ID   APOC1_NEOLE             Reviewed;          88 AA.
AC   A0A1A6FVC0;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2016, sequence version 1.
DT   03-AUG-2022, entry version 12.
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   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27408812; DOI=10.1016/j.gdata.2016.06.008;
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The draft genome sequence and annotation of the desert woodrat Neotoma
RT   lepida.";
RL   Genom Data 9:58-59(2016).
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; LZPO01117068; OBS57519.1; -; Genomic_DNA.
DR   STRING; 56216.A0A1A6FVC0; -.
DR   Proteomes; UP000092124; Unassembled WGS sequence.
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; Reference proteome; Secreted; Signal; Transport; VLDL.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..88
FT                   /note="Apolipoprotein C-I"
FT                   /id="PRO_5008345086"
FT   CHAIN           29..88
FT                   /note="Truncated apolipoprotein C-I"
FT                   /evidence="ECO:0000250|UniProtKB:P86336"
FT                   /id="PRO_0000453990"
SQ   SEQUENCE   88 AA;  9853 MW;  8B9B5E3671A91956 CRC64;
     MRLFISLPIL IVVLAMALEG PAPAQATPDL ASTFENLPDK LKEFGSALED KTRAAIEHIK
     QKGILTKTRT WFSETFDKVK EKFKTTFA