APOC1_CANLF
ID APOC1_CANLF Reviewed; 88 AA.
AC P56595;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=2515239;
RA Luo C.-C., Li W.-H., Chan L.;
RT "Structure and expression of dog apolipoprotein A-I, E, and C-I mRNAs:
RT implications for the evolution and functional constraints of apolipoprotein
RT structure.";
RL J. Lipid Res. 30:1735-1746(1989).
RN [2]
RP PROTEIN SEQUENCE OF 27-88, AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=20483223; DOI=10.1016/j.cbd.2008.08.002;
RA Puppione D.L., Bassilian S., Souda P., MacDonald M.H., Halgand F.,
RA Hagland F., Whitelegge J.P.;
RT "Mass spectral analysis of the apolipoproteins on dog (Canis lupus
RT familiaris) high density lipoproteins. Detection of apolipoprotein A-II.";
RL Comp. Biochem. Physiol. 3:290-296(2008).
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 -!- TISSUE SPECIFICITY: Expressed in the liver.
CC {ECO:0000269|PubMed:2515239}.
CC -!- MASS SPECTROMETRY: [Apolipoprotein C-I]: Mass=7042.11; Mass_error=0.2;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:20483223};
CC -!- SIMILARITY: Belongs to the apolipoprotein C1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; B60940; B60940.
DR RefSeq; NP_001183977.1; NM_001197048.1.
DR AlphaFoldDB; P56595; -.
DR SMR; P56595; -.
DR STRING; 9612.ENSCAFP00000032584; -.
DR PaxDb; P56595; -.
DR PRIDE; P56595; -.
DR Ensembl; ENSCAFT00030003392; ENSCAFP00030003005; ENSCAFG00030001852.
DR Ensembl; ENSCAFT00040021279; ENSCAFP00040018477; ENSCAFG00040011515.
DR Ensembl; ENSCAFT00845011823; ENSCAFP00845009224; ENSCAFG00845006666.
DR GeneID; 476437; -.
DR KEGG; cfa:476437; -.
DR CTD; 341; -.
DR VEuPathDB; HostDB:ENSCAFG00845006666; -.
DR eggNOG; ENOG502SEU4; Eukaryota.
DR GeneTree; ENSGT00390000011584; -.
DR HOGENOM; CLU_160094_1_0_1; -.
DR InParanoid; P56595; -.
DR OMA; NWFTEQF; -.
DR OrthoDB; 1398460at2759; -.
DR TreeFam; TF330940; -.
DR Reactome; R-CFA-8866423; VLDL assembly.
DR Reactome; R-CFA-8964046; VLDL clearance.
DR Proteomes; UP000002254; Chromosome 1.
DR Bgee; ENSCAFG00000004615; Expressed in adrenal cortex and 46 other tissues.
DR GO; GO:0034364; C:high-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0004859; F:phospholipase inhibitor activity; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR GO; GO:0032375; P:negative regulation of cholesterol transport; IBA:GO_Central.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IBA:GO_Central.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IBA:GO_Central.
DR GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IBA:GO_Central.
DR GO; GO:0006641; P:triglyceride metabolic process; IBA:GO_Central.
DR GO; GO:0034447; P:very-low-density lipoprotein particle clearance; IBA:GO_Central.
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 1: Evidence at protein level;
KW Direct protein sequencing; Lipid transport; Reference proteome; Secreted;
KW Signal; Transport; VLDL.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:20483223"
FT CHAIN 27..88
FT /note="Apolipoprotein C-I"
FT /id="PRO_0000002013"
FT CHAIN 29..88
FT /note="Truncated apolipoprotein C-I"
FT /evidence="ECO:0000250|UniProtKB:P86336"
FT /id="PRO_0000391842"
SQ SEQUENCE 88 AA; 9741 MW; A60A5C5EA933302E CRC64;
MRLILSLPVL VVVLSMVLEG PAPAQAAGEI SSTFERIPDK LKEFGNTLED KARAAIESIK
KSDIPAKTRN WFSEAFKKVK EHLKTAFS
