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Protein

Alpha-tocopherol transfer protein

Gene

Ttpa

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds alpha-tocopherol, enhances its transfer between separate membranes, and stimulates its release from liver cells. Binds both phosphatidylinol 3,4-bisphosphate and phosphatidylinol 4,5-bisphosphate; the resulting conformation change is important for the release of the bound alpha-tocopherol.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei190Phosphatidylinositol lipid headgroup1
Binding sitei192Phosphatidylinositol lipid headgroup1
Binding sitei217Phosphatidylinositol lipid headgroup1
Binding sitei221Phosphatidylinositol lipid headgroup1

GO - Molecular functioni

  • phosphatidylinositol-3,4-bisphosphate binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • transporter activity Source: InterPro
  • vitamin E binding Source: UniProtKB

GO - Biological processi

  • embryonic placenta development Source: MGI
  • intermembrane transport Source: UniProtKB
  • intracellular pH reduction Source: Ensembl
  • negative regulation of cell death Source: Ensembl
  • negative regulation of establishment of blood-brain barrier Source: BHF-UCL
  • placenta development Source: MGI
  • response to nutrient Source: Ensembl
  • response to pH Source: Ensembl
  • response to toxic substance Source: BHF-UCL
  • vitamin E metabolic process Source: BHF-UCL
  • vitamin transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-tocopherol transfer protein
Short name:
Alpha-TTP
Gene namesi
Name:Ttpa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1354168. Ttpa.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Ensembl
  • late endosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi59R → W: Abolishes binding to phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate. 1 Publication1
Mutagenesisi217K → A: Loss of tocopherol secretion (in vivo). No effect on tocopherol binding and intermembrane transfer (in vitro). 1 Publication1
Mutagenesisi221R → W: Loss of tocopherol secretion (in vivo). No effect on tocopherol binding and intermembrane transfer (in vitro). 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002107651 – 278Alpha-tocopherol transfer proteinAdd BLAST278

Proteomic databases

MaxQBiQ8BWP5.
PaxDbiQ8BWP5.
PRIDEiQ8BWP5.

PTM databases

iPTMnetiQ8BWP5.
PhosphoSitePlusiQ8BWP5.

Expressioni

Gene expression databases

BgeeiENSMUSG00000073988.
CleanExiMM_TTPA.
ExpressionAtlasiQ8BWP5. baseline and differential.
GenevisibleiQ8BWP5. MM.

Interactioni

Subunit structurei

Monomer and homotetramer. Phosphatidylinol 4,5-bisphosphate binding induces the formation of homotetramers. Phosphatidylinol 3,4-bisphosphate is less efficient in inducing tetramerization.1 Publication

Protein-protein interaction databases

IntActiQ8BWP5. 1 interactor.
MINTiMINT-1869030.
STRINGi10090.ENSMUSP00000095845.

Structurei

Secondary structure

1278
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 38Combined sources11
Beta strandi43 – 45Combined sources3
Helixi49 – 58Combined sources10
Turni59 – 61Combined sources3
Helixi63 – 79Combined sources17
Helixi81 – 84Combined sources4
Helixi90 – 92Combined sources3
Helixi93 – 98Combined sources6
Beta strandi101 – 103Combined sources3
Beta strandi113 – 118Combined sources6
Helixi119 – 121Combined sources3
Turni124 – 126Combined sources3
Helixi129 – 143Combined sources15
Helixi147 – 152Combined sources6
Beta strandi154 – 159Combined sources6
Helixi165 – 169Combined sources5
Helixi173 – 183Combined sources11
Beta strandi186 – 189Combined sources4
Beta strandi191 – 198Combined sources8
Helixi202 – 210Combined sources9
Helixi211 – 213Combined sources3
Helixi216 – 219Combined sources4
Beta strandi222 – 224Combined sources3
Helixi230 – 236Combined sources7
Turni238 – 240Combined sources3
Helixi243 – 245Combined sources3
Helixi252 – 265Combined sources14
Helixi267 – 272Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3W67X-ray2.61A/B/C/D21-278[»]
3W68X-ray2.05A/B/C/D21-278[»]
ProteinModelPortaliQ8BWP5.
SMRiQ8BWP5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini88 – 253CRAL-TRIOPROSITE-ProRule annotationAdd BLAST166

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1471. Eukaryota.
ENOG410XRSQ. LUCA.
GeneTreeiENSGT00550000074253.
HOVERGENiHBG018009.
InParanoidiQ8BWP5.
OMAiTAYDAFR.
OrthoDBiEOG091G0KN0.
PhylomeDBiQ8BWP5.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
InterProiIPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
[Graphical view]
PfamiPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]
PRINTSiPR00180. CRETINALDHBP.
SMARTiSM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BWP5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEMRPGPLV GKQLNELPDH SPLLQPGLAE LRRRVQEAGV PQTPQPLTDA
60 70 80 90 100
FLLRFLRARD FDLDLAWRLM KNYYKWRAEC PELSADLRPR SILGLLKAGY
110 120 130 140 150
HGVLRSRDST GSRVLIYRIA YWDPKVFTAY DVFRVSLITS ELIVQEVETQ
160 170 180 190 200
RNGVKAIFDL EGWQVSHAFQ ITPSVAKKIA AVLTDSFPLK VRGIHLINEP
210 220 230 240 250
VIFHAVFSMI KPFLTEKIKD RIHLHGNNYK SSMLQHFPDI LPREYGGKEF
260 270
SMEDICQEWT NFIMKSEDYL SSISETIQ
Length:278
Mass (Da):32,014
Last modified:March 1, 2003 - v1
Checksum:iBC913ADA7FB606D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004882 mRNA. Translation: BAB23640.1.
AK050374 mRNA. Translation: BAC34218.1.
AF218416 mRNA. Translation: AAF25956.1.
CCDSiCCDS17995.1.
RefSeqiNP_056582.1. NM_015767.4.
UniGeneiMm.24375.

Genome annotation databases

EnsembliENSMUST00000098244; ENSMUSP00000095845; ENSMUSG00000073988.
GeneIDi50500.
KEGGimmu:50500.
UCSCiuc008sci.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004882 mRNA. Translation: BAB23640.1.
AK050374 mRNA. Translation: BAC34218.1.
AF218416 mRNA. Translation: AAF25956.1.
CCDSiCCDS17995.1.
RefSeqiNP_056582.1. NM_015767.4.
UniGeneiMm.24375.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3W67X-ray2.61A/B/C/D21-278[»]
3W68X-ray2.05A/B/C/D21-278[»]
ProteinModelPortaliQ8BWP5.
SMRiQ8BWP5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BWP5. 1 interactor.
MINTiMINT-1869030.
STRINGi10090.ENSMUSP00000095845.

PTM databases

iPTMnetiQ8BWP5.
PhosphoSitePlusiQ8BWP5.

Proteomic databases

MaxQBiQ8BWP5.
PaxDbiQ8BWP5.
PRIDEiQ8BWP5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098244; ENSMUSP00000095845; ENSMUSG00000073988.
GeneIDi50500.
KEGGimmu:50500.
UCSCiuc008sci.1. mouse.

Organism-specific databases

CTDi7274.
MGIiMGI:1354168. Ttpa.

Phylogenomic databases

eggNOGiKOG1471. Eukaryota.
ENOG410XRSQ. LUCA.
GeneTreeiENSGT00550000074253.
HOVERGENiHBG018009.
InParanoidiQ8BWP5.
OMAiTAYDAFR.
OrthoDBiEOG091G0KN0.
PhylomeDBiQ8BWP5.

Miscellaneous databases

PROiQ8BWP5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000073988.
CleanExiMM_TTPA.
ExpressionAtlasiQ8BWP5. baseline and differential.
GenevisibleiQ8BWP5. MM.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
InterProiIPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
[Graphical view]
PfamiPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]
PRINTSiPR00180. CRETINALDHBP.
SMARTiSM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTTPA_MOUSE
AccessioniPrimary (citable) accession number: Q8BWP5
Secondary accession number(s): Q9CW51, Q9JL07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.