ID   APOC3_HETGA             Reviewed;         107 AA.
AC   G5BQH4;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 2.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Apolipoprotein C-III {ECO:0000312|EMBL:EHB11535.1};
DE            Short=Apo-CIII;
DE            Short=ApoC-III;
DE   AltName: Full=Apolipoprotein C3;
DE   Flags: Precursor;
GN   Name=Apoc3 {ECO:0000305};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000312|EMBL:EHB11535.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (AUG-2014).
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-101 with a core 1 or possibly core 8
CC       glycan. {ECO:0000250|UniProtKB:P02656}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EHB11535.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; JH171387; EHB11535.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AHKG01061059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004856700.1; XM_004856643.2.
DR   AlphaFoldDB; G5BQH4; -.
DR   SMR; G5BQH4; -.
DR   STRING; 10181.XP_004856700.1; -.
DR   Ensembl; ENSHGLT00000026991; ENSHGLP00000026753; ENSHGLG00000019030.
DR   GeneID; 101725083; -.
DR   KEGG; hgl:101725083; -.
DR   CTD; 345; -.
DR   eggNOG; ENOG502SZ00; Eukaryota.
DR   InParanoid; G5BQH4; -.
DR   OMA; YWSTFKG; -.
DR   OrthoDB; 1613530at2759; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
DR   Bgee; ENSHGLG00000019030; Expressed in adult mammalian kidney and 6 other tissues.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR   GO; GO:0034363; C:intermediate-density lipoprotein particle; IEA:Ensembl.
DR   GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IEA:Ensembl.
DR   GO; GO:0055102; F:lipase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR   GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR   GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR   GO; GO:0034382; P:chylomicron remnant clearance; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR   GO; GO:0060621; P:negative regulation of cholesterol import; IEA:Ensembl.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0010987; P:negative regulation of high-density lipoprotein particle clearance; IEA:Ensembl.
DR   GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IEA:Ensembl.
DR   GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
DR   GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR   GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IEA:Ensembl.
DR   GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IEA:Ensembl.
DR   GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IEA:Ensembl.
DR   GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR   GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IEA:Ensembl.
DR   GO; GO:0019433; P:triglyceride catabolic process; IEA:Ensembl.
DR   GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
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; Lipoprotein; Oxidation; Reference proteome; Secreted;
KW   Sialic acid; Signal; Transport; VLDL.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..107
FT                   /note="Apolipoprotein C-III"
FT                   /id="PRO_0000430652"
FT   REGION          72..106
FT                   /note="Lipid-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            45
FT                   /note="May interact with the LDL receptor"
FT                   /evidence="ECO:0000250|UniProtKB:P02656"
FT   MOD_RES         67
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P33622"
FT   CARBOHYD        101
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02656"
SQ   SEQUENCE   107 AA;  11858 MW;  81816ABDADFFDD61 CRC64;
     MQPRVFLAVT LLALLASARA LETEDASLLG YMQDYMQGYM EHASKTAQDA LTRVQDSQMA
     QQARGWMSDS LSSLQDYWSS FKGKWSGFGF WDATPEEASP TPAPEGI