APO1B_MACFA
ID APO1B_MACFA Reviewed; 83 AA.
AC P18657; A2V9Y4; G7PXV4;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Apolipoprotein C-I, basic form;
DE Short=Apo-CIB;
DE Short=ApoC-IB;
DE AltName: Full=Apolipoprotein C1B;
DE Contains:
DE RecName: Full=Cholesteryl ester transfer inhibitor protein;
DE Short=CETIP;
DE Contains:
DE RecName: Full=Truncated apolipoprotein C-I, basic form;
DE Short=Apo-CIB';
DE Short=ApoC-IB';
DE Flags: Precursor;
GN Name=APOC1B;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Kobayashi M., Uno Y., Suzuki Y., Osada N., Kusuda J., Sugano S., Inoue I.,
RA Hashimoto K.;
RT "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT microarray.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
RN [3]
RP PROTEIN SEQUENCE OF 27-48.
RX PubMed=3105581; DOI=10.1021/bi00379a037;
RA Herbert P.N., Bausserman L.L., Lynch K.M., Saritelli A.L., Kantor M.A.,
RA Nicolosi R.J., Shulman R.S.;
RT "Homologues of the human C and A apolipoproteins in the Macaca fascicularis
RT (cynomolgus) monkey.";
RL Biochemistry 26:1457-1463(1987).
RN [4]
RP REVIEW.
RX PubMed=28757862; DOI=10.1007/s11515-013-1278-7;
RA Puppione D., Whitelegge J.P.;
RT "Proteogenomic Review of the Changes in Primate apoC-I during Evolution.";
RL Front. Biol. 8:533-548(2013).
RN [5]
RP GENE DUPLICATION.
RX PubMed=25160599; DOI=10.1016/j.cbd.2014.08.001;
RA Puppione D.L.;
RT "Higher primates, but not New World monkeys, have a duplicate set of
RT enhancers flanking their apoC-I genes.";
RL Comp. Biochem. Physiol. 11:45-48(2014).
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 -!- MISCELLANEOUS: Apolipoprotein C-I is present in acidic (APOC1A) and
CC basic (APOC1B) forms in P.paniscus, P.abelii and P.troglodytes and
CC perhaps also in baboons and macaques. The two genes for ApoC-I arose
CC through a duplication process that occurred after the divergence of New
CC World monkeys from the human lineage. In human, the acidic form has
CC become a pseudogene sometime between the divergence of bonobos and
CC chimpanzees from the human lineage and the appearance of the
CC Denisovans. Pseudogenization resulted when the codon for the
CC penultimate amino acid in the signal sequence was changed to a stop
CC codon. {ECO:0000303|PubMed:25160599}.
CC -!- SIMILARITY: Belongs to the apolipoprotein C1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EHH59678.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK240617; BAF47371.1; -; mRNA.
DR EMBL; AK240623; BAF47377.1; -; mRNA.
DR EMBL; CM001294; EHH59678.1; ALT_SEQ; Genomic_DNA.
DR PIR; C26627; C26627.
DR RefSeq; XP_005589612.1; XM_005589555.2.
DR AlphaFoldDB; P18657; -.
DR SMR; P18657; -.
DR STRING; 9541.XP_005589612.1; -.
DR Ensembl; ENSMFAT00000037098; ENSMFAP00000009847; ENSMFAG00000038912.
DR Ensembl; ENSMFAT00000037155; ENSMFAP00000009855; ENSMFAG00000038912.
DR GeneID; 102139092; -.
DR KEGG; mcf:102139092; -.
DR CTD; 341; -.
DR VEuPathDB; HostDB:ENSMFAG00000038912; -.
DR eggNOG; ENOG502SEU4; Eukaryota.
DR GeneTree; ENSGT00390000011584; -.
DR OMA; NWFTEQF; -.
DR OrthoDB; 1558708at2759; -.
DR Proteomes; UP000009130; Chromosome 19.
DR Proteomes; UP000233100; Chromosome 19.
DR Bgee; ENSMFAG00000038912; Expressed in liver and 12 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0005504; F:fatty acid binding; IEA:Ensembl.
DR GO; GO:0004859; F:phospholipase inhibitor activity; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0034382; P:chylomicron remnant clearance; IEA:Ensembl.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR GO; GO:0032375; P:negative regulation of cholesterol transport; IEA:Ensembl.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IEA:Ensembl.
DR GO; GO:0010900; P:negative regulation of phosphatidylcholine catabolic process; IEA:Ensembl.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR GO; GO:0034369; P:plasma lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR GO; GO:0034447; P:very-low-density lipoprotein particle clearance; IEA:Ensembl.
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.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:3105581"
FT CHAIN 27..83
FT /note="Apolipoprotein C-I, basic form"
FT /id="PRO_0000190977"
FT CHAIN 27..64
FT /note="Cholesteryl ester transfer inhibitor protein"
FT /evidence="ECO:0000250|UniProtKB:P34929"
FT /id="PRO_0000436802"
FT CHAIN 29..83
FT /note="Truncated apolipoprotein C-I, basic form"
FT /evidence="ECO:0000250|UniProtKB:P86336"
FT /id="PRO_0000436803"
SQ SEQUENCE 83 AA; 9390 MW; D2C9603B7264B61D CRC64;
MRLFLSLPVL VVVLSMVLEG PAPAQGAPDV SSALDKLKEF GNTLEDKAWE VINRIKQSEF
PAKTRDWFSE TFRKVKEKLK INS
