ID   APOC3_MIRAN             Reviewed;         100 AA.
AC   P0DTS4;
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   Mirounga angustirostris (Northern elephant seal).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Mirounga.
OX   NCBI_TaxID=9716;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Johnson J., Muren E., Swofford R., Turner-Maier J., Marinescu V.D.,
RA   Genereux D.P., Alfoldi J., Birren B., Karlsson E.K., Lindblad-Toh K.;
RT   "The 200 mammals project: sequencing genomes by a novel cost-effective
RT   method, yielding a high resolution annotation of the human genome.";
RL   Submitted (NOV-2017) 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RL   Unpublished observations (OCT-2019).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; PITE01000000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DTS4; -.
DR   SMR; P0DTS4; -.
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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..100
FT                   /note="Apolipoprotein C-III"
FT                   /id="PRO_0000448771"
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;  10975 MW;  5516670E60163EA7 CRC64;
     MQPRVLLVAA LLVLLASARA LEAEDPSLLD LMQGYMQHAT KTAQDTLTSV QESQVAQRAR
     DWMTDGFSSL KDYWSTFKGK FSGFWDSASE AQTTPASDAS