APOA5_MOUSE
ID APOA5_MOUSE Reviewed; 368 AA.
AC Q8C7G5; Q91X90; Q99P64;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Apolipoprotein A-V;
DE Short=Apo-AV;
DE Short=ApoA-V;
DE AltName: Full=Apolipoprotein A5;
DE AltName: Full=Regeneration-associated protein 3;
DE Flags: Precursor;
GN Name=Apoa5; Synonyms=Rap3;
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 [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=11577099; DOI=10.1074/jbc.m106888200;
RA van Der Vliet H.N., Sammels M.G., Leegwater A.C.J., Levels J.H.M.,
RA Reitsma P.H., Boers W., Chamuleau R.A.F.M.;
RT "Apolipoprotein A-V. A novel apolipoprotein associated with an early phase
RT of liver regeneration.";
RL J. Biol. Chem. 276:44512-44520(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [3]
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 [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11588264; DOI=10.1126/science.1064852;
RA Pennacchio L.A., Olivier M., Hubacek J.A., Cohen J.C., Cox D.R.,
RA Fruchart J.-C., Krauss R.M., Rubin E.M.;
RT "An apolipoprotein influencing triglycerides in humans and mice revealed by
RT comparative sequencing.";
RL Science 294:169-173(2001).
RN [5]
RP FUNCTION.
RX PubMed=15090553; DOI=10.1074/jbc.m403240200;
RA Schaap F.G., Rensen P.C.N., Voshol P.J., Vrins C., van der Vliet H.N.,
RA Chamuleau R.A.F.M., Havekes L.M., Groen A.K., van Dijk K.W.;
RT "ApoAV reduces plasma triglycerides by inhibiting very low density
RT lipoprotein-triglyceride (VLDL-TG) production and stimulating lipoprotein
RT lipase-mediated VLDL-TG hydrolysis.";
RL J. Biol. Chem. 279:27941-27947(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Lung;
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: Minor apolipoprotein mainly associated with HDL and to a
CC lesser extent with VLDL. May also be associated with chylomicrons.
CC Important determinant of plasma triglyceride (TG) levels by both being
CC a potent stimulator of apo-CII lipoprotein lipase (LPL) TG hydrolysis
CC and an inhibitor of the hepatic VLDL-TG production rate (without
CC affecting the VLDL-apoB production rate). Activates poorly
CC lecithin:cholesterol acyltransferase (LCAT) and does not enhance efflux
CC of cholesterol from macrophages (By similarity). Binds heparin (By
CC similarity). {ECO:0000250|UniProtKB:Q6Q788,
CC ECO:0000269|PubMed:11588264, ECO:0000269|PubMed:15090553}.
CC -!- SUBUNIT: Interacts with GPIHBP1 (By similarity). Interacts with SORL1;
CC this interaction leads to APOA5 internalization and sorting either to
CC lysosomes and degradation, or to the trans-Golgi network (By
CC similarity). {ECO:0000250|UniProtKB:Q6Q788}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11577099}. Early
CC endosome {ECO:0000250|UniProtKB:Q6Q788}. Late endosome
CC {ECO:0000250|UniProtKB:Q6Q788}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q6Q788}. Note=In the presence of SORL1,
CC internalized to early endosomes, sorted in a retrograde fashion to late
CC endosomes, from which a portion is sent to lysosomes and degradation,
CC another portion is sorted to the trans-Golgi network.
CC {ECO:0000250|UniProtKB:Q6Q788}.
CC -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:11577099,
CC ECO:0000269|PubMed:11588264}.
CC -!- INDUCTION: Induced in early phase of liver regeneration.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:Q6Q788}.
CC -!- MISCELLANEOUS: Mice expressing the human APOAV transgene show a
CC decrease in plasma TG by one third. Conversely, knockout mice lacking
CC APOAV have a four time increase in plasma TG.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; AF327059; AAG49600.1; -; mRNA.
DR EMBL; AK050280; BAC34163.1; -; mRNA.
DR EMBL; BC011198; AAH11198.1; -; mRNA.
DR CCDS; CCDS23143.1; -.
DR RefSeq; NP_001335024.1; NM_001348095.1.
DR RefSeq; NP_536682.2; NM_080434.4.
DR RefSeq; XP_006510601.1; XM_006510538.3.
DR AlphaFoldDB; Q8C7G5; -.
DR SMR; Q8C7G5; -.
DR STRING; 10090.ENSMUSP00000113413; -.
DR iPTMnet; Q8C7G5; -.
DR PhosphoSitePlus; Q8C7G5; -.
DR CPTAC; non-CPTAC-3559; -.
DR jPOST; Q8C7G5; -.
DR MaxQB; Q8C7G5; -.
DR PaxDb; Q8C7G5; -.
DR PeptideAtlas; Q8C7G5; -.
DR PRIDE; Q8C7G5; -.
DR ProteomicsDB; 296336; -.
DR Antibodypedia; 32277; 773 antibodies from 33 providers.
DR DNASU; 66113; -.
DR Ensembl; ENSMUST00000034584; ENSMUSP00000034584; ENSMUSG00000032079.
DR Ensembl; ENSMUST00000121598; ENSMUSP00000113413; ENSMUSG00000032079.
DR GeneID; 66113; -.
DR KEGG; mmu:66113; -.
DR UCSC; uc009phf.1; mouse.
DR CTD; 116519; -.
DR MGI; MGI:1913363; Apoa5.
DR VEuPathDB; HostDB:ENSMUSG00000032079; -.
DR eggNOG; ENOG502S33P; Eukaryota.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_747959_0_0_1; -.
DR InParanoid; Q8C7G5; -.
DR OMA; AFRQDTF; -.
DR OrthoDB; 813395at2759; -.
DR PhylomeDB; Q8C7G5; -.
DR TreeFam; TF334458; -.
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-8963901; Chylomicron remodeling.
DR BioGRID-ORCS; 66113; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Apoa5; mouse.
DR PRO; PR:Q8C7G5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8C7G5; protein.
DR Bgee; ENSMUSG00000032079; Expressed in left lobe of liver and 41 other tissues.
DR ExpressionAtlas; Q8C7G5; baseline and differential.
DR Genevisible; Q8C7G5; MM.
DR GO; GO:0042627; C:chylomicron; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0060229; F:lipase activator activity; ISO:MGI.
DR GO; GO:0035473; F:lipase binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0060230; F:lipoprotein lipase activator activity; ISO:MGI.
DR GO; GO:0070325; F:lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0055090; P:acylglycerol homeostasis; IMP:BHF-UCL.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; ISO:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
DR GO; GO:0033700; P:phospholipid efflux; IBA:GO_Central.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; IBA:GO_Central.
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:0050996; P:positive regulation of lipid catabolic process; ISO:MGI.
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:0010902; P:positive regulation of very-low-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IBA:GO_Central.
DR GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
DR GO; GO:0019433; P:triglyceride catabolic process; ISO:MGI.
DR GO; GO:0070328; P:triglyceride homeostasis; ISO:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
DR GO; GO:0034370; P:triglyceride-rich lipoprotein particle remodeling; IMP:MGI.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IBA:GO_Central.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 1.
PE 1: Evidence at protein level;
KW Chylomicron; Coiled coil; Endosome; Golgi apparatus; HDL; Lipid transport;
KW Phosphoprotein; Reference proteome; Secreted; Signal; Transport; VLDL.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..368
FT /note="Apolipoprotein A-V"
FT /id="PRO_0000001982"
FT REGION 305..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 231..255
FT /evidence="ECO:0000255"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 86
FT /note="G -> D (in Ref. 1; AAG49600)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..179
FT /note="HT -> QA (in Ref. 3; AAH11198)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="V -> L (in Ref. 3; AAH11198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 41262 MW; B5B2F1982C47475B CRC64;
MAAVITWALA LLAVFASTQA RKSLWDYFSQ NSWSKGVMGQ PQKLAQENLK GSFEQDLYNM
NNYLEKLGPL RGPGKEPPLL AQDPEGIRKQ LQQELGEVSS RLEPYMAAKH QQVGWNLEGL
RQQLKPYTAE LMEQVGLSVQ ELQEQLRVVG EDTKAQLLGG VDEALNLLQD MQSRVLHHTD
RVKELFHPYA ERLVTGIGHH VQELHRSVAP HAAASPARLS RCVQTLSHKL TRKAKDLHTS
IQRNLDQLRD ELSAFIRVST DGAEDGDSLD PQALSEEVRQ RLQAFRHDTY LQIAAFTQAI
DQETEEIQHQ LAPPPPSHSA FAPELGHSDS NKALSRLQSR LDDLWEDIAY GLQDQGHSHL
SDPEGHSG
