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Q8BWP5

- TTPA_MOUSE

UniProt

Q8BWP5 - TTPA_MOUSE

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Protein
Alpha-tocopherol transfer protein
Gene
Ttpa
Organism
Mus musculus (Mouse)
Status
Reviewed - 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: 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 protein
PRO_0000210765Add
BLAST

Proteomic databases

MaxQBiQ8BWP5.
PaxDbiQ8BWP5.
PRIDEiQ8BWP5.

PTM databases

PhosphoSiteiQ8BWP5.

Expressioni

Gene expression databases

ArrayExpressiQ8BWP5.
BgeeiQ8BWP5.
CleanExiMM_TTPA.
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

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

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 253166CRAL-TRIO
Add
BLAST

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.

Phylogenomic databases

eggNOGiNOG250577.
GeneTreeiENSGT00550000074253.
HOVERGENiHBG018009.
InParanoidiQ8BWP5.
OMAiHLINEPI.
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

MAEMRPGPLV GKQLNELPDH SPLLQPGLAE LRRRVQEAGV PQTPQPLTDA    50
FLLRFLRARD FDLDLAWRLM KNYYKWRAEC PELSADLRPR SILGLLKAGY 100
HGVLRSRDST GSRVLIYRIA YWDPKVFTAY DVFRVSLITS ELIVQEVETQ 150
RNGVKAIFDL EGWQVSHAFQ ITPSVAKKIA AVLTDSFPLK VRGIHLINEP 200
VIFHAVFSMI KPFLTEKIKD RIHLHGNNYK SSMLQHFPDI LPREYGGKEF 250
SMEDICQEWT NFIMKSEDYL SSISETIQ 278
Length:278
Mass (Da):32,014
Last modified:March 1, 2003 - v1
Checksum:iBC913ADA7FB606D3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK004882 mRNA. Translation: BAB23640.1 .
AK050374 mRNA. Translation: BAC34218.1 .
AF218416 mRNA. Translation: AAF25956.1 .
CCDSi CCDS17995.1.
RefSeqi NP_056582.1. NM_015767.3.
UniGenei Mm.24375.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3W67 X-ray 2.61 A/B/C/D 21-278 [» ]
3W68 X-ray 2.05 A/B/C/D 21-278 [» ]
ProteinModelPortali Q8BWP5.
SMRi Q8BWP5. Positions 23-275.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8BWP5. 1 interaction.
MINTi MINT-1869030.

PTM databases

PhosphoSitei Q8BWP5.

Proteomic databases

MaxQBi Q8BWP5.
PaxDbi Q8BWP5.
PRIDEi Q8BWP5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000098244 ; ENSMUSP00000095845 ; ENSMUSG00000073988 .
GeneIDi 50500.
KEGGi mmu:50500.
UCSCi uc008sci.1. mouse.

Organism-specific databases

CTDi 7274.
MGIi MGI:1354168. Ttpa.

Phylogenomic databases

eggNOGi NOG250577.
GeneTreei ENSGT00550000074253.
HOVERGENi HBG018009.
InParanoidi Q8BWP5.
OMAi HLINEPI.
PhylomeDBi Q8BWP5.

Miscellaneous databases

NextBioi 307498.
PROi Q8BWP5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8BWP5.
Bgeei Q8BWP5.
CleanExi MM_TTPA.
Genevestigatori Q8BWP5.

Family and domain databases

Gene3Di 3.40.525.10. 1 hit.
InterProi IPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
[Graphical view ]
Pfami PF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view ]
PRINTSi PR00180. CRETINALDHBP.
SMARTi SM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view ]
SUPFAMi SSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEi PS50191. CRAL_TRIO. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.

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: July 9, 2014
This is version 88 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

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