P49638 · TTPA_HUMAN
- ProteinAlpha-tocopherol transfer protein
- GeneTTPA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids278 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds alpha-tocopherol, enhances its transfer between separate membranes, and stimulates its release from liver cells (PubMed:7887897).
Binds both phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate; the resulting conformation change is important for the release of the bound alpha-tocopherol (By similarity).
Binds both phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate; the resulting conformation change is important for the release of the bound alpha-tocopherol (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 185 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 187 | +-alpha-tocopherol (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 190-192 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: KVR | ||||||
Binding site | 208-211 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: SMIK | ||||||
Binding site | 217 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 221 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | late endosome | |
Molecular Function | lipid transfer activity | |
Molecular Function | phosphatidylinositol bisphosphate binding | |
Molecular Function | phosphatidylinositol-3,4-bisphosphate binding | |
Molecular Function | phosphatidylinositol-4,5-bisphosphate binding | |
Molecular Function | vitamin E binding | |
Biological Process | embryonic placenta development | |
Biological Process | intermembrane lipid transfer | |
Biological Process | lipid metabolic process | |
Biological Process | negative regulation of establishment of blood-brain barrier | |
Biological Process | positive regulation of amyloid-beta clearance | |
Biological Process | response to toxic substance | |
Biological Process | vitamin E metabolic process | |
Biological Process | vitamin transport |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-tocopherol transfer protein
- Short namesAlpha-TTP
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP49638
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Ataxia with vitamin E deficiency (AVED)
- Note
- DescriptionAn autosomal recessive disease characterized by undetectable or markedly reduced plasma levels of vitamin E, spinocerebellar degeneration, ataxia, areflexia and proprioception loss.
- See alsoMIM:277460
Natural variants in AVED
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_022388 | 59 | R>W | in AVED; dbSNP:rs397515522 | |
VAR_005668 | 101 | H>Q | in AVED; dbSNP:rs121917849 | |
VAR_022389 | 120 | A>T | in AVED; dbSNP:rs143010236 | |
VAR_022390 | 141 | E>K | in AVED; dbSNP:rs397515524 | |
VAR_007858 | 192 | R>H | in AVED; dbSNP:rs121917850 | |
VAR_022391 | 221 | R>W | in AVED; dbSNP:rs35916840 | |
VAR_022392 | 246 | G>R | in AVED; mild and slowly progressive form of the disease; dbSNP:rs397515526 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_022388 | 59 | in AVED; dbSNP:rs397515522 | |||
Sequence: R → W | ||||||
Natural variant | VAR_005668 | 101 | in AVED; dbSNP:rs121917849 | |||
Sequence: H → Q | ||||||
Natural variant | VAR_022389 | 120 | in AVED; dbSNP:rs143010236 | |||
Sequence: A → T | ||||||
Natural variant | VAR_022390 | 141 | in AVED; dbSNP:rs397515524 | |||
Sequence: E → K | ||||||
Natural variant | VAR_037973 | 172 | in dbSNP:rs34647756 | |||
Sequence: T → S | ||||||
Natural variant | VAR_007858 | 192 | in AVED; dbSNP:rs121917850 | |||
Sequence: R → H | ||||||
Natural variant | VAR_022391 | 221 | in AVED; dbSNP:rs35916840 | |||
Sequence: R → W | ||||||
Natural variant | VAR_022392 | 246 | in AVED; mild and slowly progressive form of the disease; dbSNP:rs397515526 | |||
Sequence: G → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 389 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000210764 | 1-278 | Alpha-tocopherol transfer protein | |||
Sequence: MAEARSQPSAGPQLNALPDHSPLLQPGLAALRRRAREAGVPLAPLPLTDSFLLRFLRARDFDLDLAWRLLKNYYKWRAECPEISADLHPRSIIGLLKAGYHGVLRSRDPTGSKVLIYRIAHWDPKVFTAYDVFRVSLITSELIVQEVETQRNGIKAIFDLEGWQFSHAFQITPSVAKKIAAVLTDSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNYKQSLLQHFPDILPLEYGGEEFSMEDICQEWTNFIMKSEDYLSSISESIQ |
Proteomic databases
PTM databases
Interaction
Subunit
Monomer and homotetramer. Phosphatidylinositol 4,5-bisphosphate binding induces the formation of homotetramers. Phosphatidylinositol 3,4-bisphosphate is less efficient in inducing tetramerization (By similarity).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MAEARSQPSAGPQLNALPDH | ||||||
Domain | 88-253 | CRAL-TRIO | ||||
Sequence: HPRSIIGLLKAGYHGVLRSRDPTGSKVLIYRIAHWDPKVFTAYDVFRVSLITSELIVQEVETQRNGIKAIFDLEGWQFSHAFQITPSVAKKIAAVLTDSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNYKQSLLQHFPDILPLEYGGEEFSME |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length278
- Mass (Da)31,750
- Last updated1996-02-01 v1
- Checksum64D1551CC155071E
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 271 | in Ref. 2; AAA64309 | ||||
Sequence: S → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D49488 EMBL· GenBank· DDBJ | BAA08449.1 EMBL· GenBank· DDBJ | mRNA | ||
U21938 EMBL· GenBank· DDBJ | AAA64309.1 EMBL· GenBank· DDBJ | mRNA | ||
BC058000 EMBL· GenBank· DDBJ | AAH58000.1 EMBL· GenBank· DDBJ | mRNA | ||
AH006950 EMBL· GenBank· DDBJ | AAC67490.1 EMBL· GenBank· DDBJ | Genomic DNA |