hardman D.A., Protter A.A., Chen G.C., Schilling J.W., Sato K.Y., Lau K., RA Yamanaka M., Mikita T., Miller J., Crisp T., McEnroe G., Scarborough R.M., RA Kane J.P.; RT "Structural comparison of human apolipoproteins B-48 and B-100."; RL Biochemistry 26:5478-5486(1987). RN [17] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1937-2018 AND 3811-4334. RX PubMed=3841204; DOI=10.1093/nar/13.24.8813; RA Carlsson P., Olofsson S.O., Bondjers G., Darnfors C., Wiklund O., RA Bjursell G.; RT "Molecular cloning of human apolipoprotein B cDNA."; RL Nucleic Acids Res. 13:8813-8826(1985). RN [18] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2115-2179, AND RNA EDITING. RC TISSUE=Small intestine; RX PubMed=3621347; DOI=10.1016/0092-8674(87)90510-1; RA Powell L.M., Wallis S.C., Pease R.J., Edwards Y.H., Knott T.J., Scott J.; RT "A novel form of tissue-specific RNA processing produces apolipoprotein-B48 RT in intestine."; RL Cell 50:831-840(1987). RN [19] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2127-2179, AND RNA EDITING. RX PubMed=2450346; DOI=10.1073/pnas.85.6.1772; RA Higuchi K., Hospattankar A.V., Law S.W., Meglin N., Cortright J., RA Brewer H.B. Jr.; RT "Human apolipoprotein B (apoB) mRNA: identification of two distinct apoB RT mRNAs, an mRNA with the apoB-100 sequence and an apoB mRNA containing a RT premature in-frame translational stop codon, in both liver and intestine."; RL Proc. Natl. Acad. Sci. U.S.A. 85:1772-1776(1988). RN [20] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2129-2235, AND RNA EDITING. RX PubMed=3426612; DOI=10.1016/0006-291x(87)90537-7; RA Hardman D.A., Protter A.A., Schilling J.W., Kane J.P.; RT "Carboxyl terminal analysis of human B-48 protein confirms the novel RT mechanism proposed for chain termination."; RL Biochem. Biophys. Res. Commun. 149:1214-1219(1987). RN [21] RP PROTEIN SEQUENCE OF 2169-2179. RX PubMed=2445342; DOI=10.1016/0006-291x(87)91107-7; RA Hospattankar A.V., Higuchi K., Law S.W., Meglin N., Brewer H.B. Jr.; RT "Identification of a novel in-frame translational stop codon in human RT intestine apoB mRNA."; RL Biochem. Biophys. Res. Commun. 148:279-285(1987). RN [22] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3056-3159. RX PubMed=3903660; DOI=10.1093/nar/13.19.6937; RA Mehrabian M., Schumaker V.N., Fareed G.C., West R., Johnson D.F., RA Kirchgessner T.G., Lin H.-C., Wang X., Ma Y., Mendiaz E., Lusis A.J.; RT "Human apolipoprotein B: identification of cDNA clones and characterization RT of mRNA."; RL Nucleic Acids Res. 13:6937-6953(1985). RN [23] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3109-4563, AND VARIANTS HIS-3319; LYS-3427; RP GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338. RX PubMed=2994225; DOI=10.1126/science.2994225; RA Knott T.J., Rall S.C. Jr., Innerarity T.L., Jacobson S.F., Urdea M.S., RA Levy-Wilson B., Powell L.M., Pease R.J., Eddy R., Nakai H., Byers M., RA Priestley L.M., Robertson E., Rall L.B., Betsholtz C., Shows T.B., RA Mahley R.W., Scott J.; RT "Human apolipoprotein B: structure of carboxyl-terminal domains, sites of RT gene expression, and chromosomal localization."; RL Science 230:37-43(1985). RN [24] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3728-4563, AND VARIANT ASN-4338. RX PubMed=2932736; DOI=10.1073/pnas.82.21.7265; RA Wei C.F., Chen S.H., Yang C.Y., Marcel Y.L., Milne R.W., Li W.H., RA Sparrow J.T., Gotto A.M. Jr., Chan L.; RT "Molecular cloning and expression of partial cDNAs and deduced amino acid RT sequence of a carboxyl-terminal fragment of human apolipoprotein B-100."; RL Proc. Natl. Acad. Sci. U.S.A. 82:7265-7269(1985). RN [25] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3846-4298, AND VARIANTS LEU-3949; PHE-3964 RP AND LYS-4181. RC TISSUE=Liver; RX PubMed=3841481; DOI=10.1016/0021-9150(85)90073-5; RA Shoulders C.C., Myant N.B., Sidoli A., Rodriguez J.C., Cortese C., RA Baralle F.E., Cortese R.; RT "Molecular cloning of human LDL apolipoprotein B cDNA. Evidence for more RT than one gene per haploid genome."; RL Atherosclerosis 58:277-289(1985). RN [26] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4217-4563. RX PubMed=3024665; DOI=10.1515/bchm3.1986.367.2.1077; RA Pfitzner R., Wagener R., Stoffel W.; RT "Isolation, expression and characterization of a human apolipoprotein B RT 100-specific cDNA clone."; RL Biol. Chem. Hoppe-Seyler 367:1077-1083(1986). RN [27] RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION OF APO-B48, AND RNA EDITING. RX PubMed=3659919; DOI=10.1126/science.3659919; RA Chen S.-H., Habib G., Yang C.-H., Gu Z.-W., Lee B.R., Weng S.-H., RA Silberman S.R., Cai S.-J., Deslypere J.P., Rosseneu M., Gotto A.M. Jr., RA Li W.-H., Chan L.; RT "Apolipoprotein B-48 is the product of a messenger RNA with an organ- RT specific in-frame stop codon."; RL Science 238:363-366(1987). RN [28] RP DOMAINS. RX PubMed=3773997; DOI=10.1038/323734a0; RA Knott T.C., Pease R.J., Powell L.M., Wallis S.C., Rall S.C. Jr., RA Innerarity T.L., Blackhart B., Taylor W.R., Marcel Y., Milne R., RA Johnson D., Fuller M., Lusis A.J., McCarthy B.J., Mahley R.W., RA Levy-Wilson B., Scott J.; RT "Complete protein sequence and identification of structural domains of RT human apolipoprotein B."; RL Nature 323:734-738(1986). RN [29] RP DOMAINS. RX PubMed=3095664; DOI=10.1038/323738a0; RA Yang C.-Y., Chen S.-H., Gianturco S.H., Bradley W.A., Sparrow J.T., RA Tanimura M., Li W.-H., Sparrow D.A., Deloof H., Rosseneu M., Lee F.-S., RA Gu Z.-W., Gotto A.M. Jr., Chan L.; RT "Sequence, structure, receptor-binding domains and internal repeats of RT human apolipoprotein B-100."; RL Nature 323:738-742(1986). RN [30] RP CALCIUM-BINDING. RX PubMed=3087360; DOI=10.1016/0006-291x(86)91237-4; RA Dashti N., Lee D.M., Mok T.; RT "Apolipoprotein B is a calcium binding protein."; RL Biochem. Biophys. Res. Commun. 137:493-499(1986). RN [31] RP PALMITOYLATION AT CYS-1112. RX PubMed=10679026; DOI=10.1091/mbc.11.2.721; RA Zhao Y., McCabe J.B., Vance J., Berthiaume L.G.; RT "Palmitoylation of apolipoprotein B is required for proper intracellular RT sorting and transport of cholesteroyl esters and triglycerides."; RL Mol. Biol. Cell 11:721-734(2000). RN [32] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3358. RC TISSUE=Plasma; RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [33] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1523; ASN-2982; ASN-3465 AND RP ASN-3895. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [34] RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x; RA Leong W.F., Chow V.T.; RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal RT differential cellular gene expression in response to enterovirus 71 RT infection."; RL Cell. Microbiol. 8:565-580(2006). RN [35] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185; ASN-1523; ASN-2239; RP ASN-2779; ASN-2982; ASN-3101; ASN-3224; ASN-3411; ASN-3465 AND ASN-3895. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [36] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2004, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [37] RP INVOLVEMENT IN LDLCQ4, AND VARIANT ILE-98. RX PubMed=20686565; DOI=10.1038/nature09270; RA Teslovich T.M., Musunuru K., Smith A.V., Edmondson A.C., Stylianou I.M., RA Koseki M., Pirruccello J.P., Ripatti S., Chasman D.I., Willer C.J., RA Johansen C.T., Fouchier S.W., Isaacs A., Peloso G.M., Barbalic M., RA Ricketts S.L., Bis J.C., Aulchenko Y.S., Thorleifsson G., Feitosa M.F., RA Chambers J., Orho-Melander M., Melander O., Johnson T., Li X., Guo X., RA Li M., Shin Cho Y., Jin Go M., Jin Kim Y., Lee J.Y., Park T., Kim K., RA Sim X., Twee-Hee Ong R., Croteau-Chonka D.C., Lange L.A., Smith J.D., RA Song K., Hua Zhao J., Yuan X., Luan J., Lamina C., Ziegler A., Zhang W., RA Zee R.Y., Wright A.F., Witteman J.C., Wilson J.F., Willemsen G., RA Wichmann H.E., Whitfield J.B., Waterworth D.M., Wareham N.J., Waeber G., RA Vollenweider P., Voight B.F., Vitart V., Uitterlinden A.G., Uda M., RA Tuomilehto J., Thompson J.R., Tanaka T., Surakka I., Stringham H.M., RA Spector T.D., Soranzo N., Smit J.H., Sinisalo J., Silander K., RA Sijbrands E.J., Scuteri A., Scott J., Schlessinger D., Sanna S., RA Salomaa V., Saharinen J., Sabatti C., Ruokonen A., Rudan I., Rose L.M., RA Roberts R., Rieder M., Psaty B.M., Pramstaller P.P., Pichler I., Perola M., RA Penninx B.W., Pedersen N.L., Pattaro C., Parker A.N., Pare G., Oostra B.A., RA O'Donnell C.J., Nieminen M.S., Nickerson D.A., Montgomery G.W., RA Meitinger T., McPherson R., McCarthy M.I., McArdle W., Masson D., RA Martin N.G., Marroni F., Mangino M., Magnusson P.K., Lucas G., Luben R., RA Loos R.J., Lokki M.L., Lettre G., Langenberg C., Launer L.J., Lakatta E.G., RA Laaksonen R., Kyvik K.O., Kronenberg F., Konig I.R., Khaw K.T., Kaprio J., RA Kaplan L.M., Johansson A., Jarvelin M.R., Janssens A.C., Ingelsson E., RA Igl W., Kees Hovingh G., Hottenga J.J., Hofman A., Hicks A.A., RA Hengstenberg C., Heid I.M., Hayward C., Havulinna A.S., Hastie N.D., RA Harris T.B., Haritunians T., Hall A.S., Gyllensten U., Guiducci C., RA Groop L.C., Gonzalez E., Gieger C., Freimer N.B., Ferrucci L., Erdmann J., RA Elliott P., Ejebe K.G., Doring A., Dominiczak A.F., Demissie S., RA Deloukas P., de Geus E.J., de Faire U., Crawford G., Collins F.S., RA Chen Y.D., Caulfield M.J., Campbell H., Burtt N.P., Bonnycastle L.L., RA Boomsma D.I., Boekholdt S.M., Bergman R.N., Barroso I., Bandinelli S., RA Ballantyne C.M., Assimes T.L., Quertermous T., Altshuler D., Seielstad M., RA Wong T.Y., Tai E.S., Feranil A.B., Kuzawa C.W., Adair L.S., RA Taylor H.A. Jr., Borecki I.B., Gabriel S.B., Wilson J.G., Holm H., RA Thorsteinsdottir U., Gudnason V., Krauss R.M., Mohlke K.L., Ordovas J.M., RA Munroe P.B., Kooner J.S., Tall A.R., Hegele R.A., Kastelein J.J., RA Schadt E.E., Rotter J.I., Boerwinkle E., Strachan D.P., Mooser V., RA Stefansson K., Reilly M.P., Samani N.J., Schunkert H., Cupples L.A., RA Sandhu M.S., Ridker P.M., Rader D.J., van Duijn C.M., Peltonen L., RA Abecasis G.R., Boehnke M., Kathiresan S.; RT "Biological, clinical and population relevance of 95 loci for blood RT lipids."; RL Nature 466:707-713(2010). RN [38] 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 [39] RP INVOLVEMENT IN FHBL1. RX PubMed=21981844; DOI=10.1016/j.jacl.2011.06.014; RA Gangloff A., Bergeron J., Couture P., Martins R., Hegele R.A., Gagne C.; RT "A novel mutation of apolipoprotein B in a French Canadian family with RT homozygous hypobetalipoproteinemia."; RL J. Clin. Lipidol. 5:414-417(2011). RN [40] RP SUBCELLULAR LOCATION, AND INTERACTION WITH PCSK9. RX PubMed=22580899; DOI=10.1161/atvbaha.112.250043; RA Sun H., Samarghandi A., Zhang N., Yao Z., Xiong M., Teng B.B.; RT "Proprotein convertase subtilisin/kexin type 9 interacts with RT apolipoprotein B and prevents its intracellular degradation, irrespective RT of the low-density lipoprotein receptor."; RL Arterioscler. Thromb. Vasc. Biol. 32:1585-1595(2012). RN [41] RP RNA EDITING. RX PubMed=24916387; DOI=10.15252/embr.201438450; RA Fossat N., Tourle K., Radziewic T., Barratt K., Liebhold D., Studdert J.B., RA Power M., Jones V., Loebel D.A., Tam P.P.; RT "C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RT RBM47."; RL EMBO Rep. 15:903-910(2014). RN [42] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3279; SER-4048 AND THR-4052, RP AND IDENTIFICATION BY 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 [43] RP PHOSPHORYLATION AT SER-4048. 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 [44] RP INTERACTION WITH MTTP, AND SUBCELLULAR LOCATION. RX PubMed=26224785; DOI=10.1161/circgenetics.115.001106; RA Walsh M.T., Iqbal J., Josekutty J., Soh J., Di Leo E., Oezaydin E., RA Guenduez M., Tarugi P., Hussain M.M.; RT "A novel abetalipoproteinemia missense mutation highlights the importance RT of N-Terminal beta-barrel in microsomal triglyceride transfer protein RT function."; RL Circ. Cardiovasc. Genet. 8:677-687(2015). RN [45] RP INTERACTION WITH AUP1, AND SUBCELLULAR LOCATION. RX PubMed=28183703; DOI=10.1161/atvbaha.117.309000; RA Zhang J., Zamani M., Thiele C., Taher J., Amir Alipour M., Yao Z., RA Adeli K.; RT "AUP1 (Ancient Ubiquitous Protein 1) Is a Key Determinant of Hepatic Very- RT Low-Density Lipoprotein Assembly and Secretion."; RL Arterioscler. Thromb. Vasc. Biol. 37:633-642(2017). RN [46] RP VARIANT ASN-4338. RX PubMed=1979313; DOI=10.1007/bf00205183; RA Navajas M., Laurent A.-M., Moreel J.-F., Ragab A., Cambou J.-P., Cunny G., RA Cambien F., Roizes G.; RT "Detection by denaturing gradient gel electrophoresis of a new polymorphism RT in the apolipoprotein B gene."; RL Hum. Genet. 86:91-93(1990). RN [47] RP VARIANT FHCL2 GLN-3527. RX PubMed=2563166; DOI=10.1073/pnas.86.2.587; RA Soria L.F., Ludwig E.H., Clarke H.R.G., Vega G.L., Grundy S.M., RA McCarthy B.J.; RT "Association between a specific apolipoprotein B mutation and familial RT defective apolipoprotein B-100."; RL Proc. Natl. Acad. Sci. U.S.A. 86:587-591(1989). RN [48] RP VARIANT LEU-2739. RX PubMed=2216805; DOI=10.1093/nar/18.19.5922-a; RA Huang L.-S., Gavish D., Breslow J.L.; RT "Sequence polymorphism in the human apoB gene at position 8344."; RL Nucleic Acids Res. 18:5922-5922(1990). RN [49] RP VARIANT FHCL2 CYS-3558. RX PubMed=7883971; DOI=10.1172/jci117772; RA Pullinger C.R., Hennessy L.K., Chatterton J.E., Liu W., Love J.A., RA Mendel C.M., Frost P.H., Malloy M.J., Schumaker V.N., Kane J.P.; RT "Familial ligand-defective apolipoprotein B. Identification of a new RT mutation that decreases LDL receptor binding affinity."; RL J. Clin. Invest. 95:1225-1234(1995). RN [50] RP VARIANTS LEU-1437; SER-1914; LYS-2566; THR-3121; ALA-3945; MET-4128 AND RP THR-4481. RX PubMed=8889592; RX DOI=10.1002/(sici)1098-1004(1996)8:3<282::aid-humu16>3.0.co;2-z; RA Poirier O., Ricard S., Behague I., Souriau C., Evans A.E., Arveiler D., RA Marques-Vidal P., Luc G., Roizes G., Cambien F.; RT "Detection of new variants in the apolipoprotein B (Apo B) gene by PCR- RT SSCP."; RL Hum. Mutat. 8:282-285(1996). RN [51] RP VARIANTS FHCL2 GLN-3527 AND CYS-3558. RX PubMed=9259199; RX DOI=10.1002/(sici)1098-1004(1997)10:2<160::aid-humu8>3.0.co;2-o; RA Rabes J.P., Varret M., Saint-Jore B., Erlich D., Jondeau G., Krempf M., RA Giraudet P., Junien C., Boileau C.; RT "Familial ligand-defective apolipoprotein B-100: simultaneous detection of RT the Arg3500-->Gln and Arg3531-->Cys mutations in a French population."; RL Hum. Mutat. 10:160-163(1997). RN [52] RP VARIANTS SER-1914; ARG-1923; LEU-2739; HIS-3319; LYS-3427; GLU-3432 AND RP ILE-3921. RX PubMed=9490296; DOI=10.1007/s004390050651; RA Leren T.P., Bakken K.S., Hoel V., Hjermann I., Berg K.; RT "Screening for mutations of the apolipoprotein B gene causing RT hypocholesterolemia."; RL Hum. Genet. 102:44-49(1998). RN [53] RP VARIANT FHBL1 TRP-490, VARIANT ILE-98, CHARACTERIZATION OF VARIANT TRP-490, RP AND MUTAGENESIS OF ASP-483 AND ARG-490. RX PubMed=12551903; DOI=10.1074/jbc.m300235200; RA Burnett J.R., Shan J., Miskie B.A., Whitfield A.J., Yuan J., Tran K., RA McKnight C.J., Hegele R.A., Yao Z.; RT "A novel nontruncating APOB gene mutation, R463W, causes familial RT hypobetalipoproteinemia."; RL J. Biol. Chem. 278:13442-13452(2003). RN [54] RP VARIANT HIS-1128. RX PubMed=14732481; DOI=10.1016/j.bbadis.2003.11.002; RA Lancellotti S., Di Leo E., Penacchioni J.Y., Balli F., Viola L., RA Bertolini S., Calandra S., Tarugi P.; RT "Hypobetalipoproteinemia with an apparently recessive inheritance due to a RT 'de novo' mutation of apolipoprotein B."; RL Biochim. Biophys. Acta 1688:61-67(2004). RN [55] RP VARIANT [LARGE SCALE ANALYSIS] CYS-2564. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [56] RP VARIANT FHCL2 GLN-3527. RX PubMed=21382890; DOI=10.1161/circulationaha.110.979450; RA van der Graaf A., Avis H.J., Kusters D.M., Vissers M.N., Hutten B.A., RA Defesche J.C., Huijgen R., Fouchier S.W., Wijburg F.A., Kastelein J.J., RA Wiegman A.; RT "Molecular basis of autosomal dominant hypercholesterolemia: assessment in RT a large cohort of hypercholesterolemic children."; RL Circulation 123:1167-1173(2011). RN [57] RP VARIANTS GLU-1218; ASP-1670; ASN-2037; CYS-2564 AND LYS-2566, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22028381; DOI=10.1093/jmcb/mjr024; RA Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., RA Zeng R., Wu J.R.; RT "Quantitative detection of single amino acid polymorphisms by targeted RT proteomics."; RL J. Mol. Cell Biol. 3:309-315(2011). RN [58] RP VARIANTS 12-LEU--LEU-14 DEL; ILE-98; VAL-618; ILE-730; THR-1613; ARG-1923; RP LYS-2566; LEU-2739; GLN-3638; LEU-3835; LYS-4181; THR-4270; VAL-4314; RP ASN-4338; THR-4481 AND VAL-4482. RX PubMed=22095935; DOI=10.1002/humu.21660; RA Huijgen R., Sjouke B., Vis K., de Randamie J.S., Defesche J.C., RA Kastelein J.J., Hovingh G.K., Fouchier S.W.; RT "Genetic variation in APOB, PCSK9, and ANGPTL3 in carriers of pathogenic RT autosomal dominant hypercholesterolemic mutations with unexpected low LDL- RT Cl Levels."; RL Hum. Mutat. 33:448-455(2012). RN [59] RP VARIANT FHBL1 LEU-952, VARIANT THR-251, CHARACTERIZATION OF VARIANT FHBL1 RP LEU-952, CHARACTERIZATION OF VARIANT THR-251, AND INTERACTION WITH MTTP. RX PubMed=27206948; DOI=10.1016/j.jacl.2016.01.006; RA Miller S.A., Hooper A.J., Mantiri G.A., Marais D., Tanyanyiwa D.M., RA McKnight J., Burnett J.R.; RT "Novel APOB missense variants, A224T and V925L, in a black South African RT woman with marked hypocholesterolemia."; RL J. Clin. Lipidol. 10:604-609(2016). CC -!- FUNCTION: Apolipoprotein B is a major protein constituent of CC chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B- CC 100 functions as a recognition signal for the cellular binding and CC internalization of LDL particles by the apoB/E receptor. CC -!- SUBUNIT: Interacts with PCSK9 (PubMed:22580899). Interacts with MTTP CC (PubMed:26224785, PubMed:27206948). Interacts with AUP1 CC (PubMed:28183703). Interacts with CIDEB (By similarity). CC {ECO:0000250|UniProtKB:E9Q414, ECO:0000269|PubMed:22580899, CC ECO:0000269|PubMed:26224785, ECO:0000269|PubMed:27206948, CC ECO:0000269|PubMed:28183703}. CC -!- INTERACTION: CC P04114; P01130: LDLR; NbExp=4; IntAct=EBI-3926040, EBI-988319; CC P04114; P55157: MTTP; NbExp=4; IntAct=EBI-3926040, EBI-11614052; CC P04114; PRO_0000037946 [P29991]; Xeno; NbExp=3; IntAct=EBI-3926040, EBI-8826488; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22580899}. Secreted CC {ECO:0000269|PubMed:22580899, ECO:0000269|PubMed:26224785}. Lipid CC droplet {ECO:0000269|PubMed:28183703}. CC -!- INDUCTION: Up-regulated in response to enterovirus 71 (EV71) infection CC (at protein level). {ECO:0000269|PubMed:16548883}. CC -!- PTM: Palmitoylated; structural requirement for proper assembly of the CC hydrophobic core of the lipoprotein particle. CC {ECO:0000269|PubMed:10679026}. CC -!- RNA EDITING: Modified_positions=2180; Note=The stop codon (UAA) at CC position 2180 is created by an APOBEC1-containing mRNA editing complex. CC Apo B-48, derived from the fully edited RNA, is produced only in the CC intestine and is found in chylomicrons. Apo B-48 is a shortened form of CC apo B-100 which lacks the LDL-receptor region. The unedited version CC (apo B-100) is produced by the liver and is found in the VLDL and LDL. CC {ECO:0000269|PubMed:2450346, ECO:0000269|PubMed:24916387, CC ECO:0000269|PubMed:3426612, ECO:0000269|PubMed:3621347, CC ECO:0000269|PubMed:3659919}; CC -!- POLYMORPHISM: Genetic variations in APOB define the low density CC lipoprotein cholesterol level quantitative trait locus 4 (LDLCQ4) CC [MIM:615558]. CC -!- DISEASE: Hypobetalipoproteinemia, familial, 1 (FHBL1) [MIM:615558]: A CC disorder of lipid metabolism characterized by less than 5th percentile CC age- and sex-specific levels of low density lipoproteins, and dietary CC fat malabsorption. Clinical presentation may vary from no symptoms to CC severe gastrointestinal and neurological dysfunction similar to CC abetalipoproteinemia. {ECO:0000269|PubMed:12551903, CC ECO:0000269|PubMed:21981844, ECO:0000269|PubMed:27206948}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. Most cases of FHBL1 result from nonsense mutations in the APOB CC gene that lead to a premature stop codon, which generate prematurely CC truncated apo B protein products (PubMed:21981844). CC {ECO:0000269|PubMed:21981844}. CC -!- DISEASE: Hypercholesterolemia, familial, 2 (FHCL2) [MIM:144010]: A form CC of hypercholesterolemia, a disorder of lipoprotein metabolism CC characterized by elevated serum low-density lipoprotein (LDL) CC cholesterol levels, which result in excess deposition of cholesterol in CC tissues and leads to xanthelasma, xanthomas, accelerated CC atherosclerosis and increased risk of premature coronary heart disease. CC FHCL2 inheritance is autosomal dominant. {ECO:0000269|PubMed:21382890, CC ECO:0000269|PubMed:2563166, ECO:0000269|PubMed:7883971, CC ECO:0000269|PubMed:9259199}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Note=Defects in APOB associated with defects in other genes CC (polygenic) can contribute to hypocholesterolemia. CC -!- SEQUENCE CAUTION: CC Sequence=AAA51752.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Apolipoprotein B entry; CC URL="https://en.wikipedia.org/wiki/Apolipoprotein_B"; 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; X04506; CAA28191.1; -; mRNA. DR EMBL; M19828; AAB00481.1; -; Genomic_DNA. DR EMBL; M19808; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19809; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19810; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19811; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19812; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19813; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19815; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19816; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19818; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19820; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19821; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19823; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19824; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19825; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; M19827; AAB00481.1; JOINED; Genomic_DNA. DR EMBL; J02610; AAA35549.1; -; mRNA. DR EMBL; M14162; AAB04636.1; -; mRNA. DR EMBL; M15053; AAB60718.1; -; Genomic_DNA. DR EMBL; X04714; CAA28420.1; -; mRNA. DR EMBL; AY324608; AAP72970.1; -; Genomic_DNA. DR EMBL; AC010872; AAX88848.1; -; Genomic_DNA. DR EMBL; AC115619; AAX93246.1; -; Genomic_DNA. DR EMBL; M14081; AAA51752.1; ALT_FRAME; mRNA. DR EMBL; M12681; AAA51753.1; -; mRNA. DR EMBL; M12480; AAA51751.1; -; mRNA. DR EMBL; K03175; AAA51759.1; -; mRNA. DR EMBL; M15421; AAA51758.1; -; mRNA. DR EMBL; M17367; AAA51741.1; -; mRNA. DR EMBL; M31030; AAA51756.1; -; mRNA. DR EMBL; X03325; CAA27044.1; -; mRNA. DR EMBL; X03326; CAA27045.1; -; mRNA. DR EMBL; M17779; AAA51755.1; -; mRNA. DR EMBL; M19734; AAA35544.1; -; mRNA. DR EMBL; M18471; AAA35541.1; -; mRNA. DR EMBL; X03045; CAA26850.1; -; mRNA. DR EMBL; M10374; AAA51750.1; -; mRNA. DR EMBL; M12413; AAA51742.1; -; mRNA. DR EMBL; M36676; AAA35548.1; -; mRNA. DR CCDS; CCDS1703.1; -. DR PIR; A27850; LPHUB. DR RefSeq; NP_000375.2; NM_000384.2. DR SMR; P04114; -. DR BioGRID; 106835; 225. DR DIP; DIP-44767N; -. DR IntAct; P04114; 68. DR MINT; P04114; -. DR STRING; 9606.ENSP00000233242; -. DR BindingDB; P04114; -. DR ChEMBL; CHEMBL4549; -. DR DrugBank; DB11886; Infigratinib. DR DrugBank; DB00877; Sirolimus. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR CarbonylDB; P04114; -. DR GlyConnect; 57; 67 N-Linked glycans (13 sites). DR GlyCosmos; P04114; 27 sites, 83 glycans. DR GlyGen; P04114; 30 sites, 84 N-linked glycans (16 sites), 3 O-linked glycans (10 sites). DR iPTMnet; P04114; -. DR PhosphoSitePlus; P04114; -. DR SwissPalm; P04114; -. DR BioMuta; APOB; -. DR DMDM; 300669605; -. DR CPTAC; CPTAC-1299; -. DR CPTAC; CPTAC-1300; -. DR CPTAC; CPTAC-2205; -. DR CPTAC; CPTAC-652; -. DR CPTAC; CPTAC-653; -. DR CPTAC; non-CPTAC-1080; -. DR CPTAC; non-CPTAC-1081; -. DR CPTAC; non-CPTAC-1082; -. DR EPD; P04114; -. DR jPOST; P04114; -. DR MassIVE; P04114; -. DR MaxQB; P04114; -. DR PaxDb; 9606-ENSP00000233242; -. DR PeptideAtlas; P04114; -. DR PRIDE; P04114; -. DR ProteomicsDB; 51654; -. DR Pumba; P04114; -. DR ABCD; P04114; 1 sequenced antibody. DR Antibodypedia; 4232; 1170 antibodies from 41 providers. DR CPTC; P04114; 3 antibodies. DR DNASU; 338; -. DR Ensembl; ENST00000233242.5; ENSP00000233242.1; ENSG00000084674.15. DR GeneID; 338; -. DR KEGG; hsa:338; -. DR MANE-Select; ENST00000233242.5; ENSP00000233242.1; NM_000384.3; NP_000375.3. DR UCSC; uc002red.3; human. DR AGR; HGNC:603; -. DR CTD; 338; -. DR DisGeNET; 338; -. DR GeneCards; APOB; -. DR GeneReviews; APOB; -. DR HGNC; HGNC:603; APOB. DR HPA; ENSG00000084674; Group enriched (intestine, liver). DR MalaCards; APOB; -. DR MIM; 107730; gene. DR MIM; 144010; phenotype. DR MIM; 615558; phenotype. DR neXtProt; NX_P04114; -. DR OpenTargets; ENSG00000084674; -. DR Orphanet; 391665; Homozygous familial hypercholesterolemia. DR Orphanet; 426; NON RARE IN EUROPE: Familial hypobetalipoproteinemia. DR Orphanet; 406; NON RARE IN EUROPE: Heterozygous familial hypercholesterolemia. DR PharmGKB; PA50; -. DR VEuPathDB; HostDB:ENSG00000084674; -. DR eggNOG; KOG4338; Eukaryota. DR GeneTree; ENSGT00590000083139; -. DR InParanoid; P04114; -. DR OrthoDB; 5349904at2759; -. DR PhylomeDB; P04114; -. DR TreeFam; TF331316; -. DR PathwayCommons; P04114; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-3000471; Scavenging by Class B Receptors. DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors. DR Reactome; R-HSA-3000484; Scavenging by Class F Receptors. DR Reactome; R-HSA-3000497; Scavenging by Class H Receptors. 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-432142; Platelet sensitization by LDL. DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand. DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR Reactome; R-HSA-8866423; VLDL assembly. DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR Reactome; R-HSA-8963888; Chylomicron assembly. DR Reactome; R-HSA-8963901; Chylomicron remodeling. DR Reactome; R-HSA-8964026; Chylomicron clearance. DR Reactome; R-HSA-8964038; LDL clearance. DR Reactome; R-HSA-8964041; LDL remodeling. DR Reactome; R-HSA-8964046; VLDL clearance. DR Reactome; R-HSA-9707616; Heme signaling. DR Reactome; R-HSA-975634; Retinoid metabolism and transport. DR SignaLink; P04114; -. DR SIGNOR; P04114; -. DR BioGRID-ORCS; 338; 12 hits in 1151 CRISPR screens. DR ChiTaRS; APOB; human. DR GeneWiki; Apolipoprotein_B; -. DR GenomeRNAi; 338; -. DR Pharos; P04114; Tchem. DR PRO; PR:P04114; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P04114; Protein. DR Bgee; ENSG00000084674; Expressed in jejunal mucosa and 86 other cell types or tissues. DR ExpressionAtlas; P04114; baseline and differential. DR GO; GO:0042627; C:chylomicron; IDA:BHF-UCL. DR GO; GO:0034360; C:chylomicron remnant; TAS:BHF-UCL. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005769; C:early endosome; TAS:Reactome. DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome. DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031904; C:endosome lumen; TAS:Reactome. DR GO; GO:0010008; C:endosome membrane; 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; ISS:BHF-UCL. DR GO; GO:0034363; C:intermediate-density lipoprotein particle; IDA:BHF-UCL. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell. DR GO; GO:0034362; C:low-density lipoprotein particle; IDA:BHF-UCL. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0034359; C:mature chylomicron; IDA:BHF-UCL. DR GO; GO:0043025; C:neuronal cell body; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005790; C:smooth endoplasmic reticulum; TAS:Reactome. DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL. DR GO; GO:0120020; F:cholesterol transfer activity; IMP:BHF-UCL. DR GO; GO:0008201; F:heparin binding; IDA:BHF-UCL. DR GO; GO:0035473; F:lipase binding; IPI:BHF-UCL. DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IMP:BHF-UCL. DR GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL. DR GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl. DR GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl. DR GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL. DR GO; GO:0008203; P:cholesterol metabolic process; IMP:BHF-UCL. DR GO; GO:0030301; P:cholesterol transport; IMP:BHF-UCL. DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl. DR GO; GO:0009566; P:fertilization; IEA:Ensembl. DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl. DR GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl. DR GO; GO:0042953; P:lipoprotein transport; IBA:GO_Central. DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL. DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IMP:BHF-UCL. DR GO; GO:0007399; P:nervous system development; IEA:Ensembl. DR GO; GO:0010886; P:positive regulation of cholesterol storage; IDA:BHF-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0010884; P:positive regulation of lipid storage; IDA:BHF-UCL. DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IEA:Ensembl. DR GO; GO:0009615; P:response to virus; IEP:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0019433; P:triglyceride catabolic process; IEA:Ensembl. DR GO; GO:0006642; P:triglyceride mobilization; IBA:GO_Central. DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IC:BHF-UCL. DR Gene3D; 2.20.80.10; Lipovitellin-phosvitin complex, chain A, domain 4; 1. DR Gene3D; 2.20.50.20; Lipovitellin. Chain A, domain 3; 1. DR Gene3D; 1.25.10.20; Vitellinogen, superhelical; 1. DR InterPro; IPR022176; ApoB100_C. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR015819; Lipid_transp_b-sht_shell. DR InterPro; IPR009454; Lipid_transpt_open_b-sht. DR InterPro; IPR011030; Lipovitellin_superhlx_dom. DR InterPro; IPR015816; Vitellinogen_b-sht_N. DR InterPro; IPR015255; Vitellinogen_open_b-sht. DR InterPro; IPR015817; Vitellinogen_open_b-sht_sub1. DR InterPro; IPR001747; Vitellogenin_N. DR PANTHER; PTHR13769; APOLIPOPROTEIN B; 1. DR PANTHER; PTHR13769:SF1; APOLIPOPROTEIN B-100; 1. DR Pfam; PF12491; ApoB100_C; 1. DR Pfam; PF06448; DUF1081; 1. DR Pfam; PF09172; Vit_open_b-sht; 1. DR Pfam; PF01347; Vitellogenin_N; 1. DR SMART; SM01169; DUF1943; 1. DR SMART; SM00638; LPD_N; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF48431; Lipovitellin-phosvitin complex, superhelical domain; 1. DR PROSITE; PS51211; VITELLOGENIN; 1. DR Genevisible; P04114; HS. PE 1: Evidence at protein level; KW Acetylation; Atherosclerosis; Cholesterol metabolism; Chylomicron; KW Cytoplasm; Direct protein sequencing; Disease variant; Disulfide bond; KW Glycoprotein; Heparin-binding; LDL; Lipid droplet; Lipid metabolism; KW Lipid transport; Lipoprotein; Palmitate; Phosphoprotein; KW Reference proteome; RNA editing; Secreted; Signal; Steroid metabolism; KW Sterol metabolism; Transport; VLDL. FT SIGNAL 1..27 FT CHAIN 28..4563 FT /note="Apolipoprotein B-100" FT /id="PRO_0000020750" FT CHAIN 28..2179 FT /note="Apolipoprotein B-48" FT /id="PRO_0000020751" FT DOMAIN 46..672 FT /note="Vitellogenin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557" FT REGION 32..126 FT /note="Heparin-binding" FT REGION 232..306 FT /note="Heparin-binding" FT REGION 902..959 FT /note="Heparin-binding" FT REGION 2043..2178 FT /note="Heparin-binding" FT REGION 3161..3236 FT /note="Heparin-binding" FT REGION 3174..3184 FT /note="Basic (possible receptor binding region)" FT REGION 3373..3393 FT /note="LDL receptor binding" FT REGION 3383..3516 FT /note="Heparin-binding" FT REGION 3386..3394 FT /note="Basic (possible receptor binding region)" FT MOD_RES 2004 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 3279 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 4048 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039, FT ECO:0007744|PubMed:24275569" FT MOD_RES 4052 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT LIPID 1112 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:10679026" FT CARBOHYD 34 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 185 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 983 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1368 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1377 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1523 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 2239 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 2560 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2779 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 2982 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 3101 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 3224 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 3336 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 3358 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:14760718" FT CARBOHYD 3411 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 3465 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 3895 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 4237 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 4431 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 39..88 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557, FT ECO:0000269|PubMed:2115173" FT DISULFID 78..97 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557, FT ECO:0000269|PubMed:2115173" FT DISULFID 186..212 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557, FT ECO:0000269|PubMed:2115173" FT DISULFID 245..261 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557, FT ECO:0000269|PubMed:2115173" FT DISULFID 385..390 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557, FT ECO:0000269|PubMed:2115173" FT DISULFID 478..513 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557, FT ECO:0000269|PubMed:2115173" FT DISULFID 966..976 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557, FT ECO:0000269|PubMed:2115173" FT DISULFID 3194..3324 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557, FT ECO:0000269|PubMed:2115173" FT VARIANT 12..14 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:22095935" FT /id="VAR_067277" FT VARIANT 98 FT /note="T -> I (influences plasma concentrations of low FT density lipoprotein cholesterol; dbSNP:rs1367117)" FT /evidence="ECO:0000269|PubMed:12551903, FT ECO:0000269|PubMed:20686565, ECO:0000269|PubMed:2115173, FT ECO:0000269|PubMed:22095935, ECO:0000269|PubMed:3461454, FT ECO:0000269|PubMed:3759943" FT /id="VAR_016184" FT VARIANT 103 FT /note="Y -> H (in dbSNP:rs9282603)" FT /id="VAR_022036" FT VARIANT 145 FT /note="P -> S (in dbSNP:rs6752026)" FT /id="VAR_022037" FT VARIANT 194 FT /note="T -> M (in dbSNP:rs13306198)" FT /id="VAR_056737" FT VARIANT 251 FT /note="A -> T (does not affect plasma lipid levels; FT dbSNP:rs61741625)" FT /evidence="ECO:0000269|PubMed:27206948" FT /id="VAR_076538" FT VARIANT 273 FT /note="K -> N" FT /evidence="ECO:0000269|PubMed:3763409" FT /id="VAR_019827" FT VARIANT 408 FT /note="I -> T (in dbSNP:rs12714225)" FT /id="VAR_029341" FT VARIANT 490 FT /note="R -> W (in FHBL1; reduced protein secretion; FT dbSNP:rs771541567)" FT /evidence="ECO:0000269|PubMed:12551903" FT /id="VAR_022610" FT VARIANT 554 FT /note="P -> L (in dbSNP:rs12714214)" FT /id="VAR_020135" FT VARIANT 618 FT /note="A -> V (in dbSNP:rs679899)" FT /evidence="ECO:0000269|PubMed:22095935, FT ECO:0000269|PubMed:3030729, ECO:0000269|PubMed:3759943" FT /id="VAR_019828" FT VARIANT 730 FT /note="V -> I (in dbSNP:rs12691202)" FT /evidence="ECO:0000269|PubMed:22095935" FT /id="VAR_020136" FT VARIANT 733 FT /note="V -> I (in dbSNP:rs1800476)" FT /id="VAR_016185" FT VARIANT 741 FT /note="T -> N (in dbSNP:rs12714192)" FT /id="VAR_020137" FT VARIANT 877 FT /note="P -> L (in dbSNP:rs12714097)" FT /id="VAR_029342" FT VARIANT 952 FT /note="V -> L (in FHBL1; uncertain significance; does not FT affect interaction with MTTP)" FT /evidence="ECO:0000269|PubMed:27206948" FT /id="VAR_076539" FT VARIANT 955 FT /note="P -> S (in dbSNP:rs13306206)" FT /id="VAR_056738" FT VARIANT 1086 FT /note="G -> S (in dbSNP:rs12720801)" FT /id="VAR_029343" FT VARIANT 1113 FT /note="D -> H (in dbSNP:rs12713844)" FT /id="VAR_029344" FT VARIANT 1128 FT /note="R -> H (in dbSNP:rs12713843)" FT /evidence="ECO:0000269|PubMed:14732481" FT /id="VAR_022611" FT VARIANT 1218 FT /note="Q -> E (in dbSNP:rs1041956)" FT /evidence="ECO:0000269|PubMed:22028381, FT ECO:0000269|PubMed:3763409" FT /id="VAR_019829" FT VARIANT 1388 FT /note="R -> H (in dbSNP:rs13306187)" FT /id="VAR_029345" FT VARIANT 1422 FT /note="C -> Y (in dbSNP:rs568413)" FT /evidence="ECO:0000269|PubMed:15815621" FT /id="VAR_061558" FT VARIANT 1437 FT /note="F -> L (in dbSNP:rs1801697)" FT /evidence="ECO:0000269|PubMed:8889592" FT /id="VAR_005016" FT VARIANT 1613 FT /note="S -> T (in dbSNP:rs61742247)" FT /evidence="ECO:0000269|PubMed:22095935" FT /id="VAR_067278" FT VARIANT 1670 FT /note="E -> D (in dbSNP:rs773681906)" FT /evidence="ECO:0000269|PubMed:22028381, FT ECO:0000269|PubMed:3461454" FT /id="VAR_068911" FT VARIANT 1914 FT /note="N -> S (in dbSNP:rs1801699)" FT /evidence="ECO:0000269|PubMed:8889592, FT ECO:0000269|PubMed:9490296" FT /id="VAR_005017" FT VARIANT 1923 FT /note="H -> R (in dbSNP:rs533617)" FT /evidence="ECO:0000269|PubMed:22095935, FT ECO:0000269|PubMed:9490296" FT /id="VAR_005018" FT VARIANT 2037 FT /note="I -> N" FT /evidence="ECO:0000269|PubMed:22028381, FT ECO:0000269|PubMed:3464946" FT /id="VAR_068912" FT VARIANT 2092 FT /note="L -> V (in dbSNP:rs1041960)" FT /evidence="ECO:0000269|PubMed:3763409" FT /id="VAR_019830" FT VARIANT 2299 FT /note="D -> H (in dbSNP:rs12713681)" FT /id="VAR_029346" FT VARIANT 2313 FT /note="I -> V (in dbSNP:rs584542)" FT /evidence="ECO:0000269|PubMed:2883086, FT ECO:0000269|PubMed:3030729, ECO:0000269|PubMed:3464946, FT ECO:0000269|PubMed:3652907, ECO:0000269|PubMed:3676265, FT ECO:0000269|PubMed:3759943, ECO:0000269|PubMed:3763409, FT ECO:0000269|Ref.6" FT /id="VAR_059582" FT VARIANT 2365 FT /note="A -> T (in dbSNP:rs1041971)" FT /evidence="ECO:0000269|PubMed:3763409" FT /id="VAR_019831" FT VARIANT 2456 FT /note="A -> D (in dbSNP:rs12713675)" FT /id="VAR_020138" FT VARIANT 2564 FT /note="F -> C (in a colorectal cancer sample; somatic FT mutation; confirmed at protein level)" FT /evidence="ECO:0000269|PubMed:16959974, FT ECO:0000269|PubMed:22028381" FT /id="VAR_035795" FT VARIANT 2566 FT /note="E -> K (in dbSNP:rs1801696)" FT /evidence="ECO:0000269|PubMed:22028381, FT ECO:0000269|PubMed:22095935, ECO:0000269|PubMed:8889592" FT /id="VAR_005019" FT VARIANT 2680 FT /note="L -> Q (in dbSNP:rs1042013)" FT /evidence="ECO:0000269|PubMed:3763409" FT /id="VAR_019832" FT VARIANT 2739 FT /note="P -> L (in dbSNP:rs676210)" FT /evidence="ECO:0000269|PubMed:22095935, FT ECO:0000269|PubMed:2216805, ECO:0000269|PubMed:9490296" FT /id="VAR_005020" FT VARIANT 2785 FT /note="N -> H (in dbSNP:rs2163204)" FT /id="VAR_022038" FT VARIANT 3121 FT /note="A -> T (in dbSNP:rs1801694)" FT /evidence="ECO:0000269|PubMed:8889592" FT /id="VAR_005021" FT VARIANT 3182 FT /note="H -> N (in dbSNP:rs12720848)" FT /id="VAR_029347" FT VARIANT 3279 FT /note="S -> G (in dbSNP:rs12720854)" FT /id="VAR_029348" FT VARIANT 3294 FT /note="S -> P (in dbSNP:rs12720855)" FT /id="VAR_020139" FT VARIANT 3319 FT /note="D -> H (in dbSNP:rs1042021)" FT /evidence="ECO:0000269|PubMed:2883086, FT ECO:0000269|PubMed:2994225, ECO:0000269|PubMed:3030729, FT ECO:0000269|PubMed:3464946, ECO:0000269|PubMed:3652907, FT ECO:0000269|PubMed:3759943, ECO:0000269|PubMed:3763409, FT ECO:0000269|PubMed:9490296" FT /id="VAR_005022" FT VARIANT 3427 FT /note="T -> K (in dbSNP:rs1042022)" FT /evidence="ECO:0000269|PubMed:2883086, FT ECO:0000269|PubMed:2994225, ECO:0000269|PubMed:3030729, FT ECO:0000269|PubMed:3464946, ECO:0000269|PubMed:3652907, FT ECO:0000269|PubMed:3759943, ECO:0000269|PubMed:3763409, FT ECO:0000269|PubMed:9490296" FT /id="VAR_005023" FT VARIANT 3432 FT /note="Q -> E (in dbSNP:rs1042023)" FT /evidence="ECO:0000269|PubMed:2883086, FT ECO:0000269|PubMed:2994225, ECO:0000269|PubMed:3030729, FT ECO:0000269|PubMed:3464946, ECO:0000269|PubMed:3652907, FT ECO:0000269|PubMed:3759943, ECO:0000269|PubMed:3763409, FT ECO:0000269|PubMed:9490296" FT /id="VAR_005024" FT VARIANT 3527 FT /note="R -> Q (in FHCL2; dbSNP:rs5742904)" FT /evidence="ECO:0000269|PubMed:21382890, FT ECO:0000269|PubMed:2563166, ECO:0000269|PubMed:9259199" FT /id="VAR_005025" FT VARIANT 3558 FT /note="R -> C (in FHCL2; dbSNP:rs12713559)" FT /evidence="ECO:0000269|PubMed:7883971, FT ECO:0000269|PubMed:9259199" FT /id="VAR_005026" FT VARIANT 3638 FT /note="R -> Q (in dbSNP:rs1801701)" FT /evidence="ECO:0000269|PubMed:22095935" FT /id="VAR_016186" FT VARIANT 3732 FT /note="I -> T (in dbSNP:rs1042025)" FT /evidence="ECO:0000269|PubMed:2883086, FT ECO:0000269|PubMed:2994225, ECO:0000269|PubMed:3030729, FT ECO:0000269|PubMed:3763409" FT /id="VAR_019833" FT VARIANT 3801 FT /note="S -> T (in dbSNP:rs12713540)" FT /id="VAR_029349" FT VARIANT 3835 FT /note="I -> L (in dbSNP:rs776119459)" FT /evidence="ECO:0000269|PubMed:22095935" FT /id="VAR_067279" FT VARIANT 3921 FT /note="V -> I (in dbSNP:rs72654409)" FT /evidence="ECO:0000269|PubMed:9490296" FT /id="VAR_005027" FT VARIANT 3945 FT /note="T -> A (in dbSNP:rs1801698)" FT /evidence="ECO:0000269|PubMed:8889592" FT /id="VAR_005028" FT VARIANT 3949 FT /note="F -> L (in dbSNP:rs1042027)" FT /evidence="ECO:0000269|PubMed:2994225, FT ECO:0000269|PubMed:3030729, ECO:0000269|PubMed:3464946, FT ECO:0000269|PubMed:3763409, ECO:0000269|PubMed:3841481" FT /id="VAR_019834" FT VARIANT 3964 FT /note="Y -> F (in dbSNP:rs1126468)" FT /evidence="ECO:0000269|PubMed:2994225, FT ECO:0000269|PubMed:3030729, ECO:0000269|PubMed:3763409, FT ECO:0000269|PubMed:3841481" FT /id="VAR_019835" FT VARIANT 4128 FT /note="V -> M (in dbSNP:rs1801703)" FT /evidence="ECO:0000269|PubMed:8889592" FT /id="VAR_005029" FT VARIANT 4181 FT /note="E -> K (in dbSNP:rs1042031)" FT /evidence="ECO:0000269|PubMed:22095935, FT ECO:0000269|PubMed:2994225, ECO:0000269|PubMed:3030729, FT ECO:0000269|PubMed:3464946, ECO:0000269|PubMed:3763409, FT ECO:0000269|PubMed:3841481" FT /id="VAR_016187" FT VARIANT 4270 FT /note="R -> T (in dbSNP:rs1801702)" FT /evidence="ECO:0000269|PubMed:22095935" FT /id="VAR_016188" FT VARIANT 4314 FT /note="I -> V (in dbSNP:rs72654423)" FT /evidence="ECO:0000269|PubMed:22095935" FT /id="VAR_067280" FT VARIANT 4338 FT /note="S -> N (in dbSNP:rs1042034)" FT /evidence="ECO:0000269|PubMed:1979313, FT ECO:0000269|PubMed:22095935, ECO:0000269|PubMed:2883086, FT ECO:0000269|PubMed:2932736, ECO:0000269|PubMed:2994225, FT ECO:0000269|PubMed:3030729, ECO:0000269|PubMed:3464946, FT ECO:0000269|PubMed:3652907, ECO:0000269|PubMed:3759943, FT ECO:0000269|PubMed:3763409, ECO:0000269|Ref.6" FT /id="VAR_005030" FT VARIANT 4394 FT /note="V -> A (in dbSNP:rs12720843)" FT /id="VAR_029350" FT VARIANT 4481 FT /note="A -> T (in dbSNP:rs1801695)" FT /evidence="ECO:0000269|PubMed:22095935, FT ECO:0000269|PubMed:8889592" FT /id="VAR_005031" FT VARIANT 4482 FT /note="I -> V (in dbSNP:rs142702699)" FT /evidence="ECO:0000269|PubMed:22095935" FT /id="VAR_067281" FT VARIANT 4484 FT /note="T -> M (in dbSNP:rs12713450)" FT /id="VAR_020140" FT MUTAGEN 483 FT /note="D->N: Impairs protein secretion." FT /evidence="ECO:0000269|PubMed:12551903" FT MUTAGEN 483 FT /note="D->Q: Does not affect protein secretion." FT /evidence="ECO:0000269|PubMed:12551903" FT MUTAGEN 490 FT /note="R->A: Impairs protein secretion." FT /evidence="ECO:0000269|PubMed:12551903" FT MUTAGEN 490 FT /note="R->K: Does not affect protein secretion." FT /evidence="ECO:0000269|PubMed:12551903" FT CONFLICT 11..13 FT /note="Missing (in Ref. 5; AAB60718/CAA28420)" FT /evidence="ECO:0000305" FT CONFLICT 329 FT /note="L -> V (in Ref. 3; AAA35549)" FT /evidence="ECO:0000305" FT CONFLICT 645 FT /note="L -> I (in Ref. 3; AAA35549)" FT /evidence="ECO:0000305" FT CONFLICT 704 FT /note="L -> P (in Ref. 4; AAB04636)" FT /evidence="ECO:0000305" FT CONFLICT 792..809 FT /note="LQLLGKLLLMGARTLQGI -> SSSWKAASHGCPHSAGD (in Ref. 12; FT AAA51759)" FT /evidence="ECO:0000305" FT CONFLICT 793 FT /note="Q -> R (in Ref. 4; AAB04636)" FT /evidence="ECO:0000305" FT CONFLICT 893 FT /note="D -> K (in Ref. 13; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 919 FT /note="A -> P (in Ref. 3; AAA35549)" FT /evidence="ECO:0000305" FT CONFLICT 1109 FT /note="H -> D (in Ref. 5; CAA28420)" FT /evidence="ECO:0000305" FT CONFLICT 1180 FT /note="T -> R (in Ref. 8; AAA51752)" FT /evidence="ECO:0000305" FT CONFLICT 1271 FT /note="F -> S (in Ref. 4; AAB04636)" FT /evidence="ECO:0000305" FT CONFLICT 1418 FT /note="F -> S (in Ref. 5; CAA28420)" FT /evidence="ECO:0000305" FT CONFLICT 1445 FT /note="N -> I (in Ref. 8; AAA51752)" FT /evidence="ECO:0000305" FT CONFLICT 1535 FT /note="G -> E (in Ref. 8; AAA51752)" FT /evidence="ECO:0000305" FT CONFLICT 1867 FT /note="R -> G (in Ref. 4; AAB04636)" FT /evidence="ECO:0000305" FT CONFLICT 2098 FT /note="N -> K (in Ref. 5; CAA28420)" FT /evidence="ECO:0000305" FT CONFLICT 2218 FT /note="I -> T (in Ref. 4; AAB04636)" FT /evidence="ECO:0000305" FT CONFLICT 2221 FT /note="N -> I (in Ref. 5; CAA28420)" FT /evidence="ECO:0000305" FT CONFLICT 2324..2326 FT /note="LIG -> PYW (in Ref. 16; AAA51741)" FT /evidence="ECO:0000305" FT CONFLICT 2353 FT /note="Q -> H (in Ref. 16; AAA51741)" FT /evidence="ECO:0000305" FT CONFLICT 2540 FT /note="G -> S (in Ref. 5; CAA28420)" FT /evidence="ECO:0000305" FT CONFLICT 2718..2737 FT /note="Missing (in Ref. 15; AAA51758)" FT /evidence="ECO:0000305" FT CONFLICT 2933 FT /note="C -> S (in Ref. 4; AAB04636)" FT /evidence="ECO:0000305" FT CONFLICT 3114 FT /note="H -> L (in Ref. 13; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 3131 FT /note="T -> R (in Ref. 13; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 3134 FT /note="E -> P (in Ref. 13; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 3137 FT /note="L -> R (in Ref. 13; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 3239 FT /note="H -> Q (in Ref. 5; CAA28420)" FT /evidence="ECO:0000305" FT CONFLICT 3286 FT /note="L -> I (in Ref. 4; AAB04636)" FT /evidence="ECO:0000305" FT CONFLICT 3291 FT /note="R -> L (in Ref. 15; AAA51758)" FT /evidence="ECO:0000305" FT CONFLICT 3337 FT /note="I -> N (in Ref. 15; AAA51758)" FT /evidence="ECO:0000305" FT CONFLICT 3431 FT /note="A -> P (in Ref. 4; AAB04636)" FT /evidence="ECO:0000305" FT CONFLICT 3728 FT /note="D -> N (in Ref. 24; AAA51742)" FT /evidence="ECO:0000305" FT CONFLICT 3782 FT /note="N -> T (in Ref. 4; AAB04636)" FT /evidence="ECO:0000305" FT CONFLICT 3824 FT /note="Q -> R (in Ref. 5; CAA28420 and 23; AAA51750)" FT /evidence="ECO:0000305" FT CONFLICT 3876 FT /note="V -> A (in Ref. 3; AAA35549 and 24; AAA51742)" FT /evidence="ECO:0000305" FT CONFLICT 3911 FT /note="T -> Y (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 3983 FT /note="F -> S (in Ref. 24; AAA51742)" FT /evidence="ECO:0000305" FT CONFLICT 4002 FT /note="A -> P (in Ref. 24; AAA51742)" FT /evidence="ECO:0000305" FT CONFLICT 4110..4111 FT /note="NN -> DH (in Ref. 3; AAA35549 and 24; AAA51742)" FT /evidence="ECO:0000305" FT CONFLICT 4122 FT /note="Q -> E (in Ref. 3; AAA35549 and 24; AAA51742)" FT /evidence="ECO:0000305" FT CONFLICT 4128 FT /note="V -> E (in Ref. 3; AAA35549 and 24; AAA51742)" FT /evidence="ECO:0000305" FT CONFLICT 4133 FT /note="A -> G (in Ref. 3; AAA35549 and 24; AAA51742)" FT /evidence="ECO:0000305" FT CONFLICT 4188 FT /note="H -> K (in Ref. 4; AAB04636)" FT /evidence="ECO:0000305" FT CONFLICT 4217..4218 FT /note="CT -> FP (in Ref. 26; AAA35548)" FT /evidence="ECO:0000305" FT CONFLICT 4221 FT /note="I -> M (in Ref. 4; AAB04636)" FT /evidence="ECO:0000305" SQ SEQUENCE 4563 AA; 515545 MW; D1073B2D5172A370 CRC64; MDPPRPALLA LLALPALLLL LLAGARAEEE MLENVSLVCP KDATRFKHLR KYTYNYEAES SSGVPGTADS RSATRINCKV ELEVPQLCSF ILKTSQCTLK EVYGFNPEGK ALLKKTKNSE EFAAAMSRYE LKLAIPEGKQ VFLYPEKDEP TYILNIKRGI ISALLVPPET EEAKQVLFLD TVYGNCSTHF TVKTRKGNVA TEISTERDLG QCDRFKPIRT GISPLALIKG MTRPLSTLIS SSQSCQYTLD AKRKHVAEAI CKEQHLFLPF SYKNKYGMVA QVTQTLKLED TPKINSRFFG EGTKKMGLAF ESTKSTSPPK QAEAVLKTLQ ELKKLTISEQ NIQRANLFNK LVTELRGLSD EAVTSLLPQL IEVSSPITLQ ALVQCGQPQC STHILQWLKR VHANPLLIDV VTYLVALIPE PSAQQLREIF NMARDQRSRA TLYALSHAVN NYHKTNPTGT QELLDIANYL MEQIQDDCTG DEDYTYLILR VIGNMGQTME QLTPELKSSI LKCVQSTKPS LMIQKAAIQA LRKMEPKDKD QEVLLQTFLD DASPGDKRLA AYLMLMRSPS QADINKIVQI LPWEQNEQVK NFVASHIANI LNSEELDIQD LKKLVKEALK ESQLPTVMDF RKFSRNYQLY KSVSLPSLDP ASAKIEGNLI FDPNNYLPKE SMLKTTLTAF GFASADLIEI GLEGKGFEPT LEALFGKQGF FPDSVNKALY WVNGQVPDGV SKVLVDHFGY TKDDKHEQDM VNGIMLSVEK LIKDLKSKEV PEARAYLRIL GEELGFASLH DLQLLGKLLL MGARTLQGIP QMIGEVIRKG SKNDFFLHYI FMENAFELPT GAGLQLQISS SGVIAPGAKA GVKLEVANMQ AELVAKPSVS VEFVTNMGII IPDFARSGVQ MNTNFFHESG LEAHVALKAG KLKFIIPSPK RPVKLLSGGN TLHLVSTTKT EVIPPLIENR QSWSVCKQVF PGLNYCTSGA YSNASSTDSA SYYPLTGDTR LELELRPTGE IEQYSVSATY ELQREDRALV DTLKFVTQAE GAKQTEATMT FKYNRQSMTL SSEVQIPDFD VDLGTILRVN DESTEGKTSY RLTLDIQNKK ITEVALMGHL SCDTKEERKI KGVISIPRLQ AEARSEILAH WSPAKLLLQM DSSATAYGST VSKRVAWHYD EEKIEFEWNT GTNVDTKKMT SNFPVDLSDY PKSLHMYANR LLDHRVPQTD MTFRHVGSKL IVAMSSWLQK ASGSLPYTQT LQDHLNSLKE FNLQNMGLPD FHIPENLFLK SDGRVKYTLN KNSLKIEIPL PFGGKSSRDL KMLETVRTPA LHFKSVGFHL PSREFQVPTF TIPKLYQLQV PLLGVLDLST NVYSNLYNWS ASYSGGNTST DHFSLRARYH MKADSVVDLL SYNVQGSGET TYDHKNTFTL SCDGSLRHKF LDSNIKFSHV EKLGNNPVSK GLLIFDASSS WGPQMSASVH LDSKKKQHLF VKEVKIDGQF RVSSFYAKGT YGLSCQRDPN TGRLNGESNL RFNSSYLQGT NQITGRYEDG TLSLTSTSDL QSGIIKNTAS LKYENYELTL KSDTNGKYKN FATSNKMDMT FSKQNALLRS EYQADYESLR FFSLLSGSLN SHGLELNADI LGTDKINSGA HKATLRIGQD GISTSATTNL KCSLLVLENE LNAELGLSGA SMKLTTNGRF REHNAKFSLD GKAALTELSL GSAYQAMILG VDSKNIFNFK VSQEGLKLSN DMMGSYAEMK FDHTNSLNIA GLSLDFSSKL DNIYSSDKFY KQTVNLQLQP YSLVTTLNSD LKYNALDLTN NGKLRLEPLK LHVAGNLKGA YQNNEIKHIY AISSAALSAS YKADTVAKVQ GVEFSHRLNT DIAGLASAID MSTNYNSDSL HFSNVFRSVM APFTMTIDAH TNGNGKLALW GEHTGQLYSK FLLKAEPLAF TFSHDYKGST SHHLVSRKSI SAALEHKVSA LLTPAEQTGT WKLKTQFNNN EYSQDLDAYN TKDKIGVELT GRTLADLTLL DSPIKVPLLL SEPINIIDAL EMRDAVEKPQ EFTIVAFVKY DKNQDVHSIN LPFFETLQEY FERNRQTIIV VLENVQRNLK HINIDQFVRK YRAALGKLPQ QANDYLNSFN WERQVSHAKE KLTALTKKYR ITENDIQIAL DDAKINFNEK LSQLQTYMIQ FDQYIKDSYD LHDLKIAIAN IIDEIIEKLK SLDEHYHIRV NLVKTIHDLH LFIENIDFNK SGSSTASWIQ NVDTKYQIRI QIQEKLQQLK RHIQNIDIQH LAGKLKQHIE AIDVRVLLDQ LGTTISFERI NDILEHVKHF VINLIGDFEV AEKINAFRAK VHELIERYEV DQQIQVLMDK LVELAHQYKL KETIQKLSNV LQQVKIKDYF EKLVGFIDDA VKKLNELSFK TFIEDVNKFL DMLIKKLKSF DYHQFVDETN DKIREVTQRL NGEIQALELP QKAEALKLFL EETKATVAVY LESLQDTKIT LIINWLQEAL SSASLAHMKA KFRETLEDTR DRMYQMDIQQ ELQRYLSLVG QVYSTLVTYI SDWWTLAAKN LTDFAEQYSI QDWAKRMKAL VEQGFTVPEI KTILGTMPAF EVSLQALQKA TFQTPDFIVP LTDLRIPSVQ INFKDLKNIK IPSRFSTPEF TILNTFHIPS FTIDFVEMKV KIIRTIDQML NSELQWPVPD IYLRDLKVED IPLARITLPD FRLPEIAIPE FIIPTLNLND FQVPDLHIPE FQLPHISHTI EVPTFGKLYS ILKIQSPLFT LDANADIGNG TTSANEAGIA ASITAKGESK LEVLNFDFQA NAQLSNPKIN PLALKESVKF SSKYLRTEHG SEMLFFGNAI EGKSNTVASL HTEKNTLELS NGVIVKINNQ LTLDSNTKYF HKLNIPKLDF SSQADLRNEI KTLLKAGHIA WTSSGKGSWK WACPRFSDEG THESQISFTI EGPLTSFGLS NKINSKHLRV NQNLVYESGS LNFSKLEIQS QVDSQHVGHS VLTAKGMALF GEGKAEFTGR HDAHLNGKVI GTLKNSLFFS AQPFEITAST NNEGNLKVRF PLRLTGKIDF LNNYALFLSP SAQQASWQVS ARFNQYKYNQ NFSAGNNENI MEAHVGINGE ANLDFLNIPL TIPEMRLPYT IITTPPLKDF SLWEKTGLKE FLKTTKQSFD LSVKAQYKKN KHRHSITNPL AVLCEFISQS IKSFDRHFEK NRNNALDFVT KSYNETKIKF DKYKAEKSHD ELPRTFQIPG YTVPVVNVEV SPFTIEMSAF GYVFPKAVSM PSFSILGSDV RVPSYTLILP SLELPVLHVP RNLKLSLPDF KELCTISHIF IPAMGNITYD FSFKSSVITL NTNAELFNQS DIVAHLLSSS SSVIDALQYK LEGTTRLTRK RGLKLATALS LSNKFVEGSH NSTVSLTTKN MEVSVATTTK AQIPILRMNF KQELNGNTKS KPTVSSSMEF KYDFNSSMLY STAKGAVDHK LSLESLTSYF SIESSTKGDV KGSVLSREYS GTIASEANTY LNSKSTRSSV KLQGTSKIDD IWNLEVKENF AGEATLQRIY SLWEHSTKNH LQLEGLFFTN GEHTSKATLE LSPWQMSALV QVHASQPSSF HDFPDLGQEV ALNANTKNQK IRWKNEVRIH SGSFQSQVEL SNDQEKAHLD IAGSLEGHLR FLKNIILPVY DKSLWDFLKL DVTTSIGRRQ HLRVSTAFVY TKNPNGYSFS IPVKVLADKF IIPGLKLNDL NSVLVMPTFH VPFTDLQVPS CKLDFREIQI YKKLRTSSFA LNLPTLPEVK FPEVDVLTKY SQPEDSLIPF FEITVPESQL TVSQFTLPKS VSDGIAALDL NAVANKIADF ELPTIIVPEQ TIEIPSIKFS VPAGIVIPSF QALTARFEVD SPVYNATWSA SLKNKADYVE TVLDSTCSST VQFLEYELNV LGTHKIEDGT LASKTKGTFA HRDFSAEYEE DGKYEGLQEW EGKAHLNIKS PAFTDLHLRY QKDKKGISTS AASPAVGTVG MDMDEDDDFS KWNFYYSPQS SPDKKLTIFK TELRVRESDE ETQIKVNWEE EAASGLLTSL KDNVPKATGV LYDYVNKYHW EHTGLTLREV SSKLRRNLQN NAEWVYQGAI RQIDDIDVRF QKAASGTTGT YQEWKDKAQN LYQELLTQEG QASFQGLKDN VFDGLVRVTQ EFHMKVKHLI DSLIDFLNFP RFQFPGKPGI YTREELCTMF IREVGTVLSQ VYSKVHNGSE ILFSYFQDLV ITLPFELRKH KLIDVISMYR ELLKDLSKEA QEVFKAIQSL KTTEVLRNLQ DLLQFIFQLI EDNIKQLKEM KFTYLINYIQ DEINTIFSDY IPYVFKLLKE NLCLNLHKFN EFIQNELQEA SQELQQIHQY IMALREEYFD PSIVGWTVKY YELEEKIVSL IKNLLVALKD FHSEYIVSAS NFTSQLSSQV EQFLHRNIQE YLSILTDPDG KGKEKIAELS ATAQEIIKSQ AIATKKIISD YHQQFRYKLQ DFSDQLSDYY EKFIAESKRL IDLSIQNYHT FLIYITELLK KLQSTTVMNP YMKLAPGELT IIL //