T23O_HUMAN
ID T23O_HUMAN Reviewed; 406 AA.
AC P48775; A8K053;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Tryptophan 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TDO {ECO:0000255|HAMAP-Rule:MF_03020};
DE EC=1.13.11.11 {ECO:0000255|HAMAP-Rule:MF_03020, ECO:0000269|PubMed:25066423, ECO:0000269|PubMed:27762317, ECO:0000269|PubMed:28285122};
DE AltName: Full=Tryptamin 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophan oxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TO {ECO:0000255|HAMAP-Rule:MF_03020};
DE Short=TRPO {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophan pyrrolase {ECO:0000255|HAMAP-Rule:MF_03020};
DE AltName: Full=Tryptophanase {ECO:0000255|HAMAP-Rule:MF_03020};
GN Name=TDO2 {ECO:0000255|HAMAP-Rule:MF_03020}; Synonyms=TDO;
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].
RC TISSUE=Brain;
RX PubMed=8666386; DOI=10.1006/geno.1995.9990;
RA Comings D.E., Muhleman D., Dietz G., Sherman M., Forest G.L.;
RT "Sequence of human tryptophan 2,3-dioxygenase (TDO2): presence of a
RT glucocorticoid response-like element composed of a GTT repeat and an
RT intronic CCCCT repeat.";
RL Genomics 29:390-396(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [5]
RP INVOLVEMENT IN HYPTRP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, VARIANT HYPTRP ILE-108, AND
RP CHARACTERIZATION OF VARIANT HYPTRP ILE-108.
RX PubMed=28285122; DOI=10.1016/j.ymgme.2017.02.009;
RA Ferreira P., Shin I., Sosova I., Dornevil K., Jain S., Dewey D., Liu F.,
RA Liu A.;
RT "Hypertryptophanemia due to tryptophan 2,3-dioxygenase deficiency.";
RL Mol. Genet. Metab. 120:317-324(2017).
RN [6] {ECO:0007744|PDB:4PW8}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 19-388 OF APOPROTEIN, SUBUNIT,
RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, PATHWAY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF TYR-42; TYR-45; PHE-72; HIS-76; PHE-140;
RP ARG-144; SER-151 AND HIS-328.
RX PubMed=25066423; DOI=10.1002/prot.24653;
RA Meng B., Wu D., Gu J., Ouyang S., Ding W., Liu Z.J.;
RT "Structural and functional analyses of human tryptophan 2,3-dioxygenase.";
RL Proteins 82:3210-3216(2014).
RN [7] {ECO:0007744|PDB:5TI9, ECO:0007744|PDB:5TIA}
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 18-389 IN COMPLEX WITH HEME AND
RP TRYPTOPHAN, COFACTOR, SUBUNIT, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS
RP OF TYR-175.
RX PubMed=27762317; DOI=10.1038/srep35169;
RA Lewis-Ballester A., Forouhar F., Kim S.M., Lew S., Wang Y., Karkashon S.,
RA Seetharaman J., Batabyal D., Chiang B.Y., Hussain M., Correia M.A.,
RA Yeh S.R., Tong L.;
RT "Molecular basis for catalysis and substrate-mediated cellular
RT stabilization of human tryptophan 2,3-dioxygenase.";
RL Sci. Rep. 6:35169-35169(2016).
CC -!- FUNCTION: Heme-dependent dioxygenase that catalyzes the oxidative
CC cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-
CC tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage
CC of the indole moiety. {ECO:0000255|HAMAP-Rule:MF_03020,
CC ECO:0000269|PubMed:25066423, ECO:0000269|PubMed:27762317,
CC ECO:0000269|PubMed:28285122}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan + O2 = N-formyl-L-kynurenine;
CC Xref=Rhea:RHEA:24536, ChEBI:CHEBI:15379, ChEBI:CHEBI:57912,
CC ChEBI:CHEBI:58629; EC=1.13.11.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03020, ECO:0000269|PubMed:25066423,
CC ECO:0000269|PubMed:27762317, ECO:0000269|PubMed:28285122};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03020,
CC ECO:0000269|PubMed:25066423, ECO:0000269|PubMed:27762317,
CC ECO:0000269|PubMed:28285122};
CC Note=Binds 1 heme group per subunit. {ECO:0000255|HAMAP-Rule:MF_03020,
CC ECO:0000269|PubMed:27762317};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.135 mM for L-tryptophan {ECO:0000269|PubMed:25066423};
CC KM=0.132 mM for L-tryptophan {ECO:0000269|PubMed:28285122};
CC Note=kcat is 0.54 sec(-1) with L-tryptophan as substrate.
CC {ECO:0000269|PubMed:28285122};
CC -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via
CC kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_03020, ECO:0000269|PubMed:25066423,
CC ECO:0000269|PubMed:27762317}.
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_03020, ECO:0000269|PubMed:25066423,
CC ECO:0000269|PubMed:27762317, ECO:0000269|PubMed:28285122}.
CC -!- INTERACTION:
CC P48775; O43865: AHCYL1; NbExp=3; IntAct=EBI-743494, EBI-2371423;
CC P48775; O95671: ASMTL; NbExp=11; IntAct=EBI-743494, EBI-743231;
CC P48775; P27797: CALR; NbExp=3; IntAct=EBI-743494, EBI-1049597;
CC P48775; P12830: CDH1; NbExp=3; IntAct=EBI-743494, EBI-727477;
CC P48775; P36957: DLST; NbExp=3; IntAct=EBI-743494, EBI-351007;
CC P48775; O60762: DPM1; NbExp=6; IntAct=EBI-743494, EBI-719526;
CC P48775; P06730: EIF4E; NbExp=4; IntAct=EBI-743494, EBI-73440;
CC P48775; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-743494, EBI-739832;
CC P48775; Q9H8S9: MOB1A; NbExp=6; IntAct=EBI-743494, EBI-748229;
CC P48775; Q70IA8: MOB3C; NbExp=3; IntAct=EBI-743494, EBI-9679267;
CC P48775; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-743494, EBI-1055945;
CC P48775; Q9NPG2: NGB; NbExp=6; IntAct=EBI-743494, EBI-10311409;
CC P48775; Q9HAN9: NMNAT1; NbExp=4; IntAct=EBI-743494, EBI-3917542;
CC P48775; P20393: NR1D1; NbExp=3; IntAct=EBI-743494, EBI-2811738;
CC P48775; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-743494, EBI-79165;
CC P48775; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-743494, EBI-11339910;
CC P48775; O00560: SDCBP; NbExp=7; IntAct=EBI-743494, EBI-727004;
CC P48775; Q9H190: SDCBP2; NbExp=4; IntAct=EBI-743494, EBI-742426;
CC P48775; P48775: TDO2; NbExp=6; IntAct=EBI-743494, EBI-743494;
CC P48775; Q68DK2-5: ZFYVE26; NbExp=6; IntAct=EBI-743494, EBI-8656416;
CC -!- DISEASE: Hypertryptophanemia (HYPTRP) [MIM:600627]: An autosomal
CC recessive condition characterized by persistent hypertryptophanemia and
CC hyperserotoninemia. {ECO:0000269|PubMed:28285122}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
CC {ECO:0000255|HAMAP-Rule:MF_03020}.
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; U32989; AAB08514.1; -; mRNA.
DR EMBL; AK289418; BAF82107.1; -; mRNA.
DR EMBL; CH471056; EAX04885.1; -; Genomic_DNA.
DR EMBL; BC005355; AAH05355.1; -; mRNA.
DR CCDS; CCDS34086.1; -.
DR PIR; G02022; G02022.
DR RefSeq; NP_005642.1; NM_005651.3.
DR PDB; 4PW8; X-ray; 2.90 A; A/B/C/D/E/F/G/H=19-388.
DR PDB; 5TI9; X-ray; 2.50 A; A/B/C/D=18-389.
DR PDB; 5TIA; X-ray; 2.44 A; A/B/C/D=18-389.
DR PDB; 6A4I; X-ray; 2.65 A; A/B/C/D=19-388.
DR PDB; 6PYY; X-ray; 2.40 A; A/B/C/D=18-389.
DR PDB; 6PYZ; X-ray; 2.02 A; A/B/C/D=18-389.
DR PDB; 6UD5; X-ray; 2.05 A; A/B/C/D=18-389.
DR PDB; 6VBN; X-ray; 3.18 A; A/B/C/D=18-388.
DR PDBsum; 4PW8; -.
DR PDBsum; 5TI9; -.
DR PDBsum; 5TIA; -.
DR PDBsum; 6A4I; -.
DR PDBsum; 6PYY; -.
DR PDBsum; 6PYZ; -.
DR PDBsum; 6UD5; -.
DR PDBsum; 6VBN; -.
DR AlphaFoldDB; P48775; -.
DR SMR; P48775; -.
DR BioGRID; 112858; 27.
DR IntAct; P48775; 24.
DR MINT; P48775; -.
DR STRING; 9606.ENSP00000444788; -.
DR BindingDB; P48775; -.
DR ChEMBL; CHEMBL2140; -.
DR DrugBank; DB00779; Nalidixic acid.
DR DrugBank; DB00500; Tolmetin.
DR DrugBank; DB00150; Tryptophan.
DR GuidetoPHARMACOLOGY; 2887; -.
DR iPTMnet; P48775; -.
DR PhosphoSitePlus; P48775; -.
DR BioMuta; TDO2; -.
DR DMDM; 1351188; -.
DR EPD; P48775; -.
DR MassIVE; P48775; -.
DR PaxDb; P48775; -.
DR PeptideAtlas; P48775; -.
DR PRIDE; P48775; -.
DR ProteomicsDB; 55947; -.
DR Antibodypedia; 28079; 324 antibodies from 25 providers.
DR DNASU; 6999; -.
DR Ensembl; ENST00000536354.3; ENSP00000444788.2; ENSG00000151790.9.
DR Ensembl; ENST00000573403.1; ENSP00000460086.1; ENSG00000262635.5.
DR GeneID; 6999; -.
DR KEGG; hsa:6999; -.
DR MANE-Select; ENST00000536354.3; ENSP00000444788.2; NM_005651.4; NP_005642.1.
DR UCSC; uc003ipf.3; human.
DR CTD; 6999; -.
DR DisGeNET; 6999; -.
DR GeneCards; TDO2; -.
DR HGNC; HGNC:11708; TDO2.
DR HPA; ENSG00000151790; Tissue enriched (liver).
DR MalaCards; TDO2; -.
DR MIM; 191070; gene.
DR MIM; 600627; phenotype.
DR neXtProt; NX_P48775; -.
DR OpenTargets; ENSG00000151790; -.
DR Orphanet; 2224; Hypertryptophanemia.
DR PharmGKB; PA36427; -.
DR VEuPathDB; HostDB:ENSG00000151790; -.
DR eggNOG; KOG3906; Eukaryota.
DR GeneTree; ENSGT00390000008593; -.
DR HOGENOM; CLU_045599_1_1_1; -.
DR InParanoid; P48775; -.
DR OMA; WRWRNDH; -.
DR OrthoDB; 497681at2759; -.
DR PhylomeDB; P48775; -.
DR TreeFam; TF105827; -.
DR BioCyc; MetaCyc:HS07771-MON; -.
DR BRENDA; 1.13.11.11; 2681.
DR BRENDA; 1.13.11.52; 2681.
DR PathwayCommons; P48775; -.
DR Reactome; R-HSA-71240; Tryptophan catabolism.
DR SABIO-RK; P48775; -.
DR SignaLink; P48775; -.
DR UniPathway; UPA00333; UER00453.
DR BioGRID-ORCS; 6999; 14 hits in 1068 CRISPR screens.
DR ChiTaRS; TDO2; human.
DR GeneWiki; TDO2; -.
DR GenomeRNAi; 6999; -.
DR Pharos; P48775; Tchem.
DR PRO; PR:P48775; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P48775; protein.
DR Bgee; ENSG00000151790; Expressed in right lobe of liver and 97 other tissues.
DR ExpressionAtlas; P48775; baseline and differential.
DR Genevisible; P48775; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016597; F:amino acid binding; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IEA:Ensembl.
DR GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:1904842; P:response to nitroglycerin; IEA:Ensembl.
DR GO; GO:0019442; P:tryptophan catabolic process to acetyl-CoA; IBA:GO_Central.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IDA:UniProtKB.
DR HAMAP; MF_01972; T23O; 1.
DR InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
DR InterPro; IPR004981; Trp_2_3_dOase.
DR PANTHER; PTHR10138; PTHR10138; 1.
DR Pfam; PF03301; Trp_dioxygenase; 1.
DR SUPFAM; SSF140959; SSF140959; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Disease variant; Heme; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome; Tryptophan catabolism.
FT CHAIN 1..406
FT /note="Tryptophan 2,3-dioxygenase"
FT /id="PRO_0000072399"
FT BINDING 72..76
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020,
FT ECO:0000269|PubMed:27762317, ECO:0007744|PDB:5TI9"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020,
FT ECO:0000269|PubMed:27762317, ECO:0007744|PDB:5TI9"
FT BINDING 328
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020,
FT ECO:0000269|PubMed:27762317, ECO:0007744|PDB:5TI9"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020,
FT ECO:0000269|PubMed:27762317, ECO:0007744|PDB:5TI9"
FT VARIANT 108
FT /note="M -> I (in HYPTRP; reduced tryptophan 2,3-
FT dioxygenase activity; does not affect homotetramerization;
FT dbSNP:rs1553957997)"
FT /evidence="ECO:0000269|PubMed:28285122"
FT /id="VAR_080251"
FT MUTAGEN 42
FT /note="Y->A: Reduces enzyme activity by 99%."
FT /evidence="ECO:0000269|PubMed:25066423"
FT MUTAGEN 45
FT /note="Y->A: Reduces enzyme activity by 99%."
FT /evidence="ECO:0000269|PubMed:25066423"
FT MUTAGEN 72
FT /note="F->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:25066423"
FT MUTAGEN 76
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:25066423"
FT MUTAGEN 140
FT /note="F->A: Reduces enzyme activity by 99%."
FT /evidence="ECO:0000269|PubMed:25066423"
FT MUTAGEN 144
FT /note="R->A: Reduces enzyme activity by 99%."
FT /evidence="ECO:0000269|PubMed:25066423"
FT MUTAGEN 151
FT /note="S->A: Reduces enzyme activity by 90%."
FT /evidence="ECO:0000269|PubMed:25066423"
FT MUTAGEN 175
FT /note="Y->G: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:27762317"
FT MUTAGEN 328
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:25066423"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 69..98
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 108..132
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:6PYZ"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:6PYZ"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6UD5"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:6PYZ"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 222..242
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 248..266
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 286..297
FT /evidence="ECO:0007829|PDB:6PYZ"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 305..336
FT /evidence="ECO:0007829|PDB:6PYZ"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6VBN"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 363..367
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:6PYZ"
FT HELIX 383..388
FT /evidence="ECO:0007829|PDB:6PYZ"
SQ SEQUENCE 406 AA; 47872 MW; 1B89901F445B79FE CRC64;
MSGCPFLGNN FGYTFKKLPV EGSEEDKSQT GVNRASKGGL IYGNYLHLEK VLNAQELQSE
TKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VVSRMHRVSV
ILKLLVQQFS ILETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQN MRVPYNRRHY
RDNFKGEENE LLLKSEQEKT LLELVEAWLE RTPGLEPHGF NFWGKLEKNI TRGLEEEFIR
IQAKEESEEK EEQVAEFQKQ KEVLLSLFDE KRHEHLLSKG ERRLSYRALQ GALMIYFYRE
EPRFQVPFQL LTSLMDIDSL MTKWRYNHVC MVHRMLGSKA GTGGSSGYHY LRSTVSDRYK
VFVDLFNLST YLIPRHWIPK MNPTIHKFLY TAEYCDSSYF SSDESD
