ID   APOC3_PHOVI             Reviewed;         100 AA.
AC   P0DTS5;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2019, sequence version 1.
DT   25-MAY-2022, entry version 6.
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   Phoca vitulina (Harbor seal).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Phoca.
OX   NCBI_TaxID=9720;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood;
RA   Culibrk L., Leelakumari S., Taylor G.A., Tse K., Cheng D., Chuah E.,
RA   Kirk H., Pandoh P., Troussard A., Zhao Y., Mungall A., Moore R.,
RA   Akhurst L., Marra M.A., Haulena M., Jones S.J.M.;
RT   "The genome of the Harbour Seal (Phoca vitulina).";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (OCT-2019).
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; ML169427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DTS5; -.
DR   SMR; P0DTS5; -.
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   3: Inferred from homology;
KW   Chylomicron; Glycoprotein; Lipid degradation; Lipid metabolism;
KW   Lipid transport; Secreted; Sialic acid; Signal; Transport; VLDL.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..100
FT                   /note="Apolipoprotein C-III"
FT                   /id="PRO_0000448772"
FT   REGION          68..100
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   100 AA;  10941 MW;  4E0720C160163C73 CRC64;
     MQPRVLLVAA LLVLLASARA LEAEDPSLLG LMQGYMQHAT KTAQDTLTSV QESQVAQRAR
     DWMTDGFSSL KDYWSTFKGK FSGFWDSASE VQPTPASDAS