CETP_MACFA
ID CETP_MACFA Reviewed; 493 AA.
AC P47896;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Cholesteryl ester transfer protein {ECO:0000303|PubMed:1931878};
DE AltName: Full=Lipid transfer protein I {ECO:0000305};
DE Flags: Precursor;
GN Name=CETP {ECO:0000303|PubMed:1931878};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=1931878; DOI=10.1161/01.atv.11.6.1759;
RA Pape M.E., Rehberg E.F., Marotti K.R., Melchior G.W.;
RT "Molecular cloning, sequence, and expression of cynomolgus monkey
RT cholesteryl ester transfer protein. Inverse correlation between hepatic
RT cholesteryl ester transfer protein mRNA levels and plasma high density
RT lipoprotein levels.";
RL Arterioscler. Thromb. 11:1759-1771(1991).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=24293641; DOI=10.1194/jlr.m043646;
RA Morton R.E., Izem L.;
RT "Cholesteryl ester transfer proteins from different species do not have
RT equivalent activities.";
RL J. Lipid Res. 55:258-265(2014).
CC -!- FUNCTION: Involved in the transfer of neutral lipids, including
CC cholesteryl ester and triglyceride, among lipoprotein particles. Allows
CC the net movement of cholesteryl ester from high density
CC lipoproteins/HDL to triglyceride-rich very low density
CC lipoproteins/VLDL, and the equimolar transport of triglyceride from
CC VLDL to HDL (PubMed:24293641). Regulates the reverse cholesterol
CC transport, by which excess cholesterol is removed from peripheral
CC tissues and returned to the liver for elimination (By similarity).
CC {ECO:0000250|UniProtKB:P11597, ECO:0000269|PubMed:24293641}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl (9Z-octadecenoate)(in) = cholesteryl (9Z-
CC octadecenoate)(out); Xref=Rhea:RHEA:43348, ChEBI:CHEBI:46898;
CC Evidence={ECO:0000269|PubMed:24293641};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol(in) = 1,2,3-tri-(9Z-
CC octadecenoyl)-glycerol(out); Xref=Rhea:RHEA:43352, ChEBI:CHEBI:53753;
CC Evidence={ECO:0000269|PubMed:24293641};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl (9Z,12Z)-octadecadienoate(in) = cholesteryl
CC (9Z,12Z)-octadecadienoate(out); Xref=Rhea:RHEA:43356,
CC ChEBI:CHEBI:41509; Evidence={ECO:0000250|UniProtKB:P11597};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24293641,
CC ECO:0000303|PubMed:1931878}. Note=Secreted in plasma.
CC {ECO:0000303|PubMed:1931878}.
CC -!- TISSUE SPECIFICITY: Probably primarily expressed in liver and adipose
CC tissues. Detected in adrenal gland, mesenteric fat, spleen and aorta.
CC {ECO:0000269|PubMed:1931878}.
CC -!- INDUCTION: Up-regulated by high-fat, high-cholesterol diet.
CC {ECO:0000269|PubMed:1931878}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
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DR EMBL; M86343; AAA36840.1; -; mRNA.
DR PIR; A53176; A53176.
DR AlphaFoldDB; P47896; -.
DR SMR; P47896; -.
DR STRING; 9541.XP_005592063.1; -.
DR SwissLipids; SLP:000000486; -.
DR eggNOG; KOG4160; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:InterPro.
DR GO; GO:0120020; F:cholesterol transfer activity; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030301; P:cholesterol transport; IDA:UniProtKB.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:UniProtKB.
DR GO; GO:0043691; P:reverse cholesterol transport; IEA:InterPro.
DR GO; GO:0034197; P:triglyceride transport; IDA:UniProtKB.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:UniProtKB.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR017130; Cholesteryl_ester_transfer.
DR InterPro; IPR001124; Lipid-bd_serum_glycop_C.
DR InterPro; IPR017954; Lipid-bd_serum_glycop_CS.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR PANTHER; PTHR47616; PTHR47616; 1.
DR Pfam; PF01273; LBP_BPI_CETP; 1.
DR Pfam; PF02886; LBP_BPI_CETP_C; 1.
DR PIRSF; PIRSF037185; Cholesteryl_ester_transf; 1.
DR SMART; SM00328; BPI1; 1.
DR SMART; SM00329; BPI2; 1.
DR SUPFAM; SSF55394; SSF55394; 2.
DR PROSITE; PS00400; LBP_BPI_CETP; 1.
PE 1: Evidence at protein level;
KW Cholesterol metabolism; Disulfide bond; Glycoprotein; Lipid metabolism;
KW Lipid transport; Reference proteome; Secreted; Signal; Steroid metabolism;
KW Sterol metabolism; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..493
FT /note="Cholesteryl ester transfer protein"
FT /id="PRO_0000017156"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..201
FT /evidence="ECO:0000250|UniProtKB:P11597"
SQ SEQUENCE 493 AA; 54743 MW; 7E82BE3C2A8FAE0D CRC64;
MLAATVLTLA LLGNVHACSK GTSHKAGIVC RITKPALLVL NQETAKVIQS AFQRANYPNI
TGEKAMMLLG QVKYGLHNIQ ISHLSIASSR VELVEAKSID VSIQNVSVVF KGTLKYGYTT
AWGLGIDQSV DFEIDSAIDL QINTQLTCDS GRVRTDAPDC YLSFHKLLLH LQGEREPGWI
KQLFTNFISF TLKLVLKGQI CKEINIISNI MADFVQTRAA SILSDGDIGV DISLTGDPII
TASYLESHHK GYFIYKNVSE DLPLPTFSPA LLGDSRMLYF WFSEQVFHSL AKVAFQDGRL
MLSLMGDEFK AVLETWGFNT NQEIFQEVVG GFPSQAQVTV HCLKMPRISC QNKGVVVNSS
VMVKFLFPRP DQQHSVAYTF EEDIMTTVQA SYSKKKLFLS LLDFQITPKT VSNLTESSSE
SVQSFLQSMI TTVGIPEVMS RLEAVFTALM NSKGLSLFDI INPEIITRDG FLLLQMDFGF
PEHLLVDFLQ SLS
