A8K6C1 · A8K6C1_HUMAN
- ProteinCholesteryl ester transfer protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids493 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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.
Catalytic activity
- 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)
- cholesteryl (9Z-octadecenoate)(in) = cholesteryl (9Z-octadecenoate)(out)
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | high-density lipoprotein particle | |
Molecular Function | cholesterol transfer activity | |
Molecular Function | lipid binding | |
Biological Process | cholesterol metabolic process | |
Biological Process | high-density lipoprotein particle remodeling | |
Biological Process | reverse cholesterol transport | |
Biological Process | triglyceride transport | |
Biological Process | very-low-density lipoprotein particle remodeling |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameCholesteryl ester transfer protein
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA8K6C1
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MLAATVLTLALLGNAHA | ||||||
Chain | PRO_5015219058 | 18-493 | Cholesteryl ester transfer protein | |||
Sequence: CSKGTSHEAGIVCRITKPALLVLNHETAKVIQTAFQRASYPDITGEKAMMLLGQVKYGLHNIQISHLSIASSQVELVEAKSIDVSIQNVSVVFKGTLKYGYTTAWWLGIDQSIDFEIDSAIDLQINTQLTCDSGRVRTDAPDCYLSFHKLLLHLQGEREPGWIKQLFTNFISFTLKLVLKGQICKEINVISNIMADFVQTRAASILSDGDIGVDISLTGDPVITAPYLESHHKGHFIYKNVSEDLPLPTFSPTLLGDSRMLYFWFSERVFHSLAKVAFQDGRLMLSLMGDEFKAVLETWGFNTNQEIFQEVVGGFPSQAQVTVHCLKMPKISCQNKGVVVNSSVMVKFLFPRPDQQHSVAYTFEEDIVTTVQASYSKKKLFLSLLDFQITPKTVSNLTESSSESIQSFLQSMITAVGIPEVMSRLEVVFTALMNSKGVSLFDIINPEIITRDGFLLLQMDFGFPEHLLVDFLQSLS | ||||||
Disulfide bond | 160↔201 | |||||
Sequence: CYLSFHKLLLHLQGEREPGWIKQLFTNFISFTLKLVLKGQIC |
Keywords
- PTM
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 31-258 | Lipid-binding serum glycoprotein N-terminal | ||||
Sequence: RITKPALLVLNHETAKVIQTAFQRASYPDITGEKAMMLLGQVKYGLHNIQISHLSIASSQVELVEAKSIDVSIQNVSVVFKGTLKYGYTTAWWLGIDQSIDFEIDSAIDLQINTQLTCDSGRVRTDAPDCYLSFHKLLLHLQGEREPGWIKQLFTNFISFTLKLVLKGQICKEINVISNIMADFVQTRAASILSDGDIGVDISLTGDPVITAPYLESHHKGHFIYKNV | ||||||
Domain | 272-476 | Lipid-binding serum glycoprotein C-terminal | ||||
Sequence: LGDSRMLYFWFSERVFHSLAKVAFQDGRLMLSLMGDEFKAVLETWGFNTNQEIFQEVVGGFPSQAQVTVHCLKMPKISCQNKGVVVNSSVMVKFLFPRPDQQHSVAYTFEEDIVTTVQASYSKKKLFLSLLDFQITPKTVSNLTESSSESIQSFLQSMITAVGIPEVMSRLEVVFTALMNSKGVSLFDIINPEIITRDGFLLLQM |
Sequence similarities
Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length493
- Mass (Da)54,780
- Last updated2007-12-04 v1
- Checksum16D47A02C99B07EC