ID   APOC3_ACIJB             Reviewed;         100 AA.
AC   P0DSP0;
DT   31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   25-MAY-2022, entry version 8.
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   Acinonyx jubatus (Cheetah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Acinonychinae;
OC   Acinonyx.
OX   NCBI_TaxID=32536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scott A., Pukazhenthi B., Koepfli K.-P., Mohr D., Crosier A., O'Brien S.J.,
RA   Tamazian G., Dobrynin P., Komissarov A., Kliver S., Krasheninnikova K.;
RT   "Linked reads assembly of the African cheetah.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (JUN-2019).
CC   -!- FUNCTION: Component of triglyceride-rich very low density lipoproteins
CC       (VLDL) and high density lipoproteins (HDL) in plasma (By similarity).
CC       Plays a multifaceted role in triglyceride homeostasis (By similarity).
CC       Intracellularly, promotes hepatic very low density lipoprotein 1
CC       (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis
CC       and clearance of triglyceride-rich lipoproteins (TRLs) (By similarity).
CC       Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the
CC       hepatic uptake of TRLs by remnant receptors (By similarity). Formed of
CC       several curved helices connected via semiflexible hinges, so that it
CC       can wrap tightly around the curved micelle surface and easily adapt to
CC       the different diameters of its natural binding partners (By
CC       similarity). {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 (By similarity).
CC       Less abundant glycoforms are characterized by more complex and
CC       fucosylated glycan moieties (By similarity). O-glycosylated on Thr-94
CC       with a core 1 or possibly core 8 glycan (By similarity).
CC       {ECO:0000250|UniProtKB:P02656}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C3 family. {ECO:0000305}.
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DR   EMBL; QURD01003265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DSP0; -.
DR   SMR; P0DSP0; -.
DR   Proteomes; UP000504626; Unplaced.
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; Reference proteome; Secreted; Sialic acid; Signal;
KW   Transport; VLDL.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..100
FT                   /note="Apolipoprotein C-III"
FT                   /id="PRO_0000447663"
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;  10977 MW;  6B9DE9604B2EE74E CRC64;
     MQSRVLLVTA LLVLLASARA TEGEDPSLLG LMHGYVQHAT KTAQDTLTTV REFPVAQQAR
     DWVTGRFTSL KDYWSTLTGK FSGFWDSTFA VTPTPASEAK