P22687 · CETP_RABIT
- ProteinCholesteryl ester transfer protein
- GeneCETP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids497 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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:24293641).
Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination (By similarity).
Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination (By similarity).
Catalytic activity
- cholesteryl (9Z-octadecenoate)(in) = cholesteryl (9Z-octadecenoate)(out)
- 1,2,3-tri-(9Z-octadecenoyl)-glycerol(in) = 1,2,3-tri-(9Z-octadecenoyl)-glycerol(out)
- cholesteryl (9Z,12Z)-octadecadienoate(in) = cholesteryl (9Z,12Z)-octadecadienoate(out)
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Cellular Component | high-density lipoprotein particle | |
Molecular Function | cholesterol binding | |
Molecular Function | cholesterol transfer activity | |
Molecular Function | phosphatidylcholine binding | |
Molecular Function | phospholipid transporter activity | |
Molecular Function | triglyceride binding | |
Biological Process | cholesterol homeostasis | |
Biological Process | cholesterol metabolic process | |
Biological Process | cholesterol transport | |
Biological Process | high-density lipoprotein particle remodeling | |
Biological Process | low-density lipoprotein particle remodeling | |
Biological Process | phosphatidylcholine metabolic process | |
Biological Process | phospholipid homeostasis | |
Biological Process | reverse cholesterol transport | |
Biological Process | triglyceride homeostasis | |
Biological Process | triglyceride metabolic process | |
Biological Process | triglyceride transport | |
Biological Process | very-low-density lipoprotein particle remodeling |
Keywords
- Biological process
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameCholesteryl ester transfer protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionP22687
Proteomes
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1 | |||||
Sequence: A | ||||||
Chain | PRO_0000017157 | 2-497 | Cholesteryl ester transfer protein | |||
Sequence: CPKGASYEAGIVCRITKPALLVLNQETAKVVQTAFQRAGYPDVSGERAVMLLGRVKYGLHNLQISHLSIASSQVELVDAKTIDVAIQNVSVVFKGTLNYSYTSAWGLGINQSVDFEIDSAIDLQINTELTCDAGSVRTNAPDCYLAFHKLLLHLQGEREPGWLKQLFTNFISFTLKLILKRQVCNEINTISNIMADFVQTRAASILSDGDIGVDISVTGAPVITATYLESHHKGHFTHKNVSEAFPLRAFPPGLLGDSRMLYFWFSDQVLNSLARAAFQEGRLVLSLTGDEFKKVLETQGFDTNQEIFQELSRGLPTGQAQVAVHCLKVPKISCQNRGVVVSSSVAVTFRFPRPDGREAVAYRFEEDIITTVQASYSQKKLFLHLLDFQCVPASGRAGSSANLSVALRTEAKAVSNLTESRSESLQSSLRSLIATVGIPEVMSRLEVAFTALMNSKGLDLFEIINPEIITLDGCLLLQMDFGFPKHLLVDFLQSLS | ||||||
Glycosylation | 89 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 99 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 111 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 144↔185 | |||||
Sequence: CYLAFHKLLLHLQGEREPGWLKQLFTNFISFTLKLILKRQVC | ||||||
Glycosylation | 241 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 403 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 417 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed by the liver.
Structure
Family & Domains
Sequence similarities
Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length497
- Mass (Da)54,514
- Last updated1991-08-01 v1
- ChecksumE82944E1821D0332
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: A |
Keywords
- Technical term