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Protein

Cholesteryl ester transfer protein

Gene

CETP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL to HDL (PubMed:3600759, PubMed:24293641). Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination (PubMed:17237796).1 Publication1 Publication1 Publication

GO - Molecular functioni

  • cholesterol binding Source: BHF-UCL
  • cholesterol transporter activity Source: UniProtKB
  • lipid binding Source: BHF-UCL
  • lipid transporter activity Source: BHF-UCL
  • phosphatidylcholine binding Source: BHF-UCL
  • phospholipid transporter activity Source: BHF-UCL
  • triglyceride binding Source: BHF-UCL

GO - Biological processi

  • cholesterol homeostasis Source: BHF-UCL
  • cholesterol metabolic process Source: BHF-UCL
  • cholesterol transport Source: UniProtKB
  • high-density lipoprotein particle remodeling Source: UniProtKB
  • lipid homeostasis Source: BHF-UCL
  • lipid transport Source: BHF-UCL
  • lipoprotein metabolic process Source: Reactome
  • low-density lipoprotein particle remodeling Source: BHF-UCL
  • negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  • phosphatidylcholine metabolic process Source: BHF-UCL
  • phospholipid homeostasis Source: BHF-UCL
  • phospholipid transport Source: BHF-UCL
  • receptor-mediated endocytosis Source: Reactome
  • regulation of cholesterol efflux Source: BHF-UCL
  • reverse cholesterol transport Source: BHF-UCL
  • triglyceride homeostasis Source: BHF-UCL
  • triglyceride metabolic process Source: BHF-UCL
  • triglyceride transport Source: UniProtKB
  • very-low-density lipoprotein particle remodeling Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Lipid transport, Steroid metabolism, Sterol metabolism, Transport

Enzyme and pathway databases

BioCyciZFISH:ENSG00000087237-MONOMER.
ReactomeiR-HSA-171052. LDL-mediated lipid transport.
R-HSA-194223. HDL-mediated lipid transport.
SIGNORiP11597.

Protein family/group databases

TCDBi1.C.40.1.8. the bactericidal permeability increasing protein (bpip) family.

Chemistry databases

SwissLipidsiSLP:000000472.

Names & Taxonomyi

Protein namesi
Recommended name:
Cholesteryl ester transfer protein1 Publication
Alternative name(s):
Lipid transfer protein IImported
Gene namesi
Name:CETPImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:1869. CETP.

Subcellular locationi

  • Secretedextracellular space 1 Publication

  • Note: Secreted in plasma.By similarity

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • high-density lipoprotein particle Source: BHF-UCL
  • vesicle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Hyperalphalipoproteinemia 1 (HALP1)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition characterized by high levels of high density lipoprotein (HDL) and increased HDL cholesterol levels.
See also OMIM:143470
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033099168L → P in HALP1; reduced secretion into plasma. 1 Publication1
Natural variantiVAR_033100299R → C in HALP1; reduced secretion into plasma. 1 PublicationCorresponds to variant rs142459781dbSNPEnsembl.1
Natural variantiVAR_004172459D → G in HALP1. 1 PublicationCorresponds to variant rs2303790dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi155T → Y: Reduces triglyceride transfer and cholesteryl ester transfer 5-fold. 1 Publication1
Mutagenesisi215V → W: Reduces triglyceride transfer 10-fold. No effect on cholesteryl ester transfer. 1 Publication1
Mutagenesisi218R → S: Reduces triglyceride transfer 10-fold. Slight reduction of cholesteryl ester transfer. 1 Publication1
Mutagenesisi247S → A: Reduces triglyceride transfer 5-fold. Slight reduction of cholesteryl ester transfer. 1 Publication1
Mutagenesisi282F → R: Not secreted. 1 Publication1
Mutagenesisi287F → R: Not secreted. 1 Publication1
Mutagenesisi309F → D: Not secreted. 1 Publication1
Mutagenesisi313L → Q: Reduces cholesteryl ester transfer by 60%. 1 Publication1
Mutagenesisi392Y → S: Not secreted. 1 Publication1
Mutagenesisi399L → W: Not secreted. 1 Publication1
Mutagenesisi433V → R: Reduces activity by 60%. 1 Publication1

Keywords - Diseasei

Atherosclerosis, Disease mutation

Organism-specific databases

DisGeNETi1071.
MalaCardsiCETP.
MIMi143470. phenotype.
OpenTargetsiENSG00000087237.
Orphaneti79506. Cholesterol-ester transfer protein deficiency.
PharmGKBiPA108.

Chemistry databases

ChEMBLiCHEMBL3572.

Polymorphism and mutation databases

BioMutaiCETP.
DMDMi71153497.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Add BLAST17
ChainiPRO_000001715518 – 493Cholesteryl ester transfer proteinAdd BLAST476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi105N-linked (GlcNAc...) (complex)1 Publication1
Disulfide bondi160 ↔ 2011 Publication
Glycosylationi257N-linked (GlcNAc...)1 Publication1
Glycosylationi358N-linked (GlcNAc...)1 Publication1
Glycosylationi413N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP11597.
PeptideAtlasiP11597.
PRIDEiP11597.

PTM databases

iPTMnetiP11597.
PhosphoSitePlusiP11597.
SwissPalmiP11597.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiENSG00000087237.
CleanExiHS_CETP.
ExpressionAtlasiP11597. baseline and differential.
GenevisibleiP11597. HS.

Interactioni

Protein-protein interaction databases

BioGridi107498. 2 interactors.
IntActiP11597. 3 interactors.
STRINGi9606.ENSP00000200676.

Chemistry databases

BindingDBiP11597.

Structurei

Secondary structure

1493
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 33Combined sources7
Helixi34 – 40Combined sources7
Helixi41 – 43Combined sources3
Helixi44 – 54Combined sources11
Beta strandi60 – 66Combined sources7
Turni67 – 69Combined sources3
Beta strandi70 – 94Combined sources25
Turni95 – 97Combined sources3
Beta strandi98 – 120Combined sources23
Helixi122 – 124Combined sources3
Beta strandi128 – 149Combined sources22
Beta strandi152 – 171Combined sources20
Helixi172 – 174Combined sources3
Helixi180 – 187Combined sources8
Helixi189 – 222Combined sources34
Beta strandi228 – 231Combined sources4
Beta strandi234 – 236Combined sources3
Beta strandi242 – 249Combined sources8
Beta strandi252 – 255Combined sources4
Helixi269 – 271Combined sources3
Beta strandi274 – 283Combined sources10
Helixi284 – 296Combined sources13
Beta strandi300 – 304Combined sources5
Helixi306 – 315Combined sources10
Helixi323 – 325Combined sources3
Helixi326 – 329Combined sources4
Helixi333 – 335Combined sources3
Beta strandi337 – 344Combined sources8
Beta strandi347 – 351Combined sources5
Beta strandi354 – 367Combined sources14
Helixi372 – 374Combined sources3
Beta strandi378 – 393Combined sources16
Beta strandi396 – 416Combined sources21
Helixi420 – 432Combined sources13
Helixi434 – 451Combined sources18
Turni452 – 454Combined sources3
Helixi455 – 457Combined sources3
Beta strandi458 – 468Combined sources11
Beta strandi471 – 479Combined sources9
Helixi482 – 490Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OBDX-ray2.10A18-493[»]
4EWSX-ray2.59A18-493[»]
4F2AX-ray3.11A18-493[»]
ProteinModelPortaliP11597.
SMRiP11597.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11597.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4160. Eukaryota.
ENOG410Z88E. LUCA.
GeneTreeiENSGT00390000008226.
HOGENOMiHOG000111553.
HOVERGENiHBG005310.
InParanoidiP11597.
KOiK16835.
OMAiFWFSERV.
OrthoDBiEOG091G08KX.
PhylomeDBiP11597.
TreeFamiTF333484.

Family and domain databases

InterProiIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR032942. BPI/LBP/Plunc.
IPR017130. Cholesteryl_ester_transfer.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PANTHERiPTHR10504. PTHR10504. 1 hit.
PTHR10504:SF12. PTHR10504:SF12. 1 hit.
PfamiPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF037185. Cholesteryl_ester_transf. 1 hit.
SMARTiSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMiSSF55394. SSF55394. 2 hits.
PROSITEiPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P11597-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLAATVLTLA LLGNAHACSK GTSHEAGIVC RITKPALLVL NHETAKVIQT
60 70 80 90 100
AFQRASYPDI TGEKAMMLLG QVKYGLHNIQ ISHLSIASSQ VELVEAKSID
110 120 130 140 150
VSIQNVSVVF KGTLKYGYTT AWWLGIDQSI DFEIDSAIDL QINTQLTCDS
160 170 180 190 200
GRVRTDAPDC YLSFHKLLLH LQGEREPGWI KQLFTNFISF TLKLVLKGQI
210 220 230 240 250
CKEINVISNI MADFVQTRAA SILSDGDIGV DISLTGDPVI TASYLESHHK
260 270 280 290 300
GHFIYKNVSE DLPLPTFSPT LLGDSRMLYF WFSERVFHSL AKVAFQDGRL
310 320 330 340 350
MLSLMGDEFK AVLETWGFNT NQEIFQEVVG GFPSQAQVTV HCLKMPKISC
360 370 380 390 400
QNKGVVVNSS VMVKFLFPRP DQQHSVAYTF EEDIVTTVQA SYSKKKLFLS
410 420 430 440 450
LLDFQITPKT VSNLTESSSE SVQSFLQSMI TAVGIPEVMS RLEVVFTALM
460 470 480 490
NSKGVSLFDI INPEIITRDG FLLLQMDFGF PEHLLVDFLQ SLS
Length:493
Mass (Da):54,756
Last modified:July 19, 2005 - v2
Checksum:iCD7762766A9B062E
GO
Isoform 2 (identifier: P11597-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     251-310: Missing.

Show »
Length:433
Mass (Da):47,787
Checksum:iED675FD1456F78F7
GO

Polymorphismi

Genetic variations in CETP define the high density lipoprotein cholesterol level quantitative trait locus 10 (HDLCQ10) [MIMi:143470].1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01701815A → G.1 PublicationCorresponds to variant rs34065661dbSNPEnsembl.1
Natural variantiVAR_033098154R → W.Corresponds to variant rs34716057dbSNPEnsembl.1
Natural variantiVAR_033099168L → P in HALP1; reduced secretion into plasma. 1 Publication1
Natural variantiVAR_033100299R → C in HALP1; reduced secretion into plasma. 1 PublicationCorresponds to variant rs142459781dbSNPEnsembl.1
Natural variantiVAR_013919331G → S.1 PublicationCorresponds to variant rs5881dbSNPEnsembl.1
Natural variantiVAR_017019385V → M.1 PublicationCorresponds to variant rs34855278dbSNPEnsembl.1
Natural variantiVAR_013920390A → P.2 PublicationsCorresponds to variant rs5880dbSNPEnsembl.1
Natural variantiVAR_013921422V → I.6 PublicationsCorresponds to variant rs5882dbSNPEnsembl.1
Natural variantiVAR_031127455V → M.Corresponds to variant rs2228667dbSNPEnsembl.1
Natural variantiVAR_004172459D → G in HALP1. 1 PublicationCorresponds to variant rs2303790dbSNPEnsembl.1
Natural variantiVAR_013922468R → Q.1 PublicationCorresponds to variant rs1800777dbSNPEnsembl.1
Natural variantiVAR_013923486V → M.1 PublicationCorresponds to variant rs5887dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_023645251 – 310Missing in isoform 2. 1 PublicationAdd BLAST60

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30185 mRNA. Translation: AAA51977.1.
M32998
, M32992, M32993, M32994, M32995, M32996, M32997 Genomic DNA. Translation: AAA51978.1.
AY422211 Genomic DNA. Translation: AAR03500.1.
BC025739 mRNA. Translation: AAH25739.1.
U71187 Genomic DNA. Translation: AAD14876.1.
AF027656 Genomic DNA. Translation: AAB86604.1.
M83573 mRNA. Translation: AAB59388.1.
CCDSiCCDS10772.1. [P11597-1]
CCDS67032.1. [P11597-2]
PIRiA26941.
RefSeqiNP_000069.2. NM_000078.2. [P11597-1]
UniGeneiHs.89538.

Genome annotation databases

EnsembliENST00000200676; ENSP00000200676; ENSG00000087237. [P11597-1]
ENST00000379780; ENSP00000369106; ENSG00000087237. [P11597-2]
GeneIDi1071.
KEGGihsa:1071.
UCSCiuc002eki.3. human. [P11597-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Cholesterylester transfer protein entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30185 mRNA. Translation: AAA51977.1.
M32998
, M32992, M32993, M32994, M32995, M32996, M32997 Genomic DNA. Translation: AAA51978.1.
AY422211 Genomic DNA. Translation: AAR03500.1.
BC025739 mRNA. Translation: AAH25739.1.
U71187 Genomic DNA. Translation: AAD14876.1.
AF027656 Genomic DNA. Translation: AAB86604.1.
M83573 mRNA. Translation: AAB59388.1.
CCDSiCCDS10772.1. [P11597-1]
CCDS67032.1. [P11597-2]
PIRiA26941.
RefSeqiNP_000069.2. NM_000078.2. [P11597-1]
UniGeneiHs.89538.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OBDX-ray2.10A18-493[»]
4EWSX-ray2.59A18-493[»]
4F2AX-ray3.11A18-493[»]
ProteinModelPortaliP11597.
SMRiP11597.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107498. 2 interactors.
IntActiP11597. 3 interactors.
STRINGi9606.ENSP00000200676.

Chemistry databases

BindingDBiP11597.
ChEMBLiCHEMBL3572.
SwissLipidsiSLP:000000472.

Protein family/group databases

TCDBi1.C.40.1.8. the bactericidal permeability increasing protein (bpip) family.

PTM databases

iPTMnetiP11597.
PhosphoSitePlusiP11597.
SwissPalmiP11597.

Polymorphism and mutation databases

BioMutaiCETP.
DMDMi71153497.

Proteomic databases

PaxDbiP11597.
PeptideAtlasiP11597.
PRIDEiP11597.

Protocols and materials databases

DNASUi1071.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000200676; ENSP00000200676; ENSG00000087237. [P11597-1]
ENST00000379780; ENSP00000369106; ENSG00000087237. [P11597-2]
GeneIDi1071.
KEGGihsa:1071.
UCSCiuc002eki.3. human. [P11597-1]

Organism-specific databases

CTDi1071.
DisGeNETi1071.
GeneCardsiCETP.
HGNCiHGNC:1869. CETP.
MalaCardsiCETP.
MIMi118470. gene.
143470. phenotype.
neXtProtiNX_P11597.
OpenTargetsiENSG00000087237.
Orphaneti79506. Cholesterol-ester transfer protein deficiency.
PharmGKBiPA108.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4160. Eukaryota.
ENOG410Z88E. LUCA.
GeneTreeiENSGT00390000008226.
HOGENOMiHOG000111553.
HOVERGENiHBG005310.
InParanoidiP11597.
KOiK16835.
OMAiFWFSERV.
OrthoDBiEOG091G08KX.
PhylomeDBiP11597.
TreeFamiTF333484.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000087237-MONOMER.
ReactomeiR-HSA-171052. LDL-mediated lipid transport.
R-HSA-194223. HDL-mediated lipid transport.
SIGNORiP11597.

Miscellaneous databases

EvolutionaryTraceiP11597.
GeneWikiiCholesterylester_transfer_protein.
GenomeRNAii1071.
PROiP11597.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000087237.
CleanExiHS_CETP.
ExpressionAtlasiP11597. baseline and differential.
GenevisibleiP11597. HS.

Family and domain databases

InterProiIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR032942. BPI/LBP/Plunc.
IPR017130. Cholesteryl_ester_transfer.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PANTHERiPTHR10504. PTHR10504. 1 hit.
PTHR10504:SF12. PTHR10504:SF12. 1 hit.
PfamiPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF037185. Cholesteryl_ester_transf. 1 hit.
SMARTiSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMiSSF55394. SSF55394. 2 hits.
PROSITEiPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCETP_HUMAN
AccessioniPrimary (citable) accession number: P11597
Secondary accession number(s): Q13987, Q13988, Q53YZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 19, 2005
Last modified: November 2, 2016
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.