ID   CETP_HUMAN              Reviewed;         493 AA.
AC   P11597; Q13987; Q13988; Q53YZ1;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   02-SEP-2026, entry version 227.
DE   RecName: Full=Cholesteryl ester transfer protein {ECO:0000303|PubMed:3600759};
DE   AltName: Full=Lipid transfer protein I {ECO:0000312|MIM:118470};
DE   Flags: Precursor;
GN   Name=CETP {ECO:0000312|HGNC:HGNC:1869};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP   TISSUE SPECIFICITY, AND VARIANT ILE-422.
RX   PubMed=3600759; DOI=10.1038/327632a0;
RA   Drayna D., Jarnagin A.S., McLean J., Henzel W., Kohr W., Fielding C.,
RA   Lawn R.;
RT   "Cloning and sequencing of human cholesteryl ester transfer protein cDNA.";
RL   Nature 327:632-634(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2334701; DOI=10.1021/bi00458a004;
RA   Agellon L.B., Quinet E.M., Gillette T.G., Drayna D.T., Brown M.L.,
RA   Tall A.R.;
RT   "Organization of the human cholesteryl ester transfer protein gene.";
RL   Biochemistry 29:1372-1376(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-422.
RA   Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D.,
RA   Toth E.J., Nickerson D.A.;
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-422.
RC   TISSUE=Pancreas, and Spleen;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RX   PubMed=8943225; DOI=10.1074/jbc.271.50.31831;
RA   Oliveira C.F.O., Chouinard R.A., Agellon L.B., Bruce C., Ma L., Walsh A.,
RA   Breslow J.L., Tall A.R.;
RT   "Human cholesteryl ester transfer protein gene proximal promoter contains
RT   dietary cholesterol positive responsive elements and mediates expression in
RT   small intestine and periphery while predominant liver and spleen expression
RT   is controlled by 5'-distal sequences. Cis-acting sequences mapped in
RT   transgenic mice.";
RL   J. Biol. Chem. 271:31831-31838(1996).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX   PubMed=9332354; DOI=10.1016/s0378-1119(97)00247-3;
RA   Williams S., Hayes L., Elsenboss L., Williams A., Andre C., Abramson R.,
RA   Thompson J.F., Milos P.M.;
RT   "Sequencing of the cholesteryl ester transfer protein 5' regulatory region
RT   using artificial transposons.";
RL   Gene 197:101-107(1997).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-493 (ISOFORM 2), AND VARIANT ILE-422.
RC   TISSUE=Liver;
RA   Dinchuk J.E., Hart J.T., Wirak D.O.;
RL   Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=3281933; DOI=10.1016/s0021-9258(18)60670-2;
RA   Hesler C.B., Tall A.R., Swenson T.L., Weech P.K., Marcel Y.L., Milne R.W.;
RT   "Monoclonal antibodies to the Mr 74,000 cholesteryl ester transfer protein
RT   neutralize all of the cholesteryl ester and triglyceride transfer
RT   activities in human plasma.";
RL   J. Biol. Chem. 263:5020-5023(1988).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-257 AND ASN-358.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [10]
RP   INVOLVEMENT IN HDLCQ10, AND POLYMORPHISM.
RX   PubMed=17952847; DOI=10.1086/522497;
RA   Spirin V., Schmidt S., Pertsemlidis A., Cooper R.S., Cohen J.C.,
RA   Sunyaev S.R.;
RT   "Common single-nucleotide polymorphisms act in concert to affect plasma
RT   levels of high-density lipoprotein cholesterol.";
RL   Am. J. Hum. Genet. 81:1298-1303(2007).
RN   [11]
RP   GLYCOSYLATION AT ASN-105.
RX   PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA   Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA   Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core fucosylated
RT   glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [12]
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).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 19-493 IN COMPLEX WITH LIPID,
RP   FUNCTION, DISULFIDE BOND, AND MUTAGENESIS OF THR-155; VAL-215; ARG-218;
RP   SER-247; PHE-282; PHE-287; PHE-309; LEU-313; TYR-392; LEU-399 AND VAL-433.
RX   PubMed=17237796; DOI=10.1038/nsmb1197;
RA   Qiu X., Mistry A., Ammirati M.J., Chrunyk B.A., Clark R.W., Cong Y.,
RA   Culp J.S., Danley D.E., Freeman T.B., Geoghegan K.F., Griffor M.C.,
RA   Hawrylik S.J., Hayward C.M., Hensley P., Hoth L.R., Karam G.A., Lira M.E.,
RA   Lloyd D.B., McGrath K.M., Stutzman-Engwall K.J., Subashi A.K.,
RA   Subashi T.A., Thompson J.F., Wang I.-K., Zhao H., Seddon A.P.;
RT   "Crystal structure of cholesteryl ester transfer protein reveals a long
RT   tunnel and four bound lipid molecules.";
RL   Nat. Struct. Mol. Biol. 14:106-113(2007).
RN   [14]
RP   INVOLVEMENT IN HALP1.
RX   PubMed=2215607; DOI=10.1056/nejm199011013231803;
RA   Inazu A., Brown M.L., Hesler C.B., Agellon L.B., Koizumi J., Takata K.,
RA   Maruhama Y., Mabuchi H., Tall A.R.;
RT   "Increased high-density lipoprotein levels caused by a common cholesteryl-
RT   ester transfer protein gene mutation.";
RL   N. Engl. J. Med. 323:1234-1238(1990).
RN   [15]
RP   VARIANT HALP1 GLY-459.
RX   PubMed=8408659; DOI=10.1172/jci116802;
RA   Takahashi K., Jiang X.-C., Sakai N., Yamashita S., Hirano K., Bujo H.,
RA   Yamazaki H., Kusunoki J., Miura T., Kussie P., Matsuzawa Y., Saito Y.,
RA   Tall A.;
RT   "A missense mutation in the cholesteryl ester transfer protein gene with
RT   possible dominant effects on plasma high density lipoproteins.";
RL   J. Clin. Invest. 92:2060-2064(1993).
RN   [16]
RP   VARIANTS SER-331; PRO-390; ILE-422 AND MET-486.
RX   PubMed=10391209; DOI=10.1038/10290;
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RT   "Characterization of single-nucleotide polymorphisms in coding regions of
RT   human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [17]
RP   ERRATUM OF PUBMED:10391209.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
RN   [18]
RP   VARIANTS HALP1 PRO-168 AND CYS-299, AND CHARACTERIZATION OF VARIANTS HALP1
RP   PRO-168 AND CYS-299.
RX   PubMed=12091484; DOI=10.1194/jlr.m200024-jlr200;
RA   Nagano M., Yamashita S., Hirano K., Ito M., Maruyama T., Ishihara M.,
RA   Sagehashi Y., Oka T., Kujiraoka T., Hattori H., Nakajima N., Egashira T.,
RA   Kondo M., Sakai N., Matsuzawa Y.;
RT   "Two novel missense mutations in the CETP gene in Japanese
RT   hyperalphalipoproteinemic subjects: high-throughput assay by Invader
RT   assay.";
RL   J. Lipid Res. 43:1011-1018(2002).
RN   [19]
RP   VARIANTS GLY-15; MET-385; PRO-390; ILE-422 AND GLN-468.
RX   PubMed=12966036; DOI=10.1093/hmg/ddg314;
RA   Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
RA   Alvin G.B., Das K., Gilliam T.C.;
RT   "Association of extreme blood lipid profile phenotypic variation with 11
RT   reverse cholesterol transport genes and 10 non-genetic cardiovascular
RT   disease risk factors.";
RL   Hum. Mol. Genet. 12:2733-2743(2003).
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, PubMed:3281933, PubMed:3600759).
CC       Regulates the reverse cholesterol transport, by which excess
CC       cholesterol is removed from peripheral tissues and returned to the
CC       liver for elimination (PubMed:17237796). {ECO:0000269|PubMed:24293641,
CC       ECO:0000269|PubMed:3281933, ECO:0000303|PubMed:17237796,
CC       ECO:0000305|PubMed:3600759}.
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, ECO:0000269|PubMed:3281933};
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:0000269|PubMed:3281933};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24293641,
CC       ECO:0000269|PubMed:3281933}. Note=Secreted in plasma.
CC       {ECO:0000269|PubMed:3281933}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P11597-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P11597-2; Sequence=VSP_023645;
CC   -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC       {ECO:0000269|PubMed:3281933}.
CC   -!- POLYMORPHISM: Genetic variations in CETP define the high density
CC       lipoprotein cholesterol level quantitative trait locus 10 (HDLCQ10)
CC       [MIM:143470]. {ECO:0000269|PubMed:17952847}.
CC   -!- DISEASE: Hyperalphalipoproteinemia 1 (HALP1) [MIM:143470]: A condition
CC       characterized by high levels of high density lipoprotein (HDL) and
CC       increased HDL cholesterol levels. {ECO:0000269|PubMed:12091484,
CC       ECO:0000269|PubMed:2215607, ECO:0000269|PubMed:8408659}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Cholesterylester transfer protein
CC       entry;
CC       URL="https://en.wikipedia.org/wiki/Cholesterylester_transfer_protein";
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DR   EMBL; M30185; AAA51977.1; -; mRNA.
DR   EMBL; M32998; AAA51978.1; -; Genomic_DNA.
DR   EMBL; M32992; AAA51978.1; JOINED; Genomic_DNA.
DR   EMBL; M32993; AAA51978.1; JOINED; Genomic_DNA.
DR   EMBL; M32994; AAA51978.1; JOINED; Genomic_DNA.
DR   EMBL; M32995; AAA51978.1; JOINED; Genomic_DNA.
DR   EMBL; M32996; AAA51978.1; JOINED; Genomic_DNA.
DR   EMBL; M32997; AAA51978.1; JOINED; Genomic_DNA.
DR   EMBL; AY422211; AAR03500.1; -; Genomic_DNA.
DR   EMBL; BC025739; AAH25739.1; -; mRNA.
DR   EMBL; U71187; AAD14876.1; -; Genomic_DNA.
DR   EMBL; AF027656; AAB86604.1; -; Genomic_DNA.
DR   EMBL; M83573; AAB59388.1; -; mRNA.
DR   CCDS; CCDS10772.1; -. [P11597-1]
DR   CCDS; CCDS67032.1; -. [P11597-2]
DR   PIR; A26941; A26941.
DR   RefSeq; NP_000069.2; NM_000078.3. [P11597-1]
DR   RefSeq; NP_001273014.1; NM_001286085.2. [P11597-2]
DR   PDB; 2OBD; X-ray; 2.10 A; A=18-493.
DR   PDB; 4EWS; X-ray; 2.59 A; A=18-493.
DR   PDB; 4F2A; X-ray; 3.11 A; A=18-493.
DR   AlphaFoldDB; P11597; -.
DR   SMR; P11597; -.
DR   BioGRID; 107498; 3.
DR   FunCoup; P11597; 22.
DR   IntAct; P11597; 5.
DR   NDEx; IQUERY-CP-CETP; 9 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000200676; -.
DR   BindingDB; P11597; -.
DR   ChEMBL; CHEMBL3572; -.
DR   DrugBank; DB06630; Anacetrapib.
DR   DrugBank; DB12181; Dalcetrapib.
DR   DrugBank; DB11655; Evacetrapib.
DR   DrugBank; DB14890; Obicetrapib.
DR   DrugBank; DB06281; Torcetrapib.
DR   GuidetoPHARMACOLOGY; 3248; -.
DR   SwissLipids; SLP:000000472; -.
DR   TCDB; 1.C.40.1.8; the bactericidal permeability increasing protein (bpip) family.
DR   GlyConnect; P11597; 8 N-Linked glycans (2 sites).
DR   GlyCosmos; P11597; 5 sites, 9 glycans.
DR   GlyGen; P11597; 5 sites, 14 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P11597; -.
DR   PhosphoSitePlus; P11597; -.
DR   SwissPalm; P11597; -.
DR   BioMuta; CETP; -.
DR   DMDM; 71153497; -.
DR   MassIVE; P11597; -.
DR   PaxDb; 9606-ENSP00000200676; -.
DR   PeptideAtlas; P11597; -.
DR   ProteomicsDB; 52795; -. [P11597-1]
DR   ProteomicsDB; 52796; -. [P11597-2]
DR   Antibodypedia; 28719; 446 antibodies from 38 providers.
DR   DNASU; 1071; -.
DR   Ensembl; ENST00000200676.8; ENSP00000200676.3; ENSG00000087237.13. [P11597-1]
DR   Ensembl; ENST00000379780.6; ENSP00000369106.2; ENSG00000087237.13. [P11597-2]
DR   GeneID; 1071; -.
DR   KEGG; hsa:1071; -.
DR   MANE-Select; ENST00000200676.8; ENSP00000200676.3; NM_000078.3; NP_000069.2.
DR   UCSC; uc002eki.3; human. [P11597-1]
DR   AGR; HGNC:1869; -.
DR   ClinPGx; PA108; -.
DR   CTD; 1071; -.
DR   DisGeNET; 1071; -.
DR   GeneCards; CETP; -.
DR   GeneReviews; CETP; -.
DR   HGNC; HGNC:1869; CETP.
DR   HPA; ENSG00000087237; Group enriched (adipose tissue, liver, lymphoid tissue, placenta).
DR   MalaCards; CETP; -.
DR   MIM; 118470; gene.
DR   MIM; 143470; phenotype.
DR   OpenTargets; ENSG00000087237; -.
DR   Orphanet; 181428; Familial Hyperalphalipoproteinemia.
DR   VEuPathDB; HostDB:ENSG00000087237; -.
DR   eggNOG; KOG4160; Eukaryota.
DR   GeneTree; ENSGT01100000263546; -.
DR   HOGENOM; CLU_043151_0_0_1; -.
DR   InParanoid; P11597; -.
DR   OMA; WFSDHVL; -.
DR   OrthoDB; 9940758at2759; -.
DR   PAN-GO; P11597; 15 GO annotations based on evolutionary models.
DR   PhylomeDB; P11597; -.
DR   PathwayCommons; P11597; -.
DR   Reactome; R-HSA-8964041; LDL remodeling.
DR   Reactome; R-HSA-8964058; HDL remodeling.
DR   Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR   SignaLink; P11597; -.
DR   SIGNOR; P11597; -.
DR   Agora; ENSG00000087237; Agora Nominated Target for Alzheimer's Disease.
DR   BioGRID-ORCS; 1071; 15 hits in 1148 CRISPR screens.
DR   EvolutionaryTrace; P11597; -.
DR   GeneWiki; Cholesterylester_transfer_protein; -.
DR   GenomeRNAi; 1071; -.
DR   Pharos; P11597; Tchem.
DR   PRO; PR:P11597; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P11597; protein.
DR   Bgee; ENSG00000087237; Expressed in lymph node and 101 other cell types or tissues.
DR   ExpressionAtlas; P11597; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
DR   GO; GO:0031982; C:vesicle; IDA:BHF-UCL.
DR   GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
DR   GO; GO:0120020; F:cholesterol transfer activity; IDA:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IDA:BHF-UCL.
DR   GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
DR   GO; GO:0120014; F:phospholipid transfer activity; IDA:BHF-UCL.
DR   GO; GO:0017129; F:triglyceride binding; IDA:BHF-UCL.
DR   GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
DR   GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
DR   GO; GO:0030301; P:cholesterol transport; IDA:UniProtKB.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:UniProtKB.
DR   GO; GO:0055088; P:lipid homeostasis; IDA:BHF-UCL.
DR   GO; GO:0006869; P:lipid transport; IDA:BHF-UCL.
DR   GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:BHF-UCL.
DR   GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IC:BHF-UCL.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:BHF-UCL.
DR   GO; GO:0055091; P:phospholipid homeostasis; IDA:BHF-UCL.
DR   GO; GO:0032376; P:positive regulation of cholesterol transport; IDA:BHF-UCL.
DR   GO; GO:2001140; P:positive regulation of phospholipid transport; IDA:BHF-UCL.
DR   GO; GO:0010874; P:regulation of cholesterol efflux; IMP:BHF-UCL.
DR   GO; GO:0043691; P:reverse cholesterol transport; IC:BHF-UCL.
DR   GO; GO:0070328; P:triglyceride homeostasis; IDA:BHF-UCL.
DR   GO; GO:0006641; P:triglyceride metabolic process; IDA:BHF-UCL.
DR   GO; GO:0034197; P:triglyceride transport; IDA:UniProtKB.
DR   GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:UniProtKB.
DR   CDD; cd00025; BPI1; 1.
DR   FunFam; 3.15.10.10:FF:000002; Cholesteryl ester transfer protein; 1.
DR   FunFam; 3.15.20.10:FF:000002; Cholesteryl ester transfer protein; 1.
DR   Gene3D; 3.15.10.10; Bactericidal permeability-increasing protein, domain 1; 1.
DR   Gene3D; 3.15.20.10; Bactericidal permeability-increasing protein, domain 2; 1.
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; CHOLESTERYL ESTER TRANSFER PROTEIN; 1.
DR   PANTHER; PTHR47616:SF1; CHOLESTERYL ESTER TRANSFER PROTEIN; 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; Bactericidal permeability-increasing protein, BPI; 2.
DR   PROSITE; PS00400; LBP_BPI_CETP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Atherosclerosis;
KW   Cholesterol metabolism; Direct protein sequencing; Disease variant;
KW   Disulfide bond; Glycoprotein; Lipid metabolism; Lipid transport;
KW   Proteomics identification; Reference proteome; Secreted; Signal;
KW   Steroid metabolism; Sterol metabolism; Transport.
FT   SIGNAL          1..17
FT   CHAIN           18..493
FT                   /note="Cholesteryl ester transfer protein"
FT                   /id="PRO_0000017155"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19139490"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        160..201
FT                   /evidence="ECO:0000269|PubMed:17237796"
FT   VAR_SEQ         251..310
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.7"
FT                   /id="VSP_023645"
FT   VARIANT         15
FT                   /note="A -> G (in dbSNP:rs34065661)"
FT                   /evidence="ECO:0000269|PubMed:12966036"
FT                   /id="VAR_017018"
FT   VARIANT         154
FT                   /note="R -> W (in dbSNP:rs34716057)"
FT                   /id="VAR_033098"
FT   VARIANT         168
FT                   /note="L -> P (in HALP1; reduced secretion into plasma;
FT                   dbSNP:rs1329944838)"
FT                   /evidence="ECO:0000269|PubMed:12091484"
FT                   /id="VAR_033099"
FT   VARIANT         299
FT                   /note="R -> C (in HALP1; reduced secretion into plasma;
FT                   dbSNP:rs142459781)"
FT                   /evidence="ECO:0000269|PubMed:12091484"
FT                   /id="VAR_033100"
FT   VARIANT         331
FT                   /note="G -> S (in dbSNP:rs5881)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_013919"
FT   VARIANT         385
FT                   /note="V -> M (in dbSNP:rs34855278)"
FT                   /evidence="ECO:0000269|PubMed:12966036"
FT                   /id="VAR_017019"
FT   VARIANT         390
FT                   /note="A -> P (in dbSNP:rs5880)"
FT                   /evidence="ECO:0000269|PubMed:10391209,
FT                   ECO:0000269|PubMed:12966036"
FT                   /id="VAR_013920"
FT   VARIANT         422
FT                   /note="V -> I (in dbSNP:rs5882)"
FT                   /evidence="ECO:0000269|PubMed:10391209,
FT                   ECO:0000269|PubMed:12966036, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:3600759, ECO:0000269|Ref.3,
FT                   ECO:0000269|Ref.7"
FT                   /id="VAR_013921"
FT   VARIANT         455
FT                   /note="V -> M (in dbSNP:rs2228667)"
FT                   /id="VAR_031127"
FT   VARIANT         459
FT                   /note="D -> G (in HALP1; dbSNP:rs2303790)"
FT                   /evidence="ECO:0000269|PubMed:8408659"
FT                   /id="VAR_004172"
FT   VARIANT         468
FT                   /note="R -> Q (in dbSNP:rs1800777)"
FT                   /evidence="ECO:0000269|PubMed:12966036"
FT                   /id="VAR_013922"
FT   VARIANT         486
FT                   /note="V -> M (in dbSNP:rs5887)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_013923"
FT   MUTAGEN         155
FT                   /note="T->Y: Reduces triglyceride transfer and cholesteryl
FT                   ester transfer 5-fold."
FT                   /evidence="ECO:0000269|PubMed:17237796"
FT   MUTAGEN         215
FT                   /note="V->W: Reduces triglyceride transfer 10-fold. No
FT                   effect on cholesteryl ester transfer."
FT                   /evidence="ECO:0000269|PubMed:17237796"
FT   MUTAGEN         218
FT                   /note="R->S: Reduces triglyceride transfer 10-fold. Slight
FT                   reduction of cholesteryl ester transfer."
FT                   /evidence="ECO:0000269|PubMed:17237796"
FT   MUTAGEN         247
FT                   /note="S->A: Reduces triglyceride transfer 5-fold. Slight
FT                   reduction of cholesteryl ester transfer."
FT                   /evidence="ECO:0000269|PubMed:17237796"
FT   MUTAGEN         282
FT                   /note="F->R: Not secreted."
FT                   /evidence="ECO:0000269|PubMed:17237796"
FT   MUTAGEN         287
FT                   /note="F->R: Not secreted."
FT                   /evidence="ECO:0000269|PubMed:17237796"
FT   MUTAGEN         309
FT                   /note="F->D: Not secreted."
FT                   /evidence="ECO:0000269|PubMed:17237796"
FT   MUTAGEN         313
FT                   /note="L->Q: Reduces cholesteryl ester transfer by 60%."
FT                   /evidence="ECO:0000269|PubMed:17237796"
FT   MUTAGEN         392
FT                   /note="Y->S: Not secreted."
FT                   /evidence="ECO:0000269|PubMed:17237796"
FT   MUTAGEN         399
FT                   /note="L->W: Not secreted."
FT                   /evidence="ECO:0000269|PubMed:17237796"
FT   MUTAGEN         433
FT                   /note="V->R: Reduces activity by 60%."
FT                   /evidence="ECO:0000269|PubMed:17237796"
FT   STRAND          27..33
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           34..40
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           41..43
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           44..54
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          60..66
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   TURN            67..69
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          70..94
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   TURN            95..97
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          98..120
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          128..149
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          152..171
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:4EWS"
FT   HELIX           180..183
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           184..188
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           189..222
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          228..231
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          234..236
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          242..249
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          252..255
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           262..265
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           269..271
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          274..283
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           284..296
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          300..304
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           306..315
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           323..325
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           326..329
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           333..335
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          337..344
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          347..351
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          354..367
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           372..374
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          378..393
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          396..416
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           420..429
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           430..434
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           435..451
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   TURN            452..454
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           455..457
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          458..468
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   STRAND          471..479
FT                   /evidence="ECO:0007829|PDB:2OBD"
FT   HELIX           482..490
FT                   /evidence="ECO:0007829|PDB:2OBD"
SQ   SEQUENCE   493 AA;  54756 MW;  CD7762766A9B062E CRC64;
     MLAATVLTLA LLGNAHACSK GTSHEAGIVC RITKPALLVL NHETAKVIQT AFQRASYPDI
     TGEKAMMLLG QVKYGLHNIQ ISHLSIASSQ VELVEAKSID VSIQNVSVVF KGTLKYGYTT
     AWWLGIDQSI DFEIDSAIDL QINTQLTCDS GRVRTDAPDC YLSFHKLLLH LQGEREPGWI
     KQLFTNFISF TLKLVLKGQI CKEINVISNI MADFVQTRAA SILSDGDIGV DISLTGDPVI
     TASYLESHHK GHFIYKNVSE DLPLPTFSPT LLGDSRMLYF WFSERVFHSL AKVAFQDGRL
     MLSLMGDEFK AVLETWGFNT NQEIFQEVVG GFPSQAQVTV HCLKMPKISC QNKGVVVNSS
     VMVKFLFPRP DQQHSVAYTF EEDIVTTVQA SYSKKKLFLS LLDFQITPKT VSNLTESSSE
     SVQSFLQSMI TAVGIPEVMS RLEVVFTALM NSKGVSLFDI INPEIITRDG FLLLQMDFGF
     PEHLLVDFLQ SLS
//