APOC3_MOUSE
ID APOC3_MOUSE Reviewed; 99 AA.
AC P33622; Q8VC58; Q9CPP9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Apolipoprotein C-III;
DE Short=Apo-CIII;
DE Short=ApoC-III;
DE AltName: Full=Apolipoprotein C3;
DE Flags: Precursor;
GN Name=Apoc3;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Small intestine;
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 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 PROTEIN SEQUENCE OF 42-68, MASS SPECTROMETRY, AND OXIDATION AT MET-63.
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 [5]
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: Component of triglyceride-rich very low density lipoproteins
CC (VLDL) and high density lipoproteins (HDL) in plasma. Plays a
CC multifaceted role in triglyceride homeostasis. Intracellularly,
CC promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and
CC secretion; extracellularly, attenuates hydrolysis and clearance of
CC triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by
CC inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant
CC receptors. Formed of several curved helices connected via semiflexible
CC hinges, so that it can wrap tightly around the curved micelle surface
CC and easily adapt to the different diameters of its natural binding
CC partners. {ECO:0000250|UniProtKB:P02656}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02656}.
CC -!- PTM: The most abundant glycoforms are characterized by an O-linked
CC disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc),
CC further modified with up to 3 sialic acid residues. Less abundant
CC glycoforms are characterized by more complex and fucosylated glycan
CC moieties. O-glycosylated on Thr-94 with a core 1 or possibly core 8
CC glycan. {ECO:0000250|UniProtKB:P02656}.
CC -!- MASS SPECTROMETRY: Mass=8830.5; Mass_error=0.354; Method=Electrospray;
CC Note=Strain C57BL/6. Without methionine sulfoxide.;
CC Evidence={ECO:0000269|PubMed:16876491};
CC -!- MASS SPECTROMETRY: Mass=8891.4; Method=Electrospray; Note=Strain
CC BALB/c. Without methionine sulfoxide.;
CC Evidence={ECO:0000269|PubMed:16876491};
CC -!- SIMILARITY: Belongs to the apolipoprotein C3 family. {ECO:0000305}.
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DR EMBL; L04149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L04150; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK002908; BAB22448.1; -; mRNA.
DR EMBL; AK008260; BAB25563.1; -; mRNA.
DR EMBL; BC021776; AAH21776.1; -; mRNA.
DR CCDS; CCDS23141.1; -.
DR PIR; B44364; B44364.
DR RefSeq; NP_001276685.1; NM_001289756.1.
DR RefSeq; NP_075603.1; NM_023114.4.
DR AlphaFoldDB; P33622; -.
DR SMR; P33622; -.
DR STRING; 10090.ENSMUSP00000034586; -.
DR GlyGen; P33622; 1 site.
DR iPTMnet; P33622; -.
DR PhosphoSitePlus; P33622; -.
DR CPTAC; non-CPTAC-4017; -.
DR jPOST; P33622; -.
DR MaxQB; P33622; -.
DR PaxDb; P33622; -.
DR PeptideAtlas; P33622; -.
DR PRIDE; P33622; -.
DR ProteomicsDB; 281829; -.
DR DNASU; 11814; -.
DR GeneID; 11814; -.
DR KEGG; mmu:11814; -.
DR UCSC; uc033jkf.1; mouse.
DR CTD; 345; -.
DR MGI; MGI:88055; Apoc3.
DR eggNOG; ENOG502SZ00; Eukaryota.
DR InParanoid; P33622; -.
DR PhylomeDB; P33622; -.
DR TreeFam; TF338209; -.
DR Reactome; R-MMU-8963888; Chylomicron assembly.
DR Reactome; R-MMU-8963901; Chylomicron remodeling.
DR Reactome; R-MMU-8964058; HDL remodeling.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 11814; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Apoc3; mouse.
DR PRO; PR:P33622; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P33622; protein.
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; ISO:MGI.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; 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:0030234; F:enzyme regulator activity; ISO:MGI.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0055102; F:lipase inhibitor activity; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0034382; P:chylomicron remnant clearance; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR GO; GO:0042953; P:lipoprotein transport; ISO:MGI.
DR GO; GO:0060621; P:negative regulation of cholesterol import; ISO:MGI.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0010987; P:negative regulation of high-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; ISO:MGI.
DR GO; GO:0045833; P:negative regulation of lipid metabolic process; ISO:MGI.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; ISO:MGI.
DR GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; ISO:MGI.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0010897; P:negative regulation of triglyceride catabolic process; ISO:MGI.
DR GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0033700; P:phospholipid efflux; ISO:MGI.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISO:MGI.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
DR GO; GO:0019433; P:triglyceride catabolic process; IMP:MGI.
DR GO; GO:0070328; P:triglyceride homeostasis; ISO:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
DR GO; GO:0006642; P:triglyceride mobilization; IMP:MGI.
DR Gene3D; 6.10.90.10; -; 1.
DR InterPro; IPR008403; Apo-CIII.
DR InterPro; IPR038195; Apo_CIII_sf.
DR PANTHER; PTHR14225; PTHR14225; 1.
DR Pfam; PF05778; Apo-CIII; 1.
PE 1: Evidence at protein level;
KW Chylomicron; Direct protein sequencing; Glycoprotein; Lipid degradation;
KW Lipid metabolism; Lipid transport; Oxidation; Reference proteome; Secreted;
KW Sialic acid; Signal; Transport; VLDL.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..99
FT /note="Apolipoprotein C-III"
FT /id="PRO_0000002033"
FT REGION 68..99
FT /note="Lipid-binding"
FT /evidence="ECO:0000250"
FT SITE 41
FT /note="May interact with the LDL receptor"
FT /evidence="ECO:0000250|UniProtKB:P02656"
FT MOD_RES 63
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:16876491"
FT CARBOHYD 94
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02656"
FT CONFLICT 57
FT /note="V -> A (in Ref. 1; L04150)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="F -> S (in Ref. 2; BAB22448/BAB25563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 99 AA; 10982 MW; BBC1690C055ADEC7 CRC64;
MQPRTLLTVA LLALLASARA EEVEGSLLLG SVQGYMEQAS KTVQDALSSV QESDIAVVAR
GWMDNHFRFL KGYWSKFTDK FTGFWDSNPE DQPTPAIES
