ID   APO1A_PONAB             Reviewed;          83 AA.
AC   P0CE39;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Apolipoprotein C-I, acidic form;
DE            Short=Apo-CIA;
DE            Short=ApoC-IA;
DE   AltName: Full=Apolipoprotein C1A;
DE   Contains:
DE     RecName: Full=Truncated apolipoprotein C-I, acidic form;
DE              Short=Apo-CIA';
DE              Short=ApoC-IA';
DE   Flags: Precursor;
GN   Name=APOC1A;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2]
RP   IDENTIFICATION, AND MASS SPECTROMETRY.
RX   PubMed=20209111; DOI=10.1016/j.cbd.2009.12.003;
RA   Puppione D.L., Ryan C.M., Bassilian S., Souda P., Xiao X., Ryder O.A.,
RA   Whitelegge J.P.;
RT   "Detection of two distinct forms of apoC-I in great apes.";
RL   Comp. Biochem. Physiol. 5D:73-79(2010).
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   -!- MASS SPECTROMETRY: [Apolipoprotein C-I, acidic form]: Mass=6729.6;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:20209111};
CC   -!- MASS SPECTROMETRY: [Truncated apolipoprotein C-I, acidic form]:
CC       Mass=6562.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:20209111};
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}.
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DR   AlphaFoldDB; P0CE39; -.
DR   SMR; P0CE39; -.
DR   InParanoid; P0CE39; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Lipid transport; Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..83
FT                   /note="Apolipoprotein C-I, acidic form"
FT                   /id="PRO_0000391838"
FT   CHAIN           29..83
FT                   /note="Truncated apolipoprotein C-I, acidic form"
FT                   /evidence="ECO:0000250|UniProtKB:P86336"
FT                   /id="PRO_0000391839"
SQ   SEQUENCE   83 AA;  9449 MW;  8FDC77507C6850E9 CRC64;
     MRLFLSLPVL VVVLSMVLEG PAPAQGAPDV SNPFDGLEEL GKTLEDNTRE FINRITQSEL
     PAKMWDWFSE TFRRVKEKLK IDS