alpha-tocopherol transfer protein [Homo sapiens]
NCBI Reference Sequence: NP_000361.1
LOCUS NP_000361 278 aa linear PRI 15-MAR-2015 DEFINITION alpha-tocopherol transfer protein [Homo sapiens]. ACCESSION NP_000361 XP_001128514 VERSION NP_000361.1 GI:4507723 DBSOURCE REFSEQ: accession NM_000370.3 KEYWORDS RefSeq. SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 278) AUTHORS Kono N, Ohto U, Hiramatsu T, Urabe M, Uchida Y, Satow Y and Arai H. TITLE Impaired alpha-TTP-PIPs interaction underlies familial vitamin E deficiency JOURNAL Science 340 (6136), 1106-1110 (2013) PUBMED 23599266 REMARK GeneRIF: The crystal structure of the alpha-TTP-phosphatidylinositol phosphates (PIPs) complex revealed that the familial vitamin E deficiency-related arginine residues interacted with phosphate groups of the PIPs and that the PIPs binding caused the lid of the alpha-tocopherol-binding pocket to open. REFERENCE 2 (residues 1 to 278) AUTHORS Etzl RP, Vrekoussis T, Kuhn C, Schulze S, Poschl JM, Makrigiannakis A, Jeschke U and Rotzoll DE. TITLE Oxidative stress stimulates alpha-tocopherol transfer protein in human trophoblast tumor cells BeWo JOURNAL J Perinat Med 40 (4), 373-378 (2012) PUBMED 22752767 REMARK GeneRIF: study demonstrated that alpha -TTP can be upregulated in case of oxidative stress in BeWo trophoblast cells; speculate that possibly, alpha -TTP is notonly involved in normal pregnancy, but also in cases of pregnancy disorders with intense oxidative stress Publication Status: Online-Only REFERENCE 3 (residues 1 to 278) AUTHORS Zhang WX, Thakur V, Lomize A, Pogozheva I, Panagabko C, Cecchini M, Baptist M, Morley S, Manor D and Atkinson J. TITLE The contribution of surface residues to membrane binding and ligand transfer by the alpha-tocopherol transfer protein (alpha-TTP) JOURNAL J. Mol. Biol. 405 (4), 972-988 (2011) PUBMED 21110980 REMARK GeneRIF: Substitution of residues in helices A8 (F165A and F169A) and A10 (I202A, V206A and M209A) decreased the rate of intermembrane ligand transfer as well as protein adsorption to phospholipid bilayers. REFERENCE 4 (residues 1 to 278) AUTHORS Booij JC, Bakker A, Kulumbetova J, Moutaoukil Y, Smeets B, Verheij J, Kroes HY, Klaver CC, van Schooneveld M, Bergen AA and Florijn RJ. TITLE Simultaneous mutation detection in 90 retinal disease genes in multiple patients using a custom-designed 300-kb retinal resequencing chip JOURNAL Ophthalmology 118 (1), 160-167 (2011) PUBMED 20801516 REMARK GeneRIF: Observational study of genetic testing. (HuGE Navigator) REFERENCE 5 (residues 1 to 278) AUTHORS Morley S, Thakur V, Danielpour D, Parker R, Arai H, Atkinson J, Barnholtz-Sloan J, Klein E and Manor D. TITLE Tocopherol transfer protein sensitizes prostate cancer cells to vitamin E JOURNAL J. Biol. Chem. 285 (46), 35578-35589 (2010) PUBMED 20826775 REMARK GeneRIF: Data show that reduction ('knockdown') of tocopherol transfer protein (TTP) expression resulted in resistance to the vitamin E. REFERENCE 6 (residues 1 to 278) AUTHORS Gotoda T, Arita M, Arai H, Inoue K, Yokota T, Fukuo Y, Yazaki Y and Yamada N. TITLE Adult-onset spinocerebellar dysfunction caused by a mutation in the gene for the alpha-tocopherol-transfer protein JOURNAL N. Engl. J. Med. 333 (20), 1313-1318 (1995) PUBMED 7566022 REFERENCE 7 (residues 1 to 278) AUTHORS Arita M, Sato Y, Miyata A, Tanabe T, Takahashi E, Kayden HJ, Arai H and Inoue K. TITLE Human alpha-tocopherol transfer protein: cDNA cloning, expression and chromosomal localization JOURNAL Biochem. J. 306 (PT 2), 437-443 (1995) PUBMED 7887897 REFERENCE 8 (residues 1 to 278) AUTHORS Ouahchi K, Arita M, Kayden H, Hentati F, Ben Hamida M, Sokol R, Arai H, Inoue K, Mandel JL and Koenig M. TITLE Ataxia with isolated vitamin E deficiency is caused by mutations in the alpha-tocopherol transfer protein JOURNAL Nat. Genet. 9 (2), 141-145 (1995) PUBMED 7719340 REFERENCE 9 (residues 1 to 278) AUTHORS Ben Hamida C, Doerflinger N, Belal S, Linder C, Reutenauer L, Dib C, Gyapay G, Vignal A, Le Paslier D and Cohen D. CONSRTM et al TITLE Localization of Friedreich ataxia phenotype with selective vitamin E deficiency to chromosome 8q by homozygosity mapping JOURNAL Nat. Genet. 5 (2), 195-200 (1993) PUBMED 8252047 REFERENCE 10 (residues 1 to 278) AUTHORS Schuelke,M. TITLE Ataxia with Vitamin E Deficiency JOURNAL (in) Pagon RA, Adam MP, Ardinger HH, Bird TD, Dolan CR, Fong CT, Smith RJH and Stephens K (Eds.); GENEREVIEWS(R); (1993) PUBMED 20301419 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from BC058000.1, BC041784.1 and AC120042.3. This sequence is a reference standard in the RefSeqGene project. On Sep 20, 2006 this sequence version replaced gi:113420428. Summary: This gene encodes a soluble protein that binds alpha-tocopherol, a form of vitamin E, with high selectivity and affinity. This protein plays an important role in regulating vitamin E levels in the body by transporting vitamin E between membrane vesicles and facilitating the secretion of vitamin E from hepatocytes to circulating lipoproteins. Mutations in this gene cause hereditary vitamin E deficiency (ataxia with vitamin E deficiency, AVED) and retinitis pigmentosa. [provided by RefSeq, Nov 2009]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC058000.1, BC041784.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1970526 [ECO:0000348] ##Evidence-Data-END## FEATURES Location/Qualifiers source 1..278 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="8" /map="8q12.3" Protein 1..278 /product="alpha-tocopherol transfer protein" /note="tocopherol (alpha) transfer protein (ataxia (Friedreich-like) with vitamin E deficiency); alpha-TTP" /calculated_mol_wt=31619 Region <40 ..73="" cdd="" cddsrv.cgi="" db_xref="CDD:<a href=" http:="" note="CRAL/TRIO, N-terminal domain; smart01100" region_name="CRAL_TRIO_N" tructure="" uid="215024" www.ncbi.nlm.nih.gov="">215024" Region 95..248 /region_name="SEC14" /note="Sec14p-like lipid-binding domain. Found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to...; cd00170" /db_xref="CDD:238099" Site order(113,115,117,143,158,160,176,180,184,188,191,194,196, 203,210,222) /site_type="other" /note="phospholipid binding pocket [chemical binding]" /db_xref="CDD:238099" Site order(189,221) /site_type="other" /note="salt bridge" /db_xref="CDD:238099" CDS 1..278 /gene="TTPA" /gene_synonym="alphaTTP; ATTP; AVED; TTP1" /coded_by="NM_000370.3:33..869" /db_xref="CCDS:CCDS6178.1" /db_xref="GeneID:7274" /db_xref="HGNC:HGNC:12404" /db_xref="HPRD:02685" /db_xref="MIM:600415" ORIGIN 1 maearsqpsa gpqlnalpdh spllqpglaa lrrrareagv plaplpltds fllrflrard 61 fdldlawrll knyykwraec peisadlhpr siigllkagy hgvlrsrdpt gskvliyria 121 hwdpkvftay dvfrvslits elivqevetq rngikaifdl egwqfshafq itpsvakkia 181 avltdsfplk vrgihlinep vifhavfsmi kpfltekike rihmhgnnyk qsllqhfpdi 241 lpleyggeef smedicqewt nfimksedyl ssisesiq //
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