ID   APOC1_ROULE             Reviewed;          83 AA.
AC   P0DTG5;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 1.
DT   25-MAY-2022, entry version 5.
DE   RecName: Full=Apolipoprotein C-I;
DE            Short=Apo-CI;
DE            Short=ApoC-I;
DE   AltName: Full=Apolipoprotein C1;
DE   Contains:
DE     RecName: Full=Truncated apolipoprotein C-I;
DE   Flags: Precursor;
GN   Name=APOC1;
OS   Rousettus leschenaultii (Leschenault's rousette).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Rousettus.
OX   NCBI_TaxID=9408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=32966557; DOI=10.1093/dnares/dsaa021;
RA   Nikaido M., Kondo S., Zhang Z., Wu J., Nishihara H., Niimura Y., Suzuki S.,
RA   Touhara K., Suzuki Y., Noguchi H., Minakuchi Y., Toyoda A., Fujiyama A.,
RA   Sugano S., Yoneda M., Kai C.;
RT   "Comparative genomic analyses illuminate the distinct evolution of megabats
RT   within Chiroptera.";
RL   DNA Res. 27:0-0(2020).
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (JAN-2021).
CC   -!- FUNCTION: Inhibitor of lipoprotein binding to the low density
CC       lipoprotein (LDL) receptor, LDL receptor-related protein, and very low
CC       density lipoprotein (VLDL) receptor. Associates with high density
CC       lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the
CC       plasma and makes up about 10% of the protein of the VLDL and 2% of that
CC       of HDL. Appears to interfere directly with fatty acid uptake and is
CC       also the major plasma inhibitor of cholesteryl ester transfer protein
CC       (CETP). Binds free fatty acids and reduces their intracellular
CC       esterification. Modulates the interaction of APOE with beta-migrating
CC       VLDL and inhibits binding of beta-VLDL to the LDL receptor-related
CC       protein. {ECO:0000250|UniProtKB:P02654, ECO:0000250|UniProtKB:P33047}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02654}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C1 family. {ECO:0000305}.
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DR   EMBL; BNJM01000029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DTG5; -.
DR   SMR; P0DTG5; -.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; 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; 4.10.260.30; -; 1.
DR   InterPro; IPR043081; ApoC-1_sf.
DR   InterPro; IPR006781; ApoC-I.
DR   PANTHER; PTHR16565; PTHR16565; 1.
DR   Pfam; PF04691; ApoC-I; 1.
PE   3: Inferred from homology;
KW   Lipid transport; Secreted; Signal; Transport; VLDL.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..83
FT                   /note="Apolipoprotein C-I"
FT                   /id="PRO_0000452415"
FT   CHAIN           29..83
FT                   /note="Truncated apolipoprotein C-I"
FT                   /evidence="ECO:0000250|UniProtKB:P86336"
FT                   /id="PRO_0000452416"
SQ   SEQUENCE   83 AA;  9315 MW;  ABACC669E7EBAA0F CRC64;
     MRLILSLPVL AVVLAMVLEG PAPAQAAPDV SSTLESISEK LTEFGRTVAD KFRTAVDQIK
     KSDFPEKTRN WFSEMFNKLK EKF