XXT1_ARATH
ID XXT1_ARATH Reviewed; 460 AA.
AC Q9LZJ3; B9DHH6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Xyloglucan 6-xylosyltransferase 1 {ECO:0000303|PubMed:12032363};
DE Short=AtXT1 {ECO:0000303|PubMed:12032363};
DE EC=2.4.2.39 {ECO:0000269|PubMed:16982611};
GN Name=XXT1 {ECO:0000303|PubMed:18544630};
GN Synonyms=XT1 {ECO:0000303|PubMed:12032363};
GN OrderedLocusNames=At3g62720 {ECO:0000312|Araport:AT3G62720};
GN ORFNames=F26K9_150 {ECO:0000312|EMBL:CAB83122.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, AND CHARACTERIZATION.
RX PubMed=12032363; DOI=10.1073/pnas.102644799;
RA Faik A., Price N.J., Raikhel N.V., Keegstra K.;
RT "An Arabidopsis gene encoding an alpha-xylosyltransferase involved in
RT xyloglucan biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7797-7802(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=16982611; DOI=10.1074/jbc.m606379200;
RA Cavalier D.M., Keegstra K.;
RT "Two xyloglucan xylosyltransferases catalyze the addition of multiple
RT xylosyl residues to cellohexaose.";
RL J. Biol. Chem. 281:34197-34207(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18544630; DOI=10.1105/tpc.108.059873;
RA Cavalier D.M., Lerouxel O., Neumetzler L., Yamauchi K., Reinecke A.,
RA Freshour G., Zabotina O.A., Hahn M.G., Burgert I., Pauly M., Raikhel N.V.,
RA Keegstra K.;
RT "Disrupting two Arabidopsis thaliana xylosyltransferase genes results in
RT plants deficient in xyloglucan, a major primary cell wall component.";
RL Plant Cell 20:1519-1537(2008).
RN [9]
RP NOMENCLATURE.
RX PubMed=18557833; DOI=10.1111/j.1365-313x.2008.03580.x;
RA Zabotina O.A., van de Ven W.T., Freshour G., Drakakaki G., Cavalier D.,
RA Mouille G., Hahn M.G., Keegstra K., Raikhel N.V.;
RT "Arabidopsis XXT5 gene encodes a putative alpha-1,6-xylosyltransferase that
RT is involved in xyloglucan biosynthesis.";
RL Plant J. 56:101-115(2008).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=21143678; DOI=10.1111/j.1365-313x.2010.04388.x;
RA Chevalier L., Bernard S., Ramdani Y., Lamour R., Bardor M., Lerouge P.,
RA Follet-Gueye M.L., Driouich A.;
RT "Subcompartment localization of the side chain xyloglucan-synthesizing
RT enzymes within Golgi stacks of tobacco suspension-cultured cells.";
RL Plant J. 64:977-989(2010).
RN [11]
RP INTERACTION WITH XXT2, AND SUBCELLULAR LOCATION.
RX PubMed=22665445; DOI=10.1104/pp.112.199356;
RA Chou Y.H., Pogorelko G., Zabotina O.A.;
RT "Xyloglucan xylosyltransferases XXT1, XXT2, and XXT5 and the glucan
RT synthase CSLC4 form Golgi-localized multiprotein complexes.";
RL Plant Physiol. 159:1355-1366(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 116-453 IN COMPLEX WITH UDP;
RP SUBSTRATE AND MANGANESE, FUNCTION, HOMODIMER, AND MUTAGENESIS OF LYS-206;
RP ASP-227; SER-228; ASP-229; ASN-268; ASP-317; ASP-318; GLN-319; HIS-377 AND
RP LYS-382.
RX PubMed=29784804; DOI=10.1073/pnas.1801105115;
RA Culbertson A.T., Ehrlich J.J., Choe J.Y., Honzatko R.B., Zabotina O.A.;
RT "Structure of xyloglucan xylosyltransferase 1 reveals simple steric rules
RT that define biological patterns of xyloglucan polymers.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:6064-6069(2018).
CC -!- FUNCTION: Xylosyltransferase specific to UDP-D-xylose that accepts both
CC cellopentaose and cellohexaose as substrates, with a better use of
CC cellohexaose, to produce xyloglucan. Adds preferentially the first
CC xylosyl residue to the fourth glucosyl residue from the reducing end of
CC both acceptors. Transfer one xylose mainly to the second glucose
CC residue from the non-reducing end. The acceptor should have a minimum
CC of four glucose residues. {ECO:0000269|PubMed:12032363,
CC ECO:0000269|PubMed:16982611, ECO:0000269|PubMed:18544630,
CC ECO:0000269|PubMed:29784804}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers an alpha-D-xylosyl residue from UDP-D-xylose to a
CC glucose residue in xyloglucan, forming an alpha-(1->6)-D-xylosyl-D-
CC glucose linkage.; EC=2.4.2.39;
CC Evidence={ECO:0000269|PubMed:16982611};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16982611};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:29784804};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: Forms homodimer (PubMed:29784804). Interacts with XXT2
CC (PubMed:22665445). {ECO:0000269|PubMed:22665445,
CC ECO:0000269|PubMed:29784804}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:21143678, ECO:0000269|PubMed:22665445}; Single-pass
CC type II membrane protein {ECO:0000305}. Note=Mainly located in the cis
CC and medial cisternae of Golgi apparatus. {ECO:0000269|PubMed:21143678}.
CC -!- DISRUPTION PHENOTYPE: Reduced xyloglucan content.
CC {ECO:0000269|PubMed:18544630}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 34 family.
CC {ECO:0000305}.
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DR EMBL; KJ138777; AHL38717.1; -; mRNA.
DR EMBL; AL162651; CAB83122.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80383.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80384.1; -; Genomic_DNA.
DR EMBL; AF424587; AAL11581.1; -; mRNA.
DR EMBL; BT002298; AAN73295.1; -; mRNA.
DR EMBL; AK317529; BAH20193.1; -; mRNA.
DR PIR; T48061; T48061.
DR RefSeq; NP_001030917.1; NM_001035840.2.
DR RefSeq; NP_191831.1; NM_116137.3.
DR PDB; 6BSU; X-ray; 1.50 A; A/B=116-453.
DR PDB; 6BSV; X-ray; 2.43 A; A/B=116-453.
DR PDB; 6BSW; X-ray; 2.16 A; A/B=116-453.
DR PDBsum; 6BSU; -.
DR PDBsum; 6BSV; -.
DR PDBsum; 6BSW; -.
DR AlphaFoldDB; Q9LZJ3; -.
DR SMR; Q9LZJ3; -.
DR BioGRID; 10760; 4.
DR STRING; 3702.AT3G62720.1; -.
DR CAZy; GT34; Glycosyltransferase Family 34.
DR PaxDb; Q9LZJ3; -.
DR PRIDE; Q9LZJ3; -.
DR ProteomicsDB; 242407; -.
DR EnsemblPlants; AT3G62720.1; AT3G62720.1; AT3G62720.
DR EnsemblPlants; AT3G62720.2; AT3G62720.2; AT3G62720.
DR GeneID; 825446; -.
DR Gramene; AT3G62720.1; AT3G62720.1; AT3G62720.
DR Gramene; AT3G62720.2; AT3G62720.2; AT3G62720.
DR KEGG; ath:AT3G62720; -.
DR Araport; AT3G62720; -.
DR TAIR; locus:2081625; AT3G62720.
DR eggNOG; KOG4748; Eukaryota.
DR HOGENOM; CLU_034328_1_1_1; -.
DR InParanoid; Q9LZJ3; -.
DR OMA; CIGAHRF; -.
DR OrthoDB; 1223199at2759; -.
DR PhylomeDB; Q9LZJ3; -.
DR BioCyc; ARA:AT3G62720-MON; -.
DR BioCyc; MetaCyc:AT3G62720-MON; -.
DR BRENDA; 2.4.2.39; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9LZJ3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZJ3; baseline and differential.
DR Genevisible; Q9LZJ3; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016758; F:hexosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IDA:TAIR.
DR GO; GO:0033843; F:xyloglucan 6-xylosyltransferase activity; IDA:TAIR.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IDA:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0009969; P:xyloglucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0010411; P:xyloglucan metabolic process; IDA:TAIR.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR008630; Glyco_trans_34.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR31311; PTHR31311; 1.
DR Pfam; PF05637; Glyco_transf_34; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..460
FT /note="Xyloglucan 6-xylosyltransferase 1"
FT /id="PRO_0000215169"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..460
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT BINDING 156
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:29784804,
FT ECO:0007744|PDB:6BSV"
FT BINDING 227..229
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:29784804,
FT ECO:0007744|PDB:6BSW"
FT BINDING 227
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:29784804"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:29784804"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29784804,
FT ECO:0007744|PDB:6BSW"
FT BINDING 377
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:29784804"
FT BINDING 377
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:29784804,
FT ECO:0007744|PDB:6BSW"
FT BINDING 380
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:29784804,
FT ECO:0007744|PDB:6BSW"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29784804,
FT ECO:0007744|PDB:6BSW"
FT BINDING 382
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:29784804,
FT ECO:0007744|PDB:6BSW"
FT BINDING 389..390
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29784804,
FT ECO:0007744|PDB:6BSW"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 206
FT /note="K->A: Reduces activity 2-fold."
FT /evidence="ECO:0000269|PubMed:29784804"
FT MUTAGEN 227
FT /note="D->A: Reduces activity 3-fold."
FT /evidence="ECO:0000269|PubMed:29784804"
FT MUTAGEN 227
FT /note="D->N: Reduces activity 2-fold; when associated with
FT N-229."
FT /evidence="ECO:0000269|PubMed:29784804"
FT MUTAGEN 228
FT /note="S->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:29784804"
FT MUTAGEN 229
FT /note="D->N: Reduces activity 2-fold; when associated with
FT N-227."
FT /evidence="ECO:0000269|PubMed:29784804"
FT MUTAGEN 268
FT /note="N->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:29784804"
FT MUTAGEN 317
FT /note="D->A: Reduces activity 40-fold."
FT /evidence="ECO:0000269|PubMed:29784804"
FT MUTAGEN 318
FT /note="D->A: Reduces activity 40-fold."
FT /evidence="ECO:0000269|PubMed:29784804"
FT MUTAGEN 319
FT /note="Q->A: Reduces activity 30-fold."
FT /evidence="ECO:0000269|PubMed:29784804"
FT MUTAGEN 377
FT /note="H->A: Reduces activity 1.5-fold."
FT /evidence="ECO:0000269|PubMed:29784804"
FT MUTAGEN 382
FT /note="K->A: Reduces activity 10-fold."
FT /evidence="ECO:0000269|PubMed:29784804"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:6BSU"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:6BSU"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 167..185
FT /evidence="ECO:0007829|PDB:6BSU"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:6BSU"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:6BSU"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:6BSU"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:6BSU"
FT STRAND 266..277
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:6BSU"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:6BSW"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:6BSU"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 356..362
FT /evidence="ECO:0007829|PDB:6BSU"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:6BSU"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:6BSW"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:6BSU"
FT HELIX 392..413
FT /evidence="ECO:0007829|PDB:6BSU"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:6BSU"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:6BSU"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:6BSU"
SQ SEQUENCE 460 AA; 53382 MW; 60227F8D009D9768 CRC64;
MIEKCIGAHR FRRLQRFMRQ GKVTILCLVL TVIVLRGTIG AGKFGTPEKD IEEIREHFFY
TRKRGEPHRV LVEVSSKTTS SEDGGNGGNS YETFDINKLF VDEGDEEKSR DRTNKPYSLG
PKISDWDEQR RDWLKQNPSF PNFVAPNKPR VLLVTGSAPK PCENPVGDHY LLKSIKNKID
YCRIHGIEIF YNMALLDAEM AGFWAKLPLI RKLLLSHPEI EFLWWMDSDA MFTDMVFELP
WERYKDYNLV MHGWNEMVYD QKNWIGLNTG SFLLRNSQWS LDLLDAWAPM GPKGKIREEA
GKVLTRELKD RPAFEADDQS AMVYLLATER EKWGGKVYLE SGYYLHGYWG ILVDRYEEMI
ENHKPGFGDH RWPLVTHFVG CKPCGKFGDY PVERCLRQMD RAFNFGDNQI LQMYGFTHKS
LGSRRVKPTR NQTDRPLDAK DEFGLLHPPF KAAKLSTTTT
