APOA4_MOUSE
ID APOA4_MOUSE Reviewed; 395 AA.
AC P06728; Q91XF8;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 178.
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 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].
RX PubMed=3796595; DOI=10.1128/mcb.6.11.3807-3814.1986;
RA Williams S.C., Bruckheimer S.M., Lusis A.J., LeBoeuf R.C., Kinniburgh A.J.;
RT "Mouse apolipoprotein A-IV gene: nucleotide sequence and induction by a
RT high-lipid diet.";
RL Mol. Cell. Biol. 6:3807-3814(1986).
RN [2]
RP SEQUENCE REVISION.
RA Kinniburgh A.J.;
RL Submitted (DEC-1986) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND POLYMORPHISM.
RC STRAIN=129/J, and C57BL/6J;
RX PubMed=1648102; DOI=10.1016/s0021-9258(18)98958-1;
RA Reue K., Leete T.H.;
RT "Genetic variation in mouse apolipoprotein A-IV due to insertion and
RT deletion in a region of tandem repeats.";
RL J. Biol. Chem. 266:12715-12721(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion;
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].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 52-97; 155-163; 193-204; 222-233 AND 306-326, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
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: 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:0000250|UniProtKB:P06727}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Secreted 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 -!- POLYMORPHISM: There is a polymorphism within a series of imperfect
CC repeats encoding the sequence E-Q-[AV]-Q. Insertions or deletions of 12
CC nucleotides have given rise to three forms characterized by three
CC (129), four (C57BL/6), or five (M.castaneus) copies of the repeat unit.
CC {ECO:0000269|PubMed:1648102}.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; M13966; AAA37253.1; -; Genomic_DNA.
DR EMBL; M64248; AAA37214.1; -; mRNA.
DR EMBL; M64249; AAA37215.1; -; mRNA.
DR EMBL; AK161535; BAE36447.1; -; mRNA.
DR EMBL; AK168687; BAE40533.1; -; mRNA.
DR EMBL; CH466522; EDL25684.1; -; Genomic_DNA.
DR EMBL; BC010769; AAH10769.1; -; mRNA.
DR CCDS; CCDS23142.1; -.
DR PIR; A25281; A25281.
DR PIR; A40892; A40892.
DR PIR; B40892; B40892.
DR RefSeq; NP_031494.2; NM_007468.2.
DR AlphaFoldDB; P06728; -.
DR SMR; P06728; -.
DR BioGRID; 198157; 2.
DR IntAct; P06728; 1.
DR STRING; 10090.ENSMUSP00000034585; -.
DR iPTMnet; P06728; -.
DR PhosphoSitePlus; P06728; -.
DR CPTAC; non-CPTAC-3411; -.
DR jPOST; P06728; -.
DR MaxQB; P06728; -.
DR PaxDb; P06728; -.
DR PeptideAtlas; P06728; -.
DR PRIDE; P06728; -.
DR ProteomicsDB; 296335; -.
DR Antibodypedia; 18421; 494 antibodies from 37 providers.
DR DNASU; 11808; -.
DR Ensembl; ENSMUST00000034585; ENSMUSP00000034585; ENSMUSG00000032080.
DR GeneID; 11808; -.
DR KEGG; mmu:11808; -.
DR UCSC; uc009phd.1; mouse.
DR CTD; 337; -.
DR MGI; MGI:88051; Apoa4.
DR VEuPathDB; HostDB:ENSMUSG00000032080; -.
DR eggNOG; ENOG502QSC5; Eukaryota.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_058447_0_0_1; -.
DR InParanoid; P06728; -.
DR OMA; KGHLTPY; -.
DR OrthoDB; 1299087at2759; -.
DR TreeFam; TF334458; -.
DR Reactome; R-MMU-8963888; Chylomicron assembly.
DR Reactome; R-MMU-8963901; Chylomicron remodeling.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 11808; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Apoa4; mouse.
DR PRO; PR:P06728; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P06728; protein.
DR Bgee; ENSMUSG00000032080; Expressed in small intestine Peyer's patch and 71 other tissues.
DR Genevisible; P06728; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0042627; C:chylomicron; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0016209; F:antioxidant activity; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0120020; F:cholesterol transfer activity; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:MGI.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:MGI.
DR GO; GO:0002227; P:innate immune response in mucosa; IMP:BHF-UCL.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0016042; P:lipid catabolic process; ISO:MGI.
DR GO; GO:0055088; P:lipid homeostasis; ISO:MGI.
DR GO; GO:0006869; P:lipid transport; ISO:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0034445; P:negative regulation of plasma lipoprotein oxidation; ISO:MGI.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEA:Ensembl.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISO:MGI.
DR GO; GO:0033700; P:phospholipid efflux; ISO:MGI.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; IBA:GO_Central.
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; 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; ISO:MGI.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISO:MGI.
DR GO; GO:0065005; P:protein-lipid complex assembly; ISO:MGI.
DR GO; GO:0032374; P:regulation of cholesterol transport; ISO:MGI.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IMP:MGI.
DR GO; GO:0019430; P:removal of superoxide radicals; ISO:MGI.
DR GO; GO:0006982; P:response to lipid hydroperoxide; ISO:MGI.
DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
DR GO; GO:0034014; P:response to triglyceride; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:MGI.
DR GO; GO:0070328; P:triglyceride homeostasis; IBA:GO_Central.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; ISO:MGI.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 3.
PE 1: Evidence at protein level;
KW Chylomicron; Direct protein sequencing; HDL; Lipid transport;
KW Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..20
FT CHAIN 21..395
FT /note="Apolipoprotein A-IV"
FT /id="PRO_0000001977"
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 356..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 382..385
FT /note="Missing (in strain: various strains)"
FT CONFLICT 15
FT /note="Missing (in Ref. 1; AAA37253)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="Q -> K (in Ref. 1; AAA37253)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="Q -> K (in Ref. 1; AAA37253 and 3; AAA37214/
FT AAA37215)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> R (in Ref. 1; AAA37253)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="S -> A (in Ref. 1; AAA37253)"
FT /evidence="ECO:0000305"
FT CONFLICT 294..295
FT /note="RQ -> KA (in Ref. 1; AAA37253)"
FT /evidence="ECO:0000305"
FT CONFLICT 315..316
FT /note="NK -> GG (in Ref. 1; AAA37253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 45029 MW; C48BE32EED441F71 CRC64;
MFLKAAVLTL ALVAITGTRA EVTSDQVANV VWDYFTQLSN NAKEAVEQFQ KTDVTQQLST
LFQDKLGDAS TYADGVHNKL VPFVVQLSGH LAQETERVKE EIKKELEDLR DRMMPHANKV
TQTFGENMQK LQEHLKPYAV DLQDQINTQT QEMKLQLTPY IQRMQTTIKE NVDNLHTSMM
PLATNLKDKF NRNMEELKGH LTPRANELKA TIDQNLEDLR RSLAPLTVGV QEKLNHQMEG
LAFQMKKNAE ELQTKVSAKI DQLQKNLAPL VEDVQSKVKG NTEGLQKSLE DLNRQLEQQV
EEFRRTVEPM GEMFNKALVQ QLEQFRQQLG PNSGEVESHL SFLEKSLREK VNSFMSTLEK
KGSPDQPQAL PLPEQAQEQA QEQAQEQVQP KPLES
