TTPA_HUMAN
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 03-AUG-2022, entry version 189.
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-23667468;
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.
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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; 47.
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; P49638; -.
DR PeptideAtlas; P49638; -.
DR PRIDE; P49638; -.
DR ProteomicsDB; 56032; -.
DR Antibodypedia; 55595; 122 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 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; WTDFIMA; -.
DR OrthoDB; 1053004at2759; -.
DR PhylomeDB; P49638; -.
DR PathwayCommons; P49638; -.
DR Reactome; R-HSA-8877627; Vitamin E.
DR SignaLink; P49638; -.
DR BioGRID-ORCS; 7274; 12 hits in 1081 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 88 other tissues.
DR Genevisible; P49638; HS.
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; 3.40.525.10; -; 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 Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
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
