ID   APOC3_MACFA             Reviewed;          99 AA.
AC   P18659;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   25-MAY-2022, entry version 100.
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   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leukocyte;
RX   PubMed=8448212; DOI=10.1016/0167-4781(93)90226-4;
RA   Osada J., Pocovi M., Nicolosi R.J., Schaefer E.J., Ordovas J.M.;
RT   "Nucleotide sequences of the Macaca fascicularis apolipoprotein C-III and
RT   A-IV genes.";
RL   Biochim. Biophys. Acta 1172:335-339(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-36.
RX   PubMed=3105581; DOI=10.1021/bi00379a037;
RA   Herbert P.N., Bausserman L.L., Lynch K.M., Saritelli A.L., Kantor M.A.,
RA   Nicolosi R.J., Shulman R.S.;
RT   "Homologues of the human C and A apolipoproteins in the Macaca fascicularis
RT   (cynomolgus) monkey.";
RL   Biochemistry 26:1457-1463(1987).
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   -!- SIMILARITY: Belongs to the apolipoprotein C3 family. {ECO:0000305}.
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DR   EMBL; X68359; CAA48419.1; -; Genomic_DNA.
DR   PIR; S30196; S29566.
DR   RefSeq; XP_005579787.1; XM_005579730.1.
DR   AlphaFoldDB; P18659; -.
DR   SMR; P18659; -.
DR   STRING; 9541.XP_005579786.1; -.
DR   GeneID; 102144085; -.
DR   KEGG; mcf:102144085; -.
DR   CTD; 345; -.
DR   VEuPathDB; HostDB:ENSMFAG00000001837; -.
DR   eggNOG; ENOG502SZ00; Eukaryota.
DR   OMA; YWSTFKG; -.
DR   OrthoDB; 1613530at2759; -.
DR   Proteomes; UP000233100; Chromosome 14.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
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; Reference proteome; Secreted;
KW   Sialic acid; Signal; Transport; VLDL.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:3105581"
FT   CHAIN           21..99
FT                   /note="Apolipoprotein C-III"
FT                   /id="PRO_0000002032"
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   CARBOHYD        94
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02656"
SQ   SEQUENCE   99 AA;  10747 MW;  24B476162B43F733 CRC64;
     MQPRVLLVAA LLSLLASARA SEAEDTSLLG FMQGYMQHAT KTAKDALTSV QESQVAQQAR
     GWVTDGFSSL KDYWSTVKDK LSGFWDLNPE AKPTLAEAA