ID   APO1B_COLGU             Reviewed;          83 AA.
AC   P0DKU8;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   25-MAY-2022, entry version 12.
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   Colobus guereza (Mantled guereza) (Eastern black-and-white colobus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=33548;
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RL   Unpublished observations (NOV-2012).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}.
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DR   EMBL; AC148222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DKU8; -.
DR   SMR; P0DKU8; -.
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   3: Inferred from homology;
KW   Lipid transport; Secreted; Signal; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..83
FT                   /note="Apolipoprotein C-I, basic form"
FT                   /id="PRO_0000420901"
FT   CHAIN           27..64
FT                   /note="Cholesteryl ester transfer inhibitor protein"
FT                   /evidence="ECO:0000250|UniProtKB:P34929"
FT                   /id="PRO_0000436801"
FT   CHAIN           29..83
FT                   /note="Truncated apolipoprotein C-I, basic form"
FT                   /evidence="ECO:0000250|UniProtKB:P86336"
FT                   /id="PRO_0000420902"
SQ   SEQUENCE   83 AA;  9360 MW;  D2C9673C0214B61D CRC64;
     MRLFLSLPVL VVVLSMVLEG PAPAQGAPDV SSALDKLKEF GNTLEDKARE VINRIKQSEF
     PAKTRDWFSE TFRKVKEKLK INS