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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei190 – 1901Phosphatidylinositol lipid headgroup
Binding sitei192 – 1921Phosphatidylinositol lipid headgroup
Binding sitei217 – 2171Phosphatidylinositol lipid headgroup
Binding sitei221 – 2211Phosphatidylinositol lipid headgroup

GO - Molecular functioni

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

GO - Biological processi

  1. embryonic placenta development Source: MGI
  2. intermembrane transport Source: UniProtKB
  3. intracellular pH reduction Source: Ensembl
  4. negative regulation of cell death Source: Ensembl
  5. negative regulation of establishment of blood-brain barrier Source: BHF-UCL
  6. placenta development Source: MGI
  7. response to nutrient Source: Ensembl
  8. response to pH Source: Ensembl
  9. response to toxic substance Source: BHF-UCL
  10. vitamin E metabolic process Source: BHF-UCL
  11. 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
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1354168. Ttpa.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Ensembl
  3. late endosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591R → W: Abolishes binding to phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate. 1 Publication
Mutagenesisi217 – 2171K → A: Loss of tocopherol secretion (in vivo). No effect on tocopherol binding and intermembrane transfer (in vitro). 1 Publication
Mutagenesisi221 – 2211R → W: Loss of tocopherol secretion (in vivo). No effect on tocopherol binding and intermembrane transfer (in vitro). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 278278Alpha-tocopherol transfer proteinPRO_0000210765Add
BLAST

Proteomic databases

MaxQBiQ8BWP5.
PaxDbiQ8BWP5.
PRIDEiQ8BWP5.

PTM databases

PhosphoSiteiQ8BWP5.

Expressioni

Gene expression databases

BgeeiQ8BWP5.
CleanExiMM_TTPA.
ExpressionAtlasiQ8BWP5. baseline and differential.
GenevestigatoriQ8BWP5.

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 interaction.
MINTiMINT-1869030.

Structurei

Secondary structure

1
278
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 3811Combined sources
Beta strandi43 – 453Combined sources
Helixi49 – 5810Combined sources
Turni59 – 613Combined sources
Helixi63 – 7917Combined sources
Helixi81 – 844Combined sources
Helixi90 – 923Combined sources
Helixi93 – 986Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi113 – 1186Combined sources
Helixi119 – 1213Combined sources
Turni124 – 1263Combined sources
Helixi129 – 14315Combined sources
Helixi147 – 1526Combined sources
Beta strandi154 – 1596Combined sources
Helixi165 – 1695Combined sources
Helixi173 – 18311Combined sources
Beta strandi186 – 1894Combined sources
Beta strandi191 – 1988Combined sources
Helixi202 – 2109Combined sources
Helixi211 – 2133Combined sources
Helixi216 – 2194Combined sources
Beta strandi222 – 2243Combined sources
Helixi230 – 2367Combined sources
Turni238 – 2403Combined sources
Helixi243 – 2453Combined sources
Helixi252 – 26514Combined sources
Helixi267 – 2726Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3W67X-ray2.61A/B/C/D21-278[»]
3W68X-ray2.05A/B/C/D21-278[»]
ProteinModelPortaliQ8BWP5.
SMRiQ8BWP5. Positions 23-275.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 253166CRAL-TRIOPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG250577.
GeneTreeiENSGT00550000074253.
HOVERGENiHBG018009.
InParanoidiQ8BWP5.
OMAiEYGGEEY.
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:February 28, 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_015767.3.
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_015767.3.
UniGeneiMm.24375.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3W67X-ray2.61A/B/C/D21-278[»]
3W68X-ray2.05A/B/C/D21-278[»]
ProteinModelPortaliQ8BWP5.
SMRiQ8BWP5. Positions 23-275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BWP5. 1 interaction.
MINTiMINT-1869030.

PTM databases

PhosphoSiteiQ8BWP5.

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

eggNOGiNOG250577.
GeneTreeiENSGT00550000074253.
HOVERGENiHBG018009.
InParanoidiQ8BWP5.
OMAiEYGGEEY.
PhylomeDBiQ8BWP5.

Miscellaneous databases

NextBioi307498.
PROiQ8BWP5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BWP5.
CleanExiMM_TTPA.
ExpressionAtlasiQ8BWP5. baseline and differential.
GenevestigatoriQ8BWP5.

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...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. Fechner H.
    Submitted (NOV-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(2012) [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.

Entry informationi

Entry nameiTTPA_MOUSE
AccessioniPrimary (citable) accession number: Q8BWP5
Secondary accession number(s): Q9CW51, Q9JL07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 25, 2005
Last sequence update: February 28, 2003
Last modified: January 6, 2015
This is version 92 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

External Data

Dasty 3

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 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.