TAA1_ARATH
ID TAA1_ARATH Reviewed; 391 AA.
AC Q9S7N2;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=L-tryptophan--pyruvate aminotransferase 1;
DE EC=2.6.1.27;
DE EC=2.6.1.99;
DE AltName: Full=Protein CYTOKININ INDUCED ROOT CURLING 1;
DE AltName: Full=Protein SHADE AVOIDANCE 3;
DE AltName: Full=Protein TRANSPORT INHIBITOR RESPONSE 2;
DE AltName: Full=Protein TRYPTOPHAN AMINOTRANSFERASE OF ARABIDOPSIS 1;
DE AltName: Full=Protein WEAK ETHYLENE INSENSITIVE 8;
DE AltName: Full=Tryptophan transaminase;
GN Name=TAA1; Synonyms=CKRC1, SAV3, TIR2, WEI8; OrderedLocusNames=At1g70560;
GN ORFNames=F24J13.13, F5A18.26;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-166 AND LYS-217.
RX PubMed=18394997; DOI=10.1016/j.cell.2008.01.047;
RA Stepanova A.N., Robertson-Hoyt J., Yun J., Benavente L.M., Xie D.Y.,
RA Dolezal K., Schlereth A., Juergens G., Alonso J.M.;
RT "TAA1-mediated auxin biosynthesis is essential for hormone crosstalk and
RT plant development.";
RL Cell 133:177-191(2008).
RN [6]
RP FUNCTION, MUTAGENESIS OF GLY-171, TISSUE SPECIFICITY, INDUCTION BY AUXIN
RP AND HEAT, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=19625638; DOI=10.1104/pp.109.138859;
RA Yamada M., Greenham K., Prigge M.J., Jensen P.J., Estelle M.;
RT "The TRANSPORT INHIBITOR RESPONSE2 gene is required for auxin synthesis and
RT diverse aspects of plant development.";
RL Plant Physiol. 151:168-179(2009).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=22108404; DOI=10.1105/tpc.111.089029;
RA He W., Brumos J., Li H., Ji Y., Ke M., Gong X., Zeng Q., Li W., Zhang X.,
RA An F., Wen X., Li P., Chu J., Sun X., Yan C., Yan N., Xie D.Y., Raikhel N.,
RA Yang Z., Stepanova A.N., Alonso J.M., Guo H.;
RT "A small-molecule screen identifies L-kynurenine as a competitive inhibitor
RT of TAA1/TAR activity in ethylene-directed auxin biosynthesis and root
RT growth in Arabidopsis.";
RL Plant Cell 23:3944-3960(2011).
RN [8]
RP TISSUE SPECIFICITY, INDUCTION BY ETHYLENE AND CYTOKININ, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21255165; DOI=10.1111/j.1365-313x.2011.04509.x;
RA Zhou Z.Y., Zhang C.G., Wu L., Zhang C.G., Chai J., Wang M., Jha A.,
RA Jia P.F., Cui S.J., Yang M., Chen R., Guo G.Q.;
RT "Functional characterization of the CKRC1/TAA1 gene and dissection of
RT hormonal actions in the Arabidopsis root.";
RL Plant J. 66:516-527(2011).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22025724; DOI=10.1073/pnas.1108434108;
RA Mashiguchi K., Tanaka K., Sakai T., Sugawara S., Kawaide H., Natsume M.,
RA Hanada A., Yaeno T., Shirasu K., Yao H., McSteen P., Zhao Y., Hayashi K.,
RA Kamiya Y., Kasahara H.;
RT "The main auxin biosynthesis pathway in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18512-18517(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH PYRIDOXAMINE
RP PHOSPHATE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY SHADE, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LYS-217 AND GLY-250.
RX PubMed=18394996; DOI=10.1016/j.cell.2008.01.049;
RA Tao Y., Ferrer J.L., Ljung K., Pojer F., Hong F., Long J.A., Li L.,
RA Moreno J.E., Bowman M.E., Ivans L.J., Cheng Y., Lim J., Zhao Y.,
RA Ballare C.L., Sandberg G., Noel J.P., Chory J.;
RT "Rapid synthesis of auxin via a new tryptophan-dependent pathway is
RT required for shade avoidance in plants.";
RL Cell 133:164-176(2008).
CC -!- FUNCTION: L-tryptophan aminotransferase involved in auxin (IAA)
CC biosynthesis. Can convert L-tryptophan and pyruvate to indole-3-pyruvic
CC acid (IPA) and alanine. Catalyzes the first step in IPA branch of the
CC auxin biosynthetic pathway. Required for auxin production to initiate
CC multiple change in growth in response to environmental and
CC developmental cues. It is also active with phenylalanine, tyrosine,
CC leucine, alanine, methionine and glutamine. Both TAA1 and TAR2 are
CC required for maintaining proper auxin levels in roots, while TAA1, TAR1
CC and TAR2 are required for proper embryo patterning. Involved in the
CC maintenance of the root stem cell niches and required for shade
CC avoidance. {ECO:0000269|PubMed:18394996, ECO:0000269|PubMed:18394997,
CC ECO:0000269|PubMed:19625638, ECO:0000269|PubMed:22025724}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-tryptophan = indole-3-pyruvate + L-
CC glutamate; Xref=Rhea:RHEA:14093, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:29985, ChEBI:CHEBI:57912; EC=2.6.1.27;
CC Evidence={ECO:0000269|PubMed:22025724};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan + pyruvate = indole-3-pyruvate + L-alanine;
CC Xref=Rhea:RHEA:27586, ChEBI:CHEBI:15361, ChEBI:CHEBI:17640,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:57972; EC=2.6.1.99;
CC Evidence={ECO:0000269|PubMed:22025724};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: Inhibited by L-kynurenine.
CC {ECO:0000269|PubMed:22108404}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.29 mM for L-tryptophan {ECO:0000269|PubMed:18394996};
CC KM=4.74 mM for tyrosine {ECO:0000269|PubMed:18394996};
CC KM=9.35 mM for phenylalanine {ECO:0000269|PubMed:18394996};
CC Vmax=25.8 umol/min/ug enzyme with L-tryptophan as substrate
CC {ECO:0000269|PubMed:18394996};
CC Vmax=28 umol/min/ug enzyme with tyrosine as substrate
CC {ECO:0000269|PubMed:18394996};
CC Vmax=10.6 umol/min/ug enzyme with phenylalanine as substrate
CC {ECO:0000269|PubMed:18394996};
CC pH dependence:
CC Optimum pH is 8.8. {ECO:0000269|PubMed:18394996};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:18394996};
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18394996}.
CC -!- TISSUE SPECIFICITY: Expressed at the leaf margin and in the vasculature
CC of emerging young leaves. Expressed in the quiescent center and in the
CC vasculature of root tips. Detected in the shoot apical meristem, stems,
CC sepals, stamen filaments, the shoot and root junction, the stigma and
CC the base of the silique. {ECO:0000269|PubMed:18394996,
CC ECO:0000269|PubMed:19625638, ECO:0000269|PubMed:21255165}.
CC -!- DEVELOPMENTAL STAGE: In the heart stage embryo, expressed in the
CC developing vasculature and the apical epidermal layer. At the torpedo
CC stage expressed in the developing vasculature of the root, hypocotyl
CC and cotyledons, as well as in the L1 layer of the presumptive shoot
CC apical meristem and the adaxial epidermis of the developing cotyledons.
CC In flowers, the expression is first restricted to the central outer
CC layers of flower primordia, but later expands toward the base of
CC gynoecia, becoming limited to two cell files along the meristematic
CC medial ridge. {ECO:0000269|PubMed:18394996,
CC ECO:0000269|PubMed:19625638}.
CC -!- INDUCTION: Up-regulated by trans-zeatin, ethylene and high temperature.
CC Down-regulated by auxin and shade treatment.
CC {ECO:0000269|PubMed:18394996, ECO:0000269|PubMed:19625638,
CC ECO:0000269|PubMed:21255165}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, but exhibits reduced levels of auxin (IAA), reduced auxin
CC response, reduced sensitivity to ethylene and shorter hypocotyls and
CC petioles but larger leaf area when grown in simulated shade. Defective
CC in root gravitropic response and shows an increased resistance to
CC cytokinin in primary root growth. {ECO:0000269|PubMed:18394996,
CC ECO:0000269|PubMed:18394997, ECO:0000269|PubMed:19625638,
CC ECO:0000269|PubMed:21255165}.
CC -!- SIMILARITY: Belongs to the alliinase family. {ECO:0000305}.
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DR EMBL; AC010796; AAG52476.1; -; Genomic_DNA.
DR EMBL; AC011663; AAG52348.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35079.1; -; Genomic_DNA.
DR EMBL; AK117208; BAC41884.1; -; mRNA.
DR EMBL; BT005339; AAO63403.1; -; mRNA.
DR PIR; F96729; F96729.
DR RefSeq; NP_177213.1; NM_105724.3.
DR PDB; 3BWN; X-ray; 2.25 A; A/B/C/D/E/F=1-391.
DR PDB; 3BWO; X-ray; 2.40 A; A/B/C/D/E/F=1-391.
DR PDBsum; 3BWN; -.
DR PDBsum; 3BWO; -.
DR AlphaFoldDB; Q9S7N2; -.
DR SMR; Q9S7N2; -.
DR STRING; 3702.AT1G70560.1; -.
DR PaxDb; Q9S7N2; -.
DR PRIDE; Q9S7N2; -.
DR ProteomicsDB; 234114; -.
DR EnsemblPlants; AT1G70560.1; AT1G70560.1; AT1G70560.
DR GeneID; 843393; -.
DR Gramene; AT1G70560.1; AT1G70560.1; AT1G70560.
DR KEGG; ath:AT1G70560; -.
DR Araport; AT1G70560; -.
DR TAIR; locus:2026826; AT1G70560.
DR eggNOG; ENOG502QTGD; Eukaryota.
DR HOGENOM; CLU_036760_2_0_1; -.
DR InParanoid; Q9S7N2; -.
DR OMA; CAAPYYS; -.
DR OrthoDB; 457006at2759; -.
DR PhylomeDB; Q9S7N2; -.
DR BioCyc; ARA:AT1G70560-MON; -.
DR BioCyc; MetaCyc:AT1G70560-MON; -.
DR BRENDA; 2.6.1.27; 399.
DR BRENDA; 2.6.1.99; 399.
DR UniPathway; UPA00151; -.
DR EvolutionaryTrace; Q9S7N2; -.
DR PRO; PR:Q9S7N2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S7N2; baseline and differential.
DR Genevisible; Q9S7N2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR GO; GO:0080100; F:L-glutamine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR GO; GO:0080099; F:L-methionine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR GO; GO:0047312; F:L-phenylalanine:pyruvate aminotransferase activity; IDA:TAIR.
DR GO; GO:0050362; F:L-tryptophan:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR GO; GO:0080097; F:L-tryptophan:pyruvate aminotransferase activity; IDA:TAIR.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR GO; GO:0080098; F:L-tyrosine:pyruvate aminotransferase activity; IDA:TAIR.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:TAIR.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0048825; P:cotyledon development; IGI:TAIR.
DR GO; GO:0010588; P:cotyledon vascular tissue pattern formation; IGI:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IGI:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0009908; P:flower development; IGI:TAIR.
DR GO; GO:0048467; P:gynoecium development; IGI:TAIR.
DR GO; GO:0009684; P:indoleacetic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0010078; P:maintenance of root meristem identity; IGI:TAIR.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IGI:TAIR.
DR GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
DR GO; GO:0080022; P:primary root development; IGI:TAIR.
DR GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0009641; P:shade avoidance; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IGI:TAIR.
DR Gene3D; 2.10.25.30; -; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR006948; Alliinase_C.
DR InterPro; IPR037029; Alliinase_N_sf.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF04864; Alliinase_C; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Auxin biosynthesis; Cytoplasm;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..391
FT /note="L-tryptophan--pyruvate aminotransferase 1"
FT /id="PRO_0000401375"
FT BINDING 58
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:18394996,
FT ECO:0007744|PDB:3BWN"
FT BINDING 100..101
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:18394996,
FT ECO:0007744|PDB:3BWN"
FT BINDING 168
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:18394996,
FT ECO:0007744|PDB:3BWN"
FT BINDING 191..194
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:18394996,
FT ECO:0007744|PDB:3BWN"
FT BINDING 214..217
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:18394996,
FT ECO:0007744|PDB:3BWN"
FT BINDING 225
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:18394996,
FT ECO:0007744|PDB:3BWN"
FT MOD_RES 217
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
FT MUTAGEN 166
FT /note="P->S: In wei8-2; loss of activity."
FT /evidence="ECO:0000269|PubMed:18394997"
FT MUTAGEN 171
FT /note="G->E: In tir2-1; loss of activity."
FT /evidence="ECO:0000269|PubMed:19625638"
FT MUTAGEN 217
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18394996,
FT ECO:0000269|PubMed:18394997"
FT MUTAGEN 217
FT /note="K->G,R: Reduces growth rate under shade condition."
FT /evidence="ECO:0000269|PubMed:18394996,
FT ECO:0000269|PubMed:18394997"
FT MUTAGEN 250
FT /note="G->S: In sav3-3; reduces growth rate under shade
FT condition."
FT /evidence="ECO:0000269|PubMed:18394996"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3BWN"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:3BWN"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:3BWN"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 234..248
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 253..269
FT /evidence="ECO:0007829|PDB:3BWN"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 279..299
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:3BWN"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 326..335
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:3BWN"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:3BWN"
FT HELIX 370..381
FT /evidence="ECO:0007829|PDB:3BWN"
SQ SEQUENCE 391 AA; 44801 MW; 7038D6C93E122614 CRC64;
MVKLENSRKP EKISNKNIPM SDFVVNLDHG DPTAYEEYWR KMGDRCTVTI RGCDLMSYFS
DMTNLCWFLE PELEDAIKDL HGVVGNAATE DRYIVVGTGS TQLCQAAVHA LSSLARSQPV
SVVAAAPFYS TYVEETTYVR SGMYKWEGDA WGFDKKGPYI ELVTSPNNPD GTIRETVVNR
PDDDEAKVIH DFAYYWPHYT PITRRQDHDI MLFTFSKITG HAGSRIGWAL VKDKEVAKKM
VEYIIVNSIG VSKESQVRTA KILNVLKETC KSESESENFF KYGREMMKNR WEKLREVVKE
SDAFTLPKYP EAFCNYFGKS LESYPAFAWL GTKEETDLVS ELRRHKVMSR AGERCGSDKK
HVRVSMLSRE DVFNVFLERL ANMKLIKSID L
