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 15-MAR-2017, entry version 9. 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 OS monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Atelidae; 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 RA Puppione D.L.; RL Unpublished observations (NOV-2012).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 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 CC low density lipoprotein (VLDL) receptor. Associates with high CC density lipoproteins (HDL) and the triacylglycerol-rich CC lipoproteins in the plasma and makes up about 10% of the protein CC of the VLDL and 2% of that of HDL. Appears to interfere directly CC with fatty acid uptake and is also the major plasma inhibitor of CC cholesteryl ester transfer protein (CETP). Binds free fatty acids CC and reduces their intracellular esterification. Modulates the CC interaction of APOE with beta-migrating VLDL and inhibits binding CC of beta-VLDL to the LDL receptor-related protein. CC {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) CC and basic (APOC1B) forms in P.paniscus, P.abelii and P.troglodytes CC and perhaps also in baboons and macaques. The two genes for ApoC-I CC arose through a duplication process that occurred after the CC divergence of New World monkeys from the human lineage. In human, CC the acidic form has become a pseudogene sometime between the CC divergence of bonobos and chimpanzees from the human lineage and CC the appearance of the Denisovans. Pseudogenization resulted when CC the codon for the penultimate amino acid in the signal sequence CC was changed to a stop codon. {ECO:0000303|PubMed:25160599}. CC -!- SIMILARITY: Belongs to the apolipoprotein C1 family. CC {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 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 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 {ECO:0000250}. FT CHAIN 27 86 Apolipoprotein C-I. FT /FTId=PRO_0000420976. FT CHAIN 29 86 Truncated apolipoprotein C-I. FT {ECO:0000250|UniProtKB:P86336}. FT /FTId=PRO_0000420977. SQ SEQUENCE 86 AA; 9716 MW; 0B7E4CAB7A4DFB08 CRC64; MRLFLSLPVL VVVLLMILEG PGPAQGAPEA LDTSSGLDKL KEFGNTLEDK VREFFNRVKE SDIPAKTRNW FSETLQKVKE KLRIES //