ID APOC1_ATEGE Reviewed; 86 AA. AC P0DKV3; DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2013, sequence version 1. DT 25-MAY-2022, entry version 11. 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 Ateles geoffroyi (Black-handed spider monkey) (Geoffroy's spider monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Atelidae; OC Atelinae; Ateles. OX NCBI_TaxID=9509; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Cheng J.-F., Hamilton M., Peng Y., Hosseini R., Peng Z., Malinov I., RA Rubin E.M.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP IDENTIFICATION. RA Puppione D.L.; RL Unpublished observations (NOV-2012). RN [3] 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 [4] 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 --------------------------------------------------------------------------- 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 EMBL; AC188244; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; P0DKV3; -. DR SMR; P0DKV3; -. 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:0000250" FT CHAIN 27..86 FT /note="Apolipoprotein C-I" FT /id="PRO_0000420976" FT CHAIN 29..86 FT /note="Truncated apolipoprotein C-I" FT /evidence="ECO:0000250|UniProtKB:P86336" FT /id="PRO_0000420977" SQ SEQUENCE 86 AA; 9716 MW; 0B7E4CAB7A4DFB08 CRC64; MRLFLSLPVL VVVLLMILEG PGPAQGAPEA LDTSSGLDKL KEFGNTLEDK VREFFNRVKE SDIPAKTRNW FSETLQKVKE KLRIES //