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UniProtKB - P49638 (TTPA_HUMAN)

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Protein

Alpha-tocopherol transfer protein

Gene

TTPA

Organism
Homo sapiens (Human)
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 (PubMed:7887897). 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 similarity1 Publication

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

Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Biological processTransport
LigandLipid-binding

Enzyme and pathway databases

ReactomeiR-HSA-8877627. Vitamin E.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-tocopherol transfer protein
Short name:
Alpha-TTP
Gene namesi
Name:TTPA
Synonyms:TPP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:12404. TTPA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Ataxia with isolated vitamin E deficiency (AVED)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disease characterized by undetectable or markedly reduced plasma levels of vitamin E, spinocerebellar degeneration, ataxia, areflexia and proprioception loss.
See also OMIM:277460
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02238859R → W in AVED. 2 PublicationsCorresponds to variant dbSNP:rs397515522Ensembl.1
Natural variantiVAR_005668101H → Q in AVED. 2 PublicationsCorresponds to variant dbSNP:rs121917849Ensembl.1
Natural variantiVAR_022389120A → T in AVED. 2 PublicationsCorresponds to variant dbSNP:rs143010236Ensembl.1
Natural variantiVAR_022390141E → K in AVED. 2 PublicationsCorresponds to variant dbSNP:rs397515524Ensembl.1
Natural variantiVAR_007858192R → H in AVED. 2 PublicationsCorresponds to variant dbSNP:rs28936369Ensembl.1
Natural variantiVAR_022391221R → W in AVED. 2 PublicationsCorresponds to variant dbSNP:rs35916840Ensembl.1
Natural variantiVAR_022392246G → R in AVED; mild and slowly progressive form of the disease. 1 PublicationCorresponds to variant dbSNP:rs397515526Ensembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi7274.
MalaCardsiTTPA.
MIMi277460. phenotype.
OpenTargetsiENSG00000137561.
Orphaneti96. Ataxia with vitamin E deficiency.
PharmGKBiPA37068.

Chemistry databases

DrugBankiDB00163. Vitamin E.

Polymorphism and mutation databases

BioMutaiTTPA.
DMDMi1351322.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002107641 – 278Alpha-tocopherol transfer proteinAdd BLAST278

Proteomic databases

MaxQBiP49638.
PaxDbiP49638.
PeptideAtlasiP49638.
PRIDEiP49638.

PTM databases

iPTMnetiP49638.
PhosphoSitePlusiP49638.

Expressioni

Gene expression databases

BgeeiENSG00000137561.
CleanExiHS_TPP1.
HS_TTPA.
GenevisibleiP49638. HS.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
CMTM5Q96DZ93EBI-10210710,EBI-2548702

Protein-protein interaction databases

BioGridi113125. 3 interactors.
IntActiP49638. 20 interactors.
STRINGi9606.ENSP00000260116.

Structurei

Secondary structure

1278
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 15Combined sources6
Helixi22 – 24Combined sources3
Helixi28 – 38Combined sources11
Beta strandi43 – 45Combined sources3
Helixi49 – 58Combined sources10
Turni59 – 61Combined sources3
Helixi63 – 79Combined sources17
Helixi81 – 84Combined sources4
Helixi89 – 91Combined sources3
Helixi93 – 97Combined sources5
Beta strandi101 – 103Combined sources3
Beta strandi113 – 118Combined sources6
Helixi119 – 121Combined sources3
Turni124 – 126Combined sources3
Helixi129 – 143Combined sources15
Helixi147 – 152Combined sources6
Beta strandi154 – 159Combined sources6
Helixi165 – 170Combined sources6
Helixi173 – 184Combined sources12
Beta strandi186 – 189Combined sources4
Beta strandi191 – 198Combined sources8
Helixi201 – 203Combined sources3
Helixi204 – 210Combined sources7
Helixi211 – 213Combined sources3
Helixi216 – 219Combined sources4
Beta strandi222 – 224Combined sources3
Helixi230 – 236Combined sources7
Turni238 – 240Combined sources3
Helixi243 – 245Combined sources3
Helixi252 – 265Combined sources14
Helixi267 – 272Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OIPX-ray1.95A1-278[»]
1OIZX-ray1.88A/B1-278[»]
1R5LX-ray1.50A21-278[»]
ProteinModelPortaliP49638.
SMRiP49638.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49638.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini88 – 253CRAL-TRIOPROSITE-ProRule annotationAdd BLAST166

Phylogenomic databases

eggNOGiKOG1471. Eukaryota.
ENOG410XRSQ. LUCA.
GeneTreeiENSGT00550000074253.
HOGENOMiHOG000231534.
HOVERGENiHBG018009.
InParanoidiP49638.
OMAiWRAECPE.
OrthoDBiEOG091G0KN0.
PhylomeDBiP49638.

Family and domain databases

CDDicd00170. SEC14. 1 hit.
Gene3Di3.40.525.10. 1 hit.
InterProiView protein in InterPro
IPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
PfamiView protein in Pfam
PF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
PRINTSiPR00180. CRETINALDHBP.
SMARTiView protein in SMART
SM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
SUPFAMiSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiView protein in PROSITE
PS50191. CRAL_TRIO. 1 hit.

Sequencei

Sequence statusi: Complete.

P49638-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEARSQPSA GPQLNALPDH SPLLQPGLAA LRRRAREAGV PLAPLPLTDS 
        60         70         80         90        100
FLLRFLRARD FDLDLAWRLL KNYYKWRAEC PEISADLHPR SIIGLLKAGY 
       110        120        130        140        150
HGVLRSRDPT GSKVLIYRIA HWDPKVFTAY DVFRVSLITS ELIVQEVETQ 
       160        170        180        190        200
RNGIKAIFDL EGWQFSHAFQ ITPSVAKKIA AVLTDSFPLK VRGIHLINEP 
       210        220        230        240        250
VIFHAVFSMI KPFLTEKIKE RIHMHGNNYK QSLLQHFPDI LPLEYGGEEF 
       260        270 
SMEDICQEWT NFIMKSEDYL SSISESIQ
Length:278
Mass (Da):31,750
Last modified:February 1, 1996 - v1
Checksum:i64D1551CC155071E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti271S → R in AAA64309 (PubMed:8602747).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02238859R → W in AVED. 2 PublicationsCorresponds to variant dbSNP:rs397515522Ensembl.1
Natural variantiVAR_005668101H → Q in AVED. 2 PublicationsCorresponds to variant dbSNP:rs121917849Ensembl.1
Natural variantiVAR_022389120A → T in AVED. 2 PublicationsCorresponds to variant dbSNP:rs143010236Ensembl.1
Natural variantiVAR_022390141E → K in AVED. 2 PublicationsCorresponds to variant dbSNP:rs397515524Ensembl.1
Natural variantiVAR_037973172T → S. Corresponds to variant dbSNP:rs34647756Ensembl.1
Natural variantiVAR_007858192R → H in AVED. 2 PublicationsCorresponds to variant dbSNP:rs28936369Ensembl.1
Natural variantiVAR_022391221R → W in AVED. 2 PublicationsCorresponds to variant dbSNP:rs35916840Ensembl.1
Natural variantiVAR_022392246G → R in AVED; mild and slowly progressive form of the disease. 1 PublicationCorresponds to variant dbSNP:rs397515526Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49488 mRNA. Translation: BAA08449.1.
U21938 mRNA. Translation: AAA64309.1.
BC058000 mRNA. Translation: AAH58000.1.
AH006950 Genomic DNA. Translation: AAC67490.1.
CCDSiCCDS6178.1.
PIRiS54352.
RefSeqiNP_000361.1. NM_000370.3.
UniGeneiHs.69049.

Genome annotation databases

EnsembliENST00000260116; ENSP00000260116; ENSG00000137561.
GeneIDi7274.
KEGGihsa:7274.
UCSCiuc003xux.3. human.

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.

Entry informationi

Entry nameiTTPA_HUMAN
AccessioniPrimary (citable) accession number: P49638
Secondary accession number(s): Q71V64
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 5, 2017
This is version 157 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references