APOA1_MOUSE
ID APOA1_MOUSE Reviewed; 264 AA.
AC Q00623; O08855; O09042; Q8BPD5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Apolipoprotein A-I;
DE Short=Apo-AI;
DE Short=ApoA-I;
DE AltName: Full=Apolipoprotein A1;
DE Contains:
DE RecName: Full=Proapolipoprotein A-I;
DE Short=ProapoA-I;
DE Contains:
DE RecName: Full=Truncated apolipoprotein A-I;
DE Flags: Precursor;
GN Name=Apoa1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1596360; DOI=10.1515/bchm3.1992.373.1.187;
RA Stoffel W., Mueller R., Binczek E., Hofmann K.;
RT "Mouse apolipoprotein AI. cDNA-derived primary structure, gene organisation
RT and complete nucleotide sequence.";
RL Biol. Chem. Hoppe-Seyler 373:187-193(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1478650; DOI=10.1016/s0888-7543(05)80133-8;
RA Januzzi J.L., Azrolan N., O'Connell A., Aalto-Setala K., Breslow J.L.;
RT "Characterization of the mouse apolipoprotein Apoa-1/Apoc-3 gene locus:
RT genomic, mRNA, and protein sequences with comparisons to other species.";
RL Genomics 14:1081-1088(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT 249-LYS-ALA-250.
RC STRAIN=BALB/cJ, C3H/HeJ, C57BL/6J, and ICR; TISSUE=Spleen;
RA Chiang A.-N., Fan K.-C., Shaw G.-C., Yang U.-C.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT 249-GLN-VAL-250.
RC STRAIN=C57BL/6J; TISSUE=Liver, Ovary, Placenta, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT 249-GLN-VAL-250.
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 19-46; 93-106; 120-129; 131-139; 142-154; 157-172;
RP 177-194; 201-216 AND 223-256, MASS SPECTROMETRY, AND OXIDATION AT MET-193;
RP MET-240 AND MET-242.
RX PubMed=16876491; DOI=10.1016/j.bbapap.2006.06.001;
RA Puppione D.L., Yam L.M., Bassilian S., Souda P., Castellani L.W.,
RA Schumaker V.N., Whitelegge J.P.;
RT "Mass spectral analysis of the apolipoproteins on mouse high density
RT lipoproteins. Detection of post-translational modifications.";
RL Biochim. Biophys. Acta 1764:1363-1371(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Participates in the reverse transport of cholesterol from
CC tissues to the liver for excretion by promoting cholesterol efflux from
CC tissues and by acting as a cofactor for the lecithin cholesterol
CC acyltransferase (LCAT). As part of the SPAP complex, activates
CC spermatozoa motility.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with APOA1BP and CLU.
CC Component of a sperm activating protein complex (SPAP), consisting of
CC APOA1, an immunoglobulin heavy chain, an immunoglobulin light chain and
CC albumin. Interacts with NDRG1. Interacts with SCGB3A2 (By similarity).
CC Interacts with NAXE and YJEFN3 (By similarity).
CC {ECO:0000250|UniProtKB:G5BQH5, ECO:0000250|UniProtKB:P02647,
CC ECO:0000250|UniProtKB:P04639}.
CC -!- INTERACTION:
CC Q00623; Q08460: Kcnma1; NbExp=4; IntAct=EBI-1634106, EBI-1633915;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Major protein of plasma HDL, also found in
CC chylomicrons.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000250}.
CC -!- PTM: May be acylated.
CC -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC {ECO:0000250}.
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-I]: Mass=27951.3;
CC Mass_error=1.343; Method=Electrospray; Note=Strain C57BL/6. Without
CC methionine sulfoxide.; Evidence={ECO:0000269|PubMed:16876491};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-I]: Mass=27923.8;
CC Method=Electrospray; Note=Strain BALB/c. Without methionine sulfoxide.;
CC Evidence={ECO:0000269|PubMed:16876491};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-I]: Mass=27965;
CC Method=Electrospray; Note=Strain C57BL/6. With 1 methionine sulfoxide.;
CC Evidence={ECO:0000269|PubMed:16876491};
CC -!- MASS SPECTROMETRY: [Proapolipoprotein A-I]: Mass=28819.7;
CC Method=Electrospray; Note=Strain C57BL/6. Without methionine
CC sulfoxide.; Evidence={ECO:0000269|PubMed:16876491};
CC -!- MASS SPECTROMETRY: [Proapolipoprotein A-I]: Mass=28790.7;
CC Method=Electrospray; Note=Strain BALB/c. Without methionine sulfoxide.;
CC Evidence={ECO:0000269|PubMed:16876491};
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; X64262; CAA45560.1; -; mRNA.
DR EMBL; X64263; CAA45561.1; -; Genomic_DNA.
DR EMBL; L04149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L04151; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U79572; AAB58424.1; -; Genomic_DNA.
DR EMBL; U79574; AAB58426.1; -; Genomic_DNA.
DR EMBL; U79573; AAB58425.1; -; Genomic_DNA.
DR EMBL; U79575; AAB58427.1; -; Genomic_DNA.
DR EMBL; AK076187; BAC36241.1; -; mRNA.
DR EMBL; AK149576; BAE28968.1; -; mRNA.
DR EMBL; AK161536; BAE36448.1; -; mRNA.
DR EMBL; AC116503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012253; AAH12253.1; -; mRNA.
DR EMBL; BC019837; AAH19837.1; -; mRNA.
DR CCDS; CCDS40610.1; -.
DR PIR; S22420; S22420.
DR RefSeq; NP_033822.2; NM_009692.4.
DR PDB; 2LEM; NMR; -; A=25-240.
DR PDBsum; 2LEM; -.
DR AlphaFoldDB; Q00623; -.
DR SASBDB; Q00623; -.
DR SMR; Q00623; -.
DR BioGRID; 198155; 30.
DR CORUM; Q00623; -.
DR IntAct; Q00623; 3.
DR STRING; 10090.ENSMUSP00000034588; -.
DR iPTMnet; Q00623; -.
DR PhosphoSitePlus; Q00623; -.
DR REPRODUCTION-2DPAGE; IPI00121209; -.
DR REPRODUCTION-2DPAGE; Q00623; -.
DR SWISS-2DPAGE; Q00623; -.
DR CPTAC; non-CPTAC-3892; -.
DR jPOST; Q00623; -.
DR PaxDb; Q00623; -.
DR PeptideAtlas; Q00623; -.
DR PRIDE; Q00623; -.
DR ProteomicsDB; 281800; -.
DR Antibodypedia; 32291; 1593 antibodies from 48 providers.
DR DNASU; 11806; -.
DR Ensembl; ENSMUST00000034588; ENSMUSP00000034588; ENSMUSG00000032083.
DR GeneID; 11806; -.
DR KEGG; mmu:11806; -.
DR UCSC; uc009phb.3; mouse.
DR CTD; 335; -.
DR MGI; MGI:88049; Apoa1.
DR VEuPathDB; HostDB:ENSMUSG00000032083; -.
DR eggNOG; ENOG502S1XQ; Eukaryota.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_058447_1_0_1; -.
DR InParanoid; Q00623; -.
DR OMA; KEVREMW; -.
DR OrthoDB; 1553412at2759; -.
DR PhylomeDB; Q00623; -.
DR TreeFam; TF334458; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-MMU-2168880; Scavenging of heme from plasma.
DR Reactome; R-MMU-3000471; Scavenging by Class B Receptors.
DR Reactome; R-MMU-3000480; Scavenging by Class A Receptors.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR Reactome; R-MMU-8963888; Chylomicron assembly.
DR Reactome; R-MMU-8963896; HDL assembly.
DR Reactome; R-MMU-8963901; Chylomicron remodeling.
DR Reactome; R-MMU-8964011; HDL clearance.
DR Reactome; R-MMU-8964058; HDL remodeling.
DR Reactome; R-MMU-9707616; Heme signaling.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 11806; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Apoa1; mouse.
DR PRO; PR:Q00623; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q00623; protein.
DR Bgee; ENSMUSG00000032083; Expressed in left lobe of liver and 100 other tissues.
DR ExpressionAtlas; Q00623; baseline and differential.
DR Genevisible; Q00623; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0034365; C:discoidal high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; ISO:MGI.
DR GO; GO:0034362; C:low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0034191; F:apolipoprotein A-I receptor binding; ISO:MGI.
DR GO; GO:0034190; F:apolipoprotein receptor binding; ISO:MGI.
DR GO; GO:0045499; F:chemorepellent activity; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; ISO:MGI.
DR GO; GO:0120020; F:cholesterol transfer activity; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IDA:MGI.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0055102; F:lipase inhibitor activity; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IDA:MGI.
DR GO; GO:0005319; F:lipid transporter activity; IDA:MGI.
DR GO; GO:0071813; F:lipoprotein particle binding; IDA:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0030325; P:adrenal gland development; IMP:MGI.
DR GO; GO:0031100; P:animal organ regeneration; ISO:MGI.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:MGI.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IMP:MGI.
DR GO; GO:0033344; P:cholesterol efflux; IDA:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0070508; P:cholesterol import; ISO:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
DR GO; GO:0030301; P:cholesterol transport; IDA:MGI.
DR GO; GO:0001935; P:endothelial cell proliferation; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0008211; P:glucocorticoid metabolic process; IMP:MGI.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; ISO:MGI.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0019915; P:lipid storage; IMP:MGI.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IMP:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0050919; P:negative chemotaxis; ISO:MGI.
DR GO; GO:0060354; P:negative regulation of cell adhesion molecule production; ISO:MGI.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; ISO:MGI.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; IGI:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:MGI.
DR GO; GO:0060192; P:negative regulation of lipase activity; ISO:MGI.
DR GO; GO:0060761; P:negative regulation of response to cytokine stimulus; ISO:MGI.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0018206; P:peptidyl-methionine modification; ISS:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:MGI.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
DR GO; GO:0033700; P:phospholipid efflux; ISO:MGI.
DR GO; GO:0055091; P:phospholipid homeostasis; ISO:MGI.
DR GO; GO:0006644; P:phospholipid metabolic process; IMP:MGI.
DR GO; GO:0015914; P:phospholipid transport; ISO:MGI.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; IBA:GO_Central.
DR GO; GO:0090205; P:positive regulation of cholesterol metabolic process; ISO:MGI.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; ISO:MGI.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; ISO:MGI.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IBA:GO_Central.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:1902995; P:positive regulation of phospholipid efflux; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IBA:GO_Central.
DR GO; GO:0018158; P:protein oxidation; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:MGI.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IDA:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IDA:MGI.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:MGI.
DR GO; GO:0070328; P:triglyceride homeostasis; ISO:MGI.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IBA:GO_Central.
DR GO; GO:0051180; P:vitamin transport; ISO:MGI.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cholesterol metabolism; Direct protein sequencing;
KW Glycoprotein; HDL; Lipid metabolism; Lipid transport; Lipoprotein;
KW Oxidation; Palmitate; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal; Steroid metabolism; Sterol metabolism; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..264
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000425326"
FT CHAIN 25..264
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000001946"
FT CHAIN 25..263
FT /note="Truncated apolipoprotein A-I"
FT /evidence="ECO:0000250"
FT /id="PRO_0000416576"
FT REPEAT 67..88
FT /note="1"
FT REPEAT 89..110
FT /note="2"
FT REPEAT 111..121
FT /note="3; half-length"
FT REPEAT 122..143
FT /note="4"
FT REPEAT 144..165
FT /note="5"
FT REPEAT 166..187
FT /note="6"
FT REPEAT 188..207
FT /note="7; truncated"
FT REPEAT 208..229
FT /note="8"
FT REPEAT 230..240
FT /note="9; half-length"
FT REPEAT 241..264
FT /note="10"
FT REGION 67..264
FT /note="10 X approximate tandem repeats"
FT MOD_RES 109
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 193
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:16876491"
FT MOD_RES 240
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:16876491"
FT MOD_RES 242
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:16876491"
FT VARIANT 249..250
FT /note="QV -> KA (in strain: BALB/c, C3H and ICR)"
FT CONFLICT 143
FT /note="A -> G (in Ref. 3; AAB58424/AAB58425/AAB58426/
FT AAB58427)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="Missing (in Ref. 3; AAB58424/AAB58425/AAB58426/
FT AAB58427)"
FT /evidence="ECO:0000305"
FT HELIX 30..71
FT /evidence="ECO:0007829|PDB:2LEM"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:2LEM"
FT HELIX 83..119
FT /evidence="ECO:0007829|PDB:2LEM"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:2LEM"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:2LEM"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:2LEM"
FT HELIX 167..206
FT /evidence="ECO:0007829|PDB:2LEM"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2LEM"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:2LEM"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:2LEM"
SQ SEQUENCE 264 AA; 30616 MW; 5E33FF201963583B CRC64;
MKAVVLAVAL VFLTGSQAWH VWQQDEPQSQ WDKVKDFANV YVDAVKDSGR DYVSQFESSS
LGQQLNLNLL ENWDTLGSTV SQLQERLGPL TRDFWDNLEK ETDWVRQEMN KDLEEVKQKV
QPYLDEFQKK WKEDVELYRQ KVAPLGAELQ ESARQKLQEL QGRLSPVAEE FRDRMRTHVD
SLRTQLAPHS EQMRESLAQR LAELKSNPTL NEYHTRAKTH LKTLGEKARP ALEDLRHSLM
PMLETLKTQV QSVIDKASET LTAQ
