APOC1_RAT
ID APOC1_RAT Reviewed; 88 AA.
AC P19939; Q53ZD8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Apolipoprotein C-I;
DE Short=Apo-CI;
DE Short=ApoC-I;
DE AltName: Full=Apolipoprotein C1;
DE AltName: Full=Liver regeneration-related protein LRRG04;
DE Contains:
DE RecName: Full=Truncated apolipoprotein C-I;
DE Flags: Precursor;
GN Name=Apoc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2771655; DOI=10.1093/nar/17.15.6405;
RA Shen P.Y., Howlett G.J.;
RT "Nucleotide sequence of cDNA for rat apolipoprotein C-I.";
RL Nucleic Acids Res. 17:6405-6405(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Xu C.S., Li W.Q., Li Y.C., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
RA Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F.,
RA Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; X15512; CAA33536.1; -; mRNA.
DR EMBL; AY327505; AAP97737.1; -; mRNA.
DR EMBL; BC098670; AAH98670.1; -; mRNA.
DR PIR; S05307; S05307.
DR RefSeq; NP_001103466.1; NM_001109996.1.
DR RefSeq; NP_036956.1; NM_012824.2.
DR RefSeq; XP_017443603.1; XM_017588114.1.
DR RefSeq; XP_017445495.1; XM_017590006.1.
DR AlphaFoldDB; P19939; -.
DR SMR; P19939; -.
DR IntAct; P19939; 1.
DR STRING; 10116.ENSRNOP00000040585; -.
DR iPTMnet; P19939; -.
DR PhosphoSitePlus; P19939; -.
DR PaxDb; P19939; -.
DR PRIDE; P19939; -.
DR GeneID; 25292; -.
DR KEGG; rno:25292; -.
DR UCSC; RGD:2134; rat.
DR CTD; 341; -.
DR RGD; 2134; Apoc1.
DR VEuPathDB; HostDB:ENSRNOG00000018426; -.
DR eggNOG; ENOG502SEU4; Eukaryota.
DR HOGENOM; CLU_160094_1_0_1; -.
DR InParanoid; P19939; -.
DR OMA; ELPAKMW; -.
DR OrthoDB; 1558708at2759; -.
DR PhylomeDB; P19939; -.
DR TreeFam; TF330940; -.
DR PRO; PR:P19939; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018426; Expressed in liver and 18 other tissues.
DR Genevisible; P19939; RN.
DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:RGD.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:RGD.
DR GO; GO:0005504; F:fatty acid binding; ISO:RGD.
DR GO; GO:0055102; F:lipase inhibitor activity; ISO:RGD.
DR GO; GO:0004859; F:phospholipase inhibitor activity; ISO:RGD.
DR GO; GO:0033344; P:cholesterol efflux; ISO:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR GO; GO:0034382; P:chylomicron remnant clearance; ISO:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; TAS:RGD.
DR GO; GO:0032375; P:negative regulation of cholesterol transport; ISO:RGD.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; ISO:RGD.
DR GO; GO:0045833; P:negative regulation of lipid metabolic process; ISO:RGD.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; ISO:RGD.
DR GO; GO:0010900; P:negative regulation of phosphatidylcholine catabolic process; ISO:RGD.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; ISO:RGD.
DR GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0033700; P:phospholipid efflux; ISO:RGD.
DR GO; GO:0034369; P:plasma lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0032368; P:regulation of lipid transport; IDA:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR GO; GO:0034447; P:very-low-density lipoprotein particle clearance; ISO:RGD.
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 CHAIN 27..88
FT /note="Apolipoprotein C-I"
FT /id="PRO_0000002018"
FT CHAIN 29..88
FT /note="Truncated apolipoprotein C-I"
FT /evidence="ECO:0000250|UniProtKB:P86336"
FT /id="PRO_0000391846"
SQ SEQUENCE 88 AA; 9861 MW; 4A4D70D836B30EE8 CRC64;
MRLFIALPVL IVVVAMALEG PAPAQAAPDF SSAMESLPDK LKEFGNTLED KARAAIEHIK
QKEIMIKTRN WFSETLNKMK EKLKTTFA
