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Q8BWP5

- TTPA_MOUSE

UniProt

Q8BWP5 - TTPA_MOUSE

Protein

Alpha-tocopherol transfer protein

Gene

Ttpa

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    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

    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

    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

    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

    1
    278
    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.
    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.
    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

    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: October 1, 2014
    This is version 89 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