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Protein

Alpha-tocopherol transfer protein

Gene

Ttpa

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei190Phosphatidylinositol lipid headgroupBy similarity1
Binding sitei192Phosphatidylinositol lipid headgroupBy similarity1
Binding sitei217Phosphatidylinositol lipid headgroupBy similarity1
Binding sitei221Phosphatidylinositol lipid headgroupBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • developmental process Source: RGD
  • embryonic placenta development Source: Ensembl
  • intermembrane transport Source: UniProtKB
  • intracellular pH reduction Source: RGD
  • negative regulation of cell death Source: RGD
  • negative regulation of establishment of blood-brain barrier Source: Ensembl
  • response to nutrient Source: RGD
  • response to pH Source: RGD
  • response to toxic substance Source: Ensembl
  • vitamin E metabolic process Source: RGD
  • 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
Synonyms:Tpp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi3915. Ttpa.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • late endosome Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002107661 – 278Alpha-tocopherol transfer proteinAdd BLAST278

Proteomic databases

PaxDbiP41034.
PRIDEiP41034.

PTM databases

iPTMnetiP41034.
PhosphoSitePlusiP41034.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiENSRNOG00000007139.
GenevisibleiP41034. RN.

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 (By similarity).By similarity

Protein-protein interaction databases

IntActiP41034. 1 interactor.
STRINGi10116.ENSRNOP00000009611.

Structurei

3D structure databases

ProteinModelPortaliP41034.
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.
HOGENOMiHOG000231534.
HOVERGENiHBG018009.
InParanoidiP41034.
OMAiTAYDAFR.
OrthoDBiEOG091G0KN0.
PhylomeDBiP41034.

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.

P41034-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEMRPGPVV GKQLNEQPDH SPLVQPGLAE LRRRAQEEGV PETPQPLTDA
60 70 80 90 100
FLLRFLRARD FDLDLAWRLM KNYYKWRAEC PELSADLHPR SILGLLKAGY
110 120 130 140 150
HGVLRSRDPT GSRVLIYRIS YWDPKVFTAY DVFRVSLITS ELIVQEVETQ
160 170 180 190 200
RNGVKAIFDL EGWQISHAFQ ITPSVAKKIA AVVTDSFPLK VRGIHLINEP
210 220 230 240 250
VIFHAVFSMI KPFLTEKIKG RIHLHGNNYK SSLLQHFPDI LPLEYGGNES
260 270
SMEDICQEWT NFIMKSEDYL SSISETIQ
Length:278
Mass (Da):31,846
Last modified:February 1, 1995 - v1
Checksum:i96F16E3F227F140C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16339 mRNA. Translation: BAA03843.1.
PIRiA47404.
RefSeqiNP_037180.1. NM_013048.2.
UniGeneiRn.228762.

Genome annotation databases

EnsembliENSRNOT00000009611; ENSRNOP00000009611; ENSRNOG00000007139.
GeneIDi25571.
KEGGirno:25571.
UCSCiRGD:3915. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16339 mRNA. Translation: BAA03843.1.
PIRiA47404.
RefSeqiNP_037180.1. NM_013048.2.
UniGeneiRn.228762.

3D structure databases

ProteinModelPortaliP41034.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP41034. 1 interactor.
STRINGi10116.ENSRNOP00000009611.

PTM databases

iPTMnetiP41034.
PhosphoSitePlusiP41034.

Proteomic databases

PaxDbiP41034.
PRIDEiP41034.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009611; ENSRNOP00000009611; ENSRNOG00000007139.
GeneIDi25571.
KEGGirno:25571.
UCSCiRGD:3915. rat.

Organism-specific databases

CTDi7274.
RGDi3915. Ttpa.

Phylogenomic databases

eggNOGiKOG1471. Eukaryota.
ENOG410XRSQ. LUCA.
GeneTreeiENSGT00550000074253.
HOGENOMiHOG000231534.
HOVERGENiHBG018009.
InParanoidiP41034.
OMAiTAYDAFR.
OrthoDBiEOG091G0KN0.
PhylomeDBiP41034.

Miscellaneous databases

PROiP41034.

Gene expression databases

BgeeiENSRNOG00000007139.
GenevisibleiP41034. RN.

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_RAT
AccessioniPrimary (citable) accession number: P41034
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.