APOC1_MYOGA
ID APOC1_MYOGA Reviewed; 88 AA.
AC P0DUX5;
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 Myodes glareolus (Bank vole) (Clethrionomys glareolus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Arvicolinae; Myodes.
OX NCBI_TaxID=447135;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Spleen;
RA Lundberg M.;
RT "Signatures of selection in the bank vole genome.";
RL Submitted (SEP-2017) 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RL Unpublished observations (JUL-2021).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; MULK01015774; -; 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_0000453988"
FT CHAIN 29..88
FT /note="Truncated apolipoprotein C-I"
FT /evidence="ECO:0000250|UniProtKB:P86336"
FT /id="PRO_0000453989"
SQ SEQUENCE 88 AA; 9894 MW; 751029E7346D523E CRC64;
MRLFISLPVL IVVLAMALEG PAPAQATPDL SSTFENLPDK LKEFGNTLED KARAAIEHIK
QKEFLTKTRT WISETFGKMK EKIKTTFA