ID   APOC1_GRASU             Reviewed;          88 AA.
AC   P0DUX4;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 1.
DT   03-AUG-2022, entry version 3.
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   Grammomys surdaster (African woodland thicket rat) (Thamnomys surdaster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Grammomys.
OX   NCBI_TaxID=491861;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mullikin J., Morrison R., Duffy P.;
RT   "African thicket rat Grammomys surdaster (dolichurus), natural host of
RT   rodent malaria parasites, TR1022 genome.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (JUL-2021).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). Modulates the interaction of APOE with beta-migrating VLDL and
CC       inhibits binding of beta-VLDL to the LDL receptor-related protein (By
CC       similarity). Binds free fatty acids and reduces their intracellular
CC       esterification (By similarity). {ECO:0000250|UniProtKB:P02654,
CC       ECO:0000250|UniProtKB:P33047, ECO:0000250|UniProtKB:P34928}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02654}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C1 family. {ECO:0000305}.
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DR   EMBL; SRMG01000208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
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..88
FT                   /note="Apolipoprotein C-I"
FT                   /id="PRO_0000453985"
FT   CHAIN           29..88
FT                   /note="Truncated apolipoprotein C-I"
FT                   /evidence="ECO:0000250|UniProtKB:P86336"
FT                   /id="PRO_0000453986"
SQ   SEQUENCE   88 AA;  9857 MW;  C85A642134A4CB82 CRC64;
     MRLFIALPVL IVVVAMALEG PAPAQAAPDL SSTLERLPDK LKEFGSTLED KAREAIDHIK
     QKEILTKTRT WFSETFSKVK EKLKTTFA