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APOC3_RAT
ID   APOC3_RAT               Reviewed;         101 AA.
AC   P06759;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 124.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=3020028; DOI=10.1016/s0021-9258(18)69300-7;
RA   Haddad I.A., Ordovas J.M., Fitzpatrick T., Karathanasis S.K.;
RT   "Linkage, evolution, and expression of the rat apolipoprotein A-I, C-III,
RT   and A-IV genes.";
RL   J. Biol. Chem. 261:13268-13277(1986).
RN   [2]
RP   SEQUENCE REVISION TO 60.
RA   Haddad I.A., Ordovas J.M., Fitzpatrick T., Karathanasis S.K.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
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   -!- TISSUE SPECIFICITY: Synthesized predominantly in liver and to a lesser
CC       degree in intestine. {ECO:0000269|PubMed:3020028}.
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-96 with a core 1 or possibly core 8
CC       glycan. {ECO:0000250|UniProtKB:P02656}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C3 family. {ECO:0000305}.
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DR   EMBL; J02596; AAA40746.1; -; Genomic_DNA.
DR   PIR; B24700; B24700.
DR   AlphaFoldDB; P06759; -.
DR   SMR; P06759; -.
DR   STRING; 10116.ENSRNOP00000067045; -.
DR   GlyGen; P06759; 1 site.
DR   iPTMnet; P06759; -.
DR   PhosphoSitePlus; P06759; -.
DR   PaxDb; P06759; -.
DR   PRIDE; P06759; -.
DR   RGD; 2136; Apoc3.
DR   eggNOG; ENOG502SZ00; Eukaryota.
DR   HOGENOM; CLU_154694_0_0_1; -.
DR   InParanoid; P06759; -.
DR   PhylomeDB; P06759; -.
DR   Reactome; R-RNO-8963888; Chylomicron assembly.
DR   Reactome; R-RNO-8963901; Chylomicron remodeling.
DR   Reactome; R-RNO-8964058; HDL remodeling.
DR   Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR   PRO; PR:P06759; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Genevisible; P06759; RN.
DR   GO; GO:0042627; C:chylomicron; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0034363; C:intermediate-density lipoprotein particle; ISO:RGD.
DR   GO; GO:0034366; C:spherical high-density lipoprotein particle; ISO:RGD.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:RGD.
DR   GO; GO:0030234; F:enzyme regulator activity; ISO:RGD.
DR   GO; GO:0070653; F:high-density lipoprotein particle receptor binding; ISO:RGD.
DR   GO; GO:0055102; F:lipase inhibitor activity; ISO:RGD.
DR   GO; GO:0005319; F:lipid transporter activity; TAS:RGD.
DR   GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IDA:RGD.
DR   GO; GO:0033344; P:cholesterol efflux; ISO:RGD.
DR   GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR   GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR   GO; GO:0034382; P:chylomicron remnant clearance; ISO:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:RGD.
DR   GO; GO:0006954; P:inflammatory response; IEP:RGD.
DR   GO; GO:0006869; P:lipid transport; TAS:RGD.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR   GO; GO:0042953; P:lipoprotein transport; IDA:RGD.
DR   GO; GO:0060621; P:negative regulation of cholesterol import; ISO:RGD.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISO:RGD.
DR   GO; GO:0010987; P:negative regulation of high-density lipoprotein particle clearance; ISO:RGD.
DR   GO; GO:0050995; P:negative regulation of lipid catabolic process; ISO:RGD.
DR   GO; GO:0045833; P:negative regulation of lipid metabolic process; ISO:RGD.
DR   GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; ISO:RGD.
DR   GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; ISO:RGD.
DR   GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IDA:RGD.
DR   GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; ISO:RGD.
DR   GO; GO:0010897; P:negative regulation of triglyceride catabolic process; ISO:RGD.
DR   GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; ISO:RGD.
DR   GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; ISO:RGD.
DR   GO; GO:0033700; P:phospholipid efflux; ISO:RGD.
DR   GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IMP:RGD.
DR   GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:RGD.
DR   GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR   GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IDA:RGD.
DR   GO; GO:0034014; P:response to triglyceride; IEP:RGD.
DR   GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0019433; P:triglyceride catabolic process; ISO:RGD.
DR   GO; GO:0070328; P:triglyceride homeostasis; ISO:RGD.
DR   GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR   GO; GO:0006642; P:triglyceride mobilization; ISO:RGD.
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   2: Evidence at transcript level;
KW   Chylomicron; Glycoprotein; Lipid degradation; Lipid metabolism;
KW   Lipid transport; Oxidation; Reference proteome; Secreted; Sialic acid;
KW   Signal; Transport; VLDL.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..101
FT                   /note="Apolipoprotein C-III"
FT                   /id="PRO_0000002035"
FT   REGION          69..101
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         64
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P33622"
FT   CARBOHYD        96
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02656"
SQ   SEQUENCE   101 AA;  11117 MW;  1A7260DB909692D2 CRC64;
     MQPRMLLIVA LVALLASARA DEGEGSLLLG SMQGYMEQAS KTVQDALSSM QESDIAVVAS
     RGWMDNRFKS LKGYWSKFTD KFTGLWESGP EDQLTTPTLE P
 
 
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