APO1B_PAPHA
ID APO1B_PAPHA Reviewed; 83 AA.
AC P34929;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 86.
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 Papio hamadryas (Hamadryas baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9557;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1612596; DOI=10.1016/0888-7543(92)90255-q;
RA Pastorcic M., Birnbaum S., Hixson J.E.;
RT "Baboon apolipoprotein C-I: cDNA and gene structure and evolution.";
RL Genomics 13:368-374(1992).
RN [2]
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-2003) to the EMBL/GenBank/DDBJ databases.
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).
RN [5]
RP STRUCTURE BY NMR OF 27-64.
RX PubMed=10975576; DOI=10.1110/ps.9.8.1548;
RA Buchko G.W., Rozek A., Kanda P., Kennedy M.A., Cushley R.J.;
RT "Structural studies of a baboon (Papio sp.) plasma protein inhibitor of
RT cholesteryl ester transferase.";
RL Protein Sci. 9:1548-1558(2000).
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; L13175; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; L13176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC145523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 1EZE; NMR; -; A=27-64.
DR PDBsum; 1EZE; -.
DR AlphaFoldDB; P34929; -.
DR SMR; P34929; -.
DR EvolutionaryTrace; P34929; -.
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 3D-structure; Lipid transport; Secreted; Signal; Transport.
FT SIGNAL 1..26
FT CHAIN 27..83
FT /note="Apolipoprotein C-I, basic form"
FT /id="PRO_0000002016"
FT CHAIN 27..64
FT /note="Cholesteryl ester transfer inhibitor protein"
FT /evidence="ECO:0000269|PubMed:10975576"
FT /id="PRO_0000002017"
FT CHAIN 29..83
FT /note="Truncated apolipoprotein C-I, basic form"
FT /evidence="ECO:0000250|UniProtKB:P86336"
FT /id="PRO_0000391845"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:1EZE"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:1EZE"
FT HELIX 43..56
FT /evidence="ECO:0007829|PDB:1EZE"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:1EZE"
SQ SEQUENCE 83 AA; 9418 MW; D2C9602C6564A10A CRC64;
MRLFLSLPVL VVVLSMVLEG PAPVQGAPDV SSALDKLKEF GNTLEDKAWE VINRIKQSEF
PAKTRDWFSE TFRKVKEKLK INS
