ID   APOC1_RABIT             Reviewed;          28 AA.
AC   P33047;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Apolipoprotein C-I;
DE            Short=Apo-CI;
DE            Short=ApoC-I;
DE   AltName: Full=Apolipoprotein C1;
DE   Flags: Fragment;
GN   Name=APOC1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RX   PubMed=2266137; DOI=10.1016/s0021-9258(18)45726-2;
RA   Weisgraber K.H., Mahley R.W., Kowal R.C., Herz J., Goldstein J.L.,
RA   Brown M.S.;
RT   "Apolipoprotein C-I modulates the interaction of apolipoprotein E with
RT   beta-migrating very low density lipoproteins (beta-VLDL) and inhibits
RT   binding of beta-VLDL to low density lipoprotein receptor-related protein.";
RL   J. Biol. Chem. 265:22453-22459(1990).
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 (By similarity). Modulates the interaction of APOE with
CC       beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL
CC       receptor-related protein. {ECO:0000250|UniProtKB:P02654,
CC       ECO:0000269|PubMed:2266137}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02654}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C1 family. {ECO:0000305}.
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DR   PIR; A23691; A23691.
DR   AlphaFoldDB; P33047; -.
DR   STRING; 9986.ENSOCUP00000018618; -.
DR   eggNOG; ENOG502SEU4; Eukaryota.
DR   Proteomes; UP000001811; Unplaced.
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   Pfam; PF04691; ApoC-I; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lipid transport; Reference proteome; Secreted;
KW   Transport; VLDL.
FT   CHAIN           1..>28
FT                   /note="Apolipoprotein C-I"
FT                   /id="PRO_0000190978"
FT   NON_TER         28
SQ   SEQUENCE   28 AA;  3165 MW;  2903C027F676541C CRC64;
     APDFSTLELI PDKLKEFGNT LEEKARMA