APOC1_LYNPA
ID APOC1_LYNPA Reviewed; 78 AA.
AC P0DPH1;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 25-MAY-2022, entry version 7.
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 Lynx pardinus (Iberian lynx) (Felis pardina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX NCBI_TaxID=191816;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (MAY-2018).
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; FIZN01081397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DPH1; -.
DR SMR; P0DPH1; -.
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 InterPro; IPR006781; ApoC-I.
DR PANTHER; PTHR16565; PTHR16565; 1.
PE 3: Inferred from homology;
KW Lipid transport; Secreted; Signal; Transport; VLDL.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..78
FT /note="Apolipoprotein C-I"
FT /id="PRO_0000444586"
FT CHAIN 29..78
FT /note="Truncated apolipoprotein C-I"
FT /evidence="ECO:0000250|UniProtKB:P86336"
FT /id="PRO_0000444587"
SQ SEQUENCE 78 AA; 8636 MW; 47FFC7A2C73C94F6 CRC64;
MRLILWLPVL VVVLLMVLEG PAPAQGAPDI AGTFRNIPNS LKEFGNNLKD AFENIPEATR
KLMTSFAEGL KNFRIPMV