ID   APOC1_OTOGA             Reviewed;          80 AA.
AC   P0DMP0;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 25.
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   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611;
RN   [1]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (JUL-2014).
RN   [2]
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   [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 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}.
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DR   RefSeq; XP_003799546.1; XM_003799498.2.
DR   AlphaFoldDB; P0DMP0; -.
DR   SMR; P0DMP0; -.
DR   STRING; 30611.ENSOGAP00000017609; -.
DR   Ensembl; ENSOGAT00000024249; ENSOGAP00000017609; ENSOGAG00000028159.
DR   GeneID; 100955916; -.
DR   KEGG; oga:100955916; -.
DR   CTD; 341; -.
DR   eggNOG; ENOG502SEU4; Eukaryota.
DR   GeneTree; ENSGT00390000011584; -.
DR   HOGENOM; CLU_160094_1_0_1; -.
DR   OMA; NWFTEQF; -.
DR   OrthoDB; 1558708at2759; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
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:UniProtKB-KW.
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   3: Inferred from homology;
KW   Lipid transport; Reference proteome; Secreted; Signal; Transport; VLDL.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..80
FT                   /note="Apolipoprotein C-I"
FT                   /id="PRO_0000430329"
FT   CHAIN           ?..80
FT                   /note="Truncated apolipoprotein C-I"
FT                   /id="PRO_0000430330"
SQ   SEQUENCE   80 AA;  9144 MW;  E31B65A4CDA221EA CRC64;
     MRLMLSLPVL VLVLAMVLEG PAPAQGTMDL DFTRHLKEFG NTMGDKAREV IDRIKQSDIP
     AKTRNWFSET FQKVKEKLKI