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Q8BWP5 (TTPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-tocopherol transfer protein

Short name=Alpha-TTP
Gene names
Name:Ttpa
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Subunit structure

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

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Contains 1 CRAL-TRIO domain.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
   LigandLipid-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processembryonic placenta development

Inferred from mutant phenotype PubMed 16014812. Source: MGI

intermembrane transport

Inferred from direct assay Ref.3. Source: UniProtKB

intracellular pH reduction

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell death

Inferred from electronic annotation. Source: Ensembl

negative regulation of establishment of blood-brain barrier

Inferred from mutant phenotype PubMed 19923370. Source: BHF-UCL

placenta development

Inferred from mutant phenotype PubMed 11076932. Source: MGI

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to pH

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from mutant phenotype PubMed 19923370. Source: BHF-UCL

vitamin E metabolic process

Inferred from mutant phenotype PubMed 19923370. Source: BHF-UCL

vitamin transport

Inferred from direct assay Ref.3. Source: UniProtKB

   Cellular_componentcytoplasm

Traceable author statement PubMed 11076932PubMed 11095717. Source: MGI

cytosol

Inferred from electronic annotation. Source: Ensembl

late endosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionphosphatidylinositol-3,4-bisphosphate binding

Inferred from direct assay Ref.3. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate binding

Inferred from direct assay Ref.3. Source: UniProtKB

transporter activity

Inferred from electronic annotation. Source: InterPro

vitamin E binding

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 278278Alpha-tocopherol transfer protein
PRO_0000210765

Regions

Domain88 – 253166CRAL-TRIO

Sites

Binding site1901Phosphatidylinositol lipid headgroup
Binding site1921Phosphatidylinositol lipid headgroup
Binding site2171Phosphatidylinositol lipid headgroup
Binding site2211Phosphatidylinositol lipid headgroup

Experimental info

Mutagenesis591R → W: Abolishes binding to phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate. Ref.3
Mutagenesis2171K → A: Loss of tocopherol secretion (in vivo). No effect on tocopherol binding and intermembrane transfer (in vitro). Ref.3
Mutagenesis2211R → W: Loss of tocopherol secretion (in vivo). No effect on tocopherol binding and intermembrane transfer (in vitro). Ref.3

Secondary structure

..................................................... 278
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8BWP5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: BC913ADA7FB606D3

FASTA27832,014
        10         20         30         40         50         60 
MAEMRPGPLV GKQLNELPDH SPLLQPGLAE LRRRVQEAGV PQTPQPLTDA FLLRFLRARD 

        70         80         90        100        110        120 
FDLDLAWRLM KNYYKWRAEC PELSADLRPR SILGLLKAGY HGVLRSRDST GSRVLIYRIA 

       130        140        150        160        170        180 
YWDPKVFTAY DVFRVSLITS ELIVQEVETQ RNGVKAIFDL EGWQVSHAFQ ITPSVAKKIA 

       190        200        210        220        230        240 
AVLTDSFPLK VRGIHLINEP VIFHAVFSMI KPFLTEKIKD RIHLHGNNYK SSMLQHFPDI 

       250        260        270 
LPREYGGKEF SMEDICQEWT NFIMKSEDYL SSISETIQ 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[2]Fechner H.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-271.
Strain: C57BL/6.
[3]"Impaired alpha-TTP-PIPs interaction underlies familial vitamin E deficiency."
Kono N., Ohto U., Hiramatsu T., Urabe M., Uchida Y., Satow Y., Arai H.
Science 340:1106-1110(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 21-278 IN COMPLEXES WITH ALPHA-TOCOPHEROL; PHOSPHATIDYLINOSITOL-3,4-BISPHOSPHATE AND PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE, FUNCTION, SUBUNIT, MUTAGENESIS OF ARG-59; LYS-217 AND ARG-221.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK004882 mRNA. Translation: BAB23640.1.
AK050374 mRNA. Translation: BAC34218.1.
AF218416 mRNA. Translation: AAF25956.1.
CCDSCCDS17995.1.
RefSeqNP_056582.1. NM_015767.3.
UniGeneMm.24375.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3W67X-ray2.61A/B/C/D21-278[»]
3W68X-ray2.05A/B/C/D21-278[»]
ProteinModelPortalQ8BWP5.
SMRQ8BWP5. Positions 23-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BWP5. 1 interaction.
MINTMINT-1869030.

PTM databases

PhosphoSiteQ8BWP5.

Proteomic databases

MaxQBQ8BWP5.
PaxDbQ8BWP5.
PRIDEQ8BWP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000098244; ENSMUSP00000095845; ENSMUSG00000073988.
GeneID50500.
KEGGmmu:50500.
UCSCuc008sci.1. mouse.

Organism-specific databases

CTD7274.
MGIMGI:1354168. Ttpa.

Phylogenomic databases

eggNOGNOG250577.
GeneTreeENSGT00550000074253.
HOVERGENHBG018009.
InParanoidQ8BWP5.
OMAHLINEPI.
PhylomeDBQ8BWP5.

Gene expression databases

ArrayExpressQ8BWP5.
BgeeQ8BWP5.
CleanExMM_TTPA.
GenevestigatorQ8BWP5.

Family and domain databases

Gene3D3.40.525.10. 1 hit.
InterProIPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
[Graphical view]
PfamPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]
PRINTSPR00180. CRETINALDHBP.
SMARTSM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEPS50191. CRAL_TRIO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio307498.
PROQ8BWP5.
SOURCESearch...

Entry information

Entry nameTTPA_MOUSE
AccessionPrimary (citable) accession number: Q8BWP5
Secondary accession number(s): Q9CW51, Q9JL07
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot