ID TTPA_HUMAN Reviewed; 278 AA. AC P49638; Q71V64; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 24-JAN-2024, entry version 197. DE RecName: Full=Alpha-tocopherol transfer protein; DE Short=Alpha-TTP; GN Name=TTPA; Synonyms=TPP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION. RC TISSUE=Liver; RX PubMed=7887897; DOI=10.1042/bj3060437; RA Arita M., Sato Y., Miyata A., Tanabe T., Takahashi E., Kayden H.J., RA Arai H., Inoue K.; RT "Human alpha-tocopherol transfer protein: cDNA cloning, expression and RT chromosomal localization."; RL Biochem. J. 306:437-443(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT AVED HIS-192. RX PubMed=8602747; DOI=10.1002/ana.410390305; RA Hentati A., Deng H.-X., Hung W.-Y., Nayer M., Ahmed M.S., He X., Tim R., RA Stumpf D.A., Siddique T.; RT "Human alpha-tocopherol transfer protein: gene structure and mutations in RT familial vitamin E deficiency."; RL Ann. Neurol. 39:295-300(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-119, AND VARIANTS AVED TRP-59; RP THR-120; LYS-141 AND TRP-221. RX PubMed=9463307; DOI=10.1086/301699; RA Cavalier L., Ouahchi K., Kayden H.J., Di Donato S., Reutenauer L., RA Mandel J.-L., Koenig M.; RT "Ataxia with isolated vitamin E deficiency: heterogeneity of mutations and RT phenotypic variability in a large number of families."; RL Am. J. Hum. Genet. 62:301-310(1998). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 170-180 AND 246-265, AND DISEASE. RX PubMed=7719340; DOI=10.1038/ng0295-141; RA Ouahchi K., Arita M., Kayden H., Hentati F., Ben-Hamida M., Sokol R., RA Arai H., Inoue K., Mandel J.-L., Koenig M.; RT "Ataxia with isolated vitamin E deficiency is caused by mutations in the RT alpha-tocopherol transfer protein."; RL Nat. Genet. 9:141-145(1995). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS). RX PubMed=12899840; DOI=10.1016/s0022-2836(03)00724-1; RA Meier R., Tomizaki T., Schulze-Briese C., Baumann U., Stocker A.; RT "The molecular basis of vitamin E retention: structure of human alpha- RT tocopherol transfer protein."; RL J. Mol. Biol. 331:725-734(2003). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 21-278. RX PubMed=14657365; DOI=10.1073/pnas.2136684100; RA Min K.C., Kovall R.A., Hendrickson W.A.; RT "Crystal structure of human alpha-tocopherol transfer protein bound to its RT ligand: implications for ataxia with vitamin E deficiency."; RL Proc. Natl. Acad. Sci. U.S.A. 100:14713-14718(2003). RN [9] RP VARIANT AVED GLN-101. RX PubMed=7566022; DOI=10.1056/nejm199511163332003; RA Gotoda T., Arita M., Arai H., Inoue K., Yokota T., Fukuo Y., Yazaki Y., RA Yamada N.; RT "Adult-onset spinocerebellar dysfunction caused by a mutation in the gene RT for the alpha-tocopherol-transfer protein."; RL N. Engl. J. Med. 333:1313-1318(1995). RN [10] RP CHARACTERIZATION OF VARIANTS AVED TRP-59; GLN-101; THR-120; LYS-141; RP HIS-192 AND TRP-221. RX PubMed=15065857; DOI=10.1021/bi0363073; RA Morley S., Panagabko C., Shineman D., Mani B., Stocker A., Atkinson J., RA Manor D.; RT "Molecular determinants of heritable vitamin E deficiency."; RL Biochemistry 43:4143-4149(2004). RN [11] RP VARIANT AVED ARG-246. RX PubMed=15300460; DOI=10.1007/s10072-004-0246-z; RA Mariotti C., Gellera C., Rimoldi M., Mineri R., Uziel G., Zorzi G., RA Pareyson D., Piccolo G., Gambi D., Piacentini S., Squitieri F., Capra R., RA Castellotti B., Di Donato S.; RT "Ataxia with isolated vitamin E deficiency: neurological phenotype, RT clinical follow-up and novel mutations in TTPA gene in Italian families."; RL Neurol. Sci. 25:130-137(2004). CC -!- FUNCTION: Binds alpha-tocopherol, enhances its transfer between CC separate membranes, and stimulates its release from liver cells CC (PubMed:7887897). Binds both phosphatidylinositol 3,4-bisphosphate and CC phosphatidylinositol 4,5-bisphosphate; the resulting conformation CC change is important for the release of the bound alpha-tocopherol (By CC similarity). {ECO:0000250, ECO:0000269|PubMed:7887897}. CC -!- SUBUNIT: Monomer and homotetramer. Phosphatidylinositol 4,5- CC bisphosphate binding induces the formation of homotetramers. CC Phosphatidylinositol 3,4-bisphosphate is less efficient in inducing CC tetramerization (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC P49638; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-10210710, EBI-11522760; CC P49638; Q6Q788: APOA5; NbExp=3; IntAct=EBI-10210710, EBI-3936819; CC P49638; P02655: APOC2; NbExp=3; IntAct=EBI-10210710, EBI-1223594; CC P49638; P53365: ARFIP2; NbExp=3; IntAct=EBI-10210710, EBI-638194; CC P49638; Q5T9G4-2: ARMC12; NbExp=3; IntAct=EBI-10210710, EBI-36513937; CC P49638; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-10210710, EBI-517623; CC P49638; Q8N5K1: CISD2; NbExp=5; IntAct=EBI-10210710, EBI-1045797; CC P49638; Q8IZR5-2: CMTM4; NbExp=3; IntAct=EBI-10210710, EBI-17278014; CC P49638; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-10210710, EBI-2548702; CC P49638; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-10210710, EBI-11522780; CC P49638; Q9NZJ6: COQ3; NbExp=3; IntAct=EBI-10210710, EBI-10897372; CC P49638; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10210710, EBI-3867333; CC P49638; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-10210710, EBI-12831978; CC P49638; Q02127: DHODH; NbExp=3; IntAct=EBI-10210710, EBI-3928775; CC P49638; Q8N9I5: FADS6; NbExp=3; IntAct=EBI-10210710, EBI-3943864; CC P49638; Q9NRY5: FAM114A2; NbExp=3; IntAct=EBI-10210710, EBI-10973142; CC P49638; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-10210710, EBI-14240149; CC P49638; Q92915-2: FGF14; NbExp=3; IntAct=EBI-10210710, EBI-12836320; CC P49638; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-10210710, EBI-3918971; CC P49638; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10210710, EBI-618309; CC P49638; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-10210710, EBI-1052304; CC P49638; Q8TAC2: JOSD2; NbExp=3; IntAct=EBI-10210710, EBI-12205593; CC P49638; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10210710, EBI-10172290; CC P49638; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-10210710, EBI-10176379; CC P49638; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-10210710, EBI-11953334; CC P49638; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-10210710, EBI-14065470; CC P49638; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-10210710, EBI-17490413; CC P49638; Q969L2: MAL2; NbExp=5; IntAct=EBI-10210710, EBI-944295; CC P49638; Q6IN84: MRM1; NbExp=3; IntAct=EBI-10210710, EBI-5454865; CC P49638; O95182: NDUFA7; NbExp=3; IntAct=EBI-10210710, EBI-721471; CC P49638; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-10210710, EBI-22310682; CC P49638; O00623: PEX12; NbExp=3; IntAct=EBI-10210710, EBI-594836; CC P49638; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-10210710, EBI-11337973; CC P49638; Q9NS64: RPRM; NbExp=3; IntAct=EBI-10210710, EBI-1052363; CC P49638; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-10210710, EBI-3920694; CC P49638; O15126: SCAMP1; NbExp=3; IntAct=EBI-10210710, EBI-954338; CC P49638; Q8TAC9: SCAMP5; NbExp=3; IntAct=EBI-10210710, EBI-2695784; CC P49638; Q8N3Y7: SDR16C5; NbExp=3; IntAct=EBI-10210710, EBI-3923480; CC P49638; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-10210710, EBI-2623095; CC P49638; Q7Z769: SLC35E3; NbExp=3; IntAct=EBI-10210710, EBI-13389236; CC P49638; O43761: SYNGR3; NbExp=3; IntAct=EBI-10210710, EBI-11321949; CC P49638; Q8WY91: THAP4; NbExp=3; IntAct=EBI-10210710, EBI-726691; CC P49638; P55327-2: TPD52; NbExp=3; IntAct=EBI-10210710, EBI-12124194; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7887897}. CC -!- DISEASE: Ataxia with vitamin E deficiency (AVED) [MIM:277460]: An CC autosomal recessive disease characterized by undetectable or markedly CC reduced plasma levels of vitamin E, spinocerebellar degeneration, CC ataxia, areflexia and proprioception loss. CC {ECO:0000269|PubMed:15065857, ECO:0000269|PubMed:15300460, CC ECO:0000269|PubMed:7566022, ECO:0000269|PubMed:8602747, CC ECO:0000269|PubMed:9463307}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D49488; BAA08449.1; -; mRNA. DR EMBL; U21938; AAA64309.1; -; mRNA. DR EMBL; BC058000; AAH58000.1; -; mRNA. DR EMBL; AH006950; AAC67490.1; -; Genomic_DNA. DR CCDS; CCDS6178.1; -. DR PIR; S54352; S54352. DR RefSeq; NP_000361.1; NM_000370.3. DR PDB; 1OIP; X-ray; 1.95 A; A=1-278. DR PDB; 1OIZ; X-ray; 1.88 A; A/B=1-278. DR PDB; 1R5L; X-ray; 1.50 A; A=21-278. DR PDB; 5MUE; X-ray; 2.40 A; A=48-275. DR PDB; 5MUG; X-ray; 2.42 A; A=48-278. DR PDB; 6ZPD; X-ray; 2.24 A; A=48-278. DR PDBsum; 1OIP; -. DR PDBsum; 1OIZ; -. DR PDBsum; 1R5L; -. DR PDBsum; 5MUE; -. DR PDBsum; 5MUG; -. DR PDBsum; 6ZPD; -. DR AlphaFoldDB; P49638; -. DR SMR; P49638; -. DR BioGRID; 113125; 48. DR IntAct; P49638; 42. DR STRING; 9606.ENSP00000260116; -. DR BindingDB; P49638; -. DR ChEMBL; CHEMBL3308919; -. DR DrugBank; DB02080; 1-{2-[2-(2-Methoxyethoxy)Ethoxy]Ethoxy}-4-(1,1,3,3-Tetramethylbutyl)Benzene. DR DrugBank; DB14003; alpha-Tocopherol acetate. DR DrugBank; DB14001; alpha-Tocopherol succinate. DR DrugBank; DB14002; D-alpha-Tocopherol acetate. DR DrugBank; DB11635; Tocofersolan. DR DrugBank; DB11251; Tocopherol. DR DrugBank; DB00163; Vitamin E. DR iPTMnet; P49638; -. DR PhosphoSitePlus; P49638; -. DR BioMuta; TTPA; -. DR DMDM; 1351322; -. DR jPOST; P49638; -. DR MassIVE; P49638; -. DR MaxQB; P49638; -. DR PaxDb; 9606-ENSP00000260116; -. DR PeptideAtlas; P49638; -. DR ProteomicsDB; 56032; -. DR Antibodypedia; 55595; 133 antibodies from 17 providers. DR DNASU; 7274; -. DR Ensembl; ENST00000260116.5; ENSP00000260116.4; ENSG00000137561.5. DR GeneID; 7274; -. DR KEGG; hsa:7274; -. DR MANE-Select; ENST00000260116.5; ENSP00000260116.4; NM_000370.3; NP_000361.1. DR UCSC; uc003xux.3; human. DR AGR; HGNC:12404; -. DR CTD; 7274; -. DR DisGeNET; 7274; -. DR GeneCards; TTPA; -. DR GeneReviews; TTPA; -. DR HGNC; HGNC:12404; TTPA. DR HPA; ENSG00000137561; Tissue enriched (liver). DR MalaCards; TTPA; -. DR MIM; 277460; phenotype. DR MIM; 600415; gene. DR neXtProt; NX_P49638; -. DR OpenTargets; ENSG00000137561; -. DR Orphanet; 96; Ataxia with vitamin E deficiency. DR PharmGKB; PA37068; -. DR VEuPathDB; HostDB:ENSG00000137561; -. DR eggNOG; KOG1471; Eukaryota. DR GeneTree; ENSGT00940000159203; -. DR HOGENOM; CLU_046597_1_2_1; -. DR InParanoid; P49638; -. DR OMA; KQRVYMH; -. DR OrthoDB; 522503at2759; -. DR PhylomeDB; P49638; -. DR PathwayCommons; P49638; -. DR Reactome; R-HSA-8877627; Vitamin E. DR SignaLink; P49638; -. DR BioGRID-ORCS; 7274; 12 hits in 1159 CRISPR screens. DR ChiTaRS; TTPA; human. DR EvolutionaryTrace; P49638; -. DR GeneWiki; Alpha-tocopherol_transfer_protein; -. DR GenomeRNAi; 7274; -. DR Pharos; P49638; Tchem. DR PRO; PR:P49638; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P49638; Protein. DR Bgee; ENSG00000137561; Expressed in right lobe of liver and 89 other cell types or tissues. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005770; C:late endosome; IBA:GO_Central. DR GO; GO:0120013; F:lipid transfer activity; IBA:GO_Central. DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IBA:GO_Central. DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB. DR GO; GO:0008431; F:vitamin E binding; ISS:UniProtKB. DR GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl. DR GO; GO:0120009; P:intermembrane lipid transfer; ISS:UniProtKB. DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc. DR GO; GO:0090212; P:negative regulation of establishment of blood-brain barrier; IEA:Ensembl. DR GO; GO:1900223; P:positive regulation of amyloid-beta clearance; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR GO; GO:0042360; P:vitamin E metabolic process; IBA:GO_Central. DR GO; GO:0051180; P:vitamin transport; ISS:UniProtKB. DR CDD; cd00170; SEC14; 1. DR Gene3D; 1.20.5.1200; Alpha-tocopherol transfer; 1. DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1. DR Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 1. DR InterPro; IPR001251; CRAL-TRIO_dom. DR InterPro; IPR036865; CRAL-TRIO_dom_sf. DR InterPro; IPR011074; CRAL/TRIO_N_dom. DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf. DR PANTHER; PTHR10174:SF225; ALPHA-TOCOPHEROL TRANSFER PROTEIN; 1. DR PANTHER; PTHR10174; ALPHA-TOCOPHEROL TRANSFER PROTEIN-RELATED; 1. DR Pfam; PF00650; CRAL_TRIO; 1. DR Pfam; PF03765; CRAL_TRIO_N; 1. DR PRINTS; PR00180; CRETINALDHBP. DR SMART; SM01100; CRAL_TRIO_N; 1. DR SMART; SM00516; SEC14; 1. DR SUPFAM; SSF52087; CRAL/TRIO domain; 1. DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1. DR PROSITE; PS50191; CRAL_TRIO; 1. DR Genevisible; P49638; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Disease variant; Lipid-binding; KW Reference proteome; Transport. FT CHAIN 1..278 FT /note="Alpha-tocopherol transfer protein" FT /id="PRO_0000210764" FT DOMAIN 88..253 FT /note="CRAL-TRIO" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 185 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:57658" FT /evidence="ECO:0000250|UniProtKB:Q8BWP5" FT BINDING 187 FT /ligand="(+)-alpha-tocopherol" FT /ligand_id="ChEBI:CHEBI:18145" FT /evidence="ECO:0000250|UniProtKB:Q8BWP5" FT BINDING 190..192 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:57658" FT /evidence="ECO:0000250|UniProtKB:Q8BWP5" FT BINDING 208..211 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-4,5-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:58456" FT /evidence="ECO:0000250|UniProtKB:Q8BWP5" FT BINDING 217 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:57658" FT /evidence="ECO:0000250|UniProtKB:Q8BWP5" FT BINDING 221 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:57658" FT /evidence="ECO:0000250|UniProtKB:Q8BWP5" FT VARIANT 59 FT /note="R -> W (in AVED; dbSNP:rs397515522)" FT /evidence="ECO:0000269|PubMed:15065857, FT ECO:0000269|PubMed:9463307" FT /id="VAR_022388" FT VARIANT 101 FT /note="H -> Q (in AVED; dbSNP:rs121917849)" FT /evidence="ECO:0000269|PubMed:15065857, FT ECO:0000269|PubMed:7566022" FT /id="VAR_005668" FT VARIANT 120 FT /note="A -> T (in AVED; dbSNP:rs143010236)" FT /evidence="ECO:0000269|PubMed:15065857, FT ECO:0000269|PubMed:9463307" FT /id="VAR_022389" FT VARIANT 141 FT /note="E -> K (in AVED; dbSNP:rs397515524)" FT /evidence="ECO:0000269|PubMed:15065857, FT ECO:0000269|PubMed:9463307" FT /id="VAR_022390" FT VARIANT 172 FT /note="T -> S (in dbSNP:rs34647756)" FT /id="VAR_037973" FT VARIANT 192 FT /note="R -> H (in AVED; dbSNP:rs121917850)" FT /evidence="ECO:0000269|PubMed:15065857, FT ECO:0000269|PubMed:8602747" FT /id="VAR_007858" FT VARIANT 221 FT /note="R -> W (in AVED; dbSNP:rs35916840)" FT /evidence="ECO:0000269|PubMed:15065857, FT ECO:0000269|PubMed:9463307" FT /id="VAR_022391" FT VARIANT 246 FT /note="G -> R (in AVED; mild and slowly progressive form of FT the disease; dbSNP:rs397515526)" FT /evidence="ECO:0000269|PubMed:15300460" FT /id="VAR_022392" FT CONFLICT 271 FT /note="S -> R (in Ref. 2; AAA64309)" FT /evidence="ECO:0000305" FT HELIX 10..15 FT /evidence="ECO:0007829|PDB:1OIZ" FT HELIX 22..24 FT /evidence="ECO:0007829|PDB:1OIZ" FT HELIX 28..38 FT /evidence="ECO:0007829|PDB:1R5L" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 49..58 FT /evidence="ECO:0007829|PDB:1R5L" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 63..79 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 81..84 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 93..97 FT /evidence="ECO:0007829|PDB:1R5L" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:1R5L" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:1R5L" FT TURN 124..126 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 129..143 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 147..152 FT /evidence="ECO:0007829|PDB:1R5L" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 165..170 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 173..184 FT /evidence="ECO:0007829|PDB:1R5L" FT STRAND 186..189 FT /evidence="ECO:0007829|PDB:1R5L" FT STRAND 191..198 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 204..210 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 216..219 FT /evidence="ECO:0007829|PDB:1R5L" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 230..236 FT /evidence="ECO:0007829|PDB:1R5L" FT TURN 238..240 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 243..245 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 252..265 FT /evidence="ECO:0007829|PDB:1R5L" FT HELIX 267..272 FT /evidence="ECO:0007829|PDB:1R5L" SQ SEQUENCE 278 AA; 31750 MW; 64D1551CC155071E CRC64; MAEARSQPSA GPQLNALPDH SPLLQPGLAA LRRRAREAGV PLAPLPLTDS FLLRFLRARD FDLDLAWRLL KNYYKWRAEC PEISADLHPR SIIGLLKAGY HGVLRSRDPT GSKVLIYRIA HWDPKVFTAY DVFRVSLITS ELIVQEVETQ RNGIKAIFDL EGWQFSHAFQ ITPSVAKKIA AVLTDSFPLK VRGIHLINEP VIFHAVFSMI KPFLTEKIKE RIHMHGNNYK QSLLQHFPDI LPLEYGGEEF SMEDICQEWT NFIMKSEDYL SSISESIQ //