TBL29_ARATH
ID TBL29_ARATH Reviewed; 487 AA.
AC Q9LY46; Q8GWS5;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Xylan O-acetyltransferase 1 {ECO:0000303|PubMed:30083810};
DE EC=2.3.1.- {ECO:0000269|PubMed:30083810};
DE AltName: Full=Protein ESKIMO 1 {ECO:0000303|PubMed:17316173};
DE AltName: Full=Protein trichome birefringence-like 29 {ECO:0000303|PubMed:23340742};
GN Name=ESK1 {ECO:0000303|PubMed:17316173};
GN Synonyms=TBL29 {ECO:0000303|PubMed:23340742},
GN XOAT1 {ECO:0000303|PubMed:30083810};
GN OrderedLocusNames=At3g55990 {ECO:0000312|Araport:AT3G55990};
GN ORFNames=F27K19.170 {ECO:0000312|EMBL:CAB87853.1};
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 [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 [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 FUNCTION, MUTAGENESIS OF GLY-145; GLY-214 AND GLU-259, DISRUPTION
RP PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY COLD, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=17316173; DOI=10.1111/j.1365-313x.2006.02994.x;
RA Xin Z., Mandaokar A., Chen J., Last R.L., Browse J.;
RT "Arabidopsis ESK1 encodes a novel regulator of freezing tolerance.";
RL Plant J. 49:786-799(2007).
RN [5]
RP FUNCTION.
RX PubMed=19061521; DOI=10.1186/1471-2229-8-125;
RA Bouchabke-Coussa O., Quashie M.L., Seoane-Redondo J., Fortabat M.N.,
RA Gery C., Yu A., Linderme D., Trouverie J., Granier F., Teoule E.,
RA Durand-Tardif M.;
RT "ESKIMO1 is a key gene involved in water economy as well as cold
RT acclimation and salt tolerance.";
RL BMC Plant Biol. 8:125-125(2008).
RN [6]
RP FUNCTION.
RX PubMed=19054354; DOI=10.1111/j.1365-3040.2008.01898.x;
RA Lugan R., Niogret M.F., Kervazo L., Larher F.R., Kopka J., Bouchereau A.;
RT "Metabolome and water status phenotyping of Arabidopsis under abiotic
RT stress cues reveals new insight into ESK1 function.";
RL Plant Cell Environ. 32:95-108(2009).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20388664; DOI=10.1104/pp.110.153320;
RA Bischoff V., Nita S., Neumetzler L., Schindelasch D., Urbain A., Eshed R.,
RA Persson S., Delmer D., Scheible W.R.;
RT "TRICHOME BIREFRINGENCE and its homolog AT5G01360 encode plant-specific
RT DUF231 proteins required for cellulose biosynthesis in Arabidopsis.";
RL Plant Physiol. 153:590-602(2010).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21408051; DOI=10.1371/journal.pone.0016645;
RA Lefebvre V., Fortabat M.N., Ducamp A., North H.M., Maia-Grondard A.,
RA Trouverie J., Boursiac Y., Mouille G., Durand-Tardif M.;
RT "ESKIMO1 disruption in Arabidopsis alters vascular tissue and impairs water
RT transport.";
RL PLoS ONE 6:E16645-E16645(2011).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=23340742; DOI=10.1093/mp/sst014;
RA Xiong G., Cheng K., Pauly M.;
RT "Xylan O-acetylation impacts xylem development and enzymatic recalcitrance
RT as indicated by the Arabidopsis mutant tbl29.";
RL Mol. Plant 6:1373-1375(2013).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23659919; DOI=10.1093/pcp/pct070;
RA Yuan Y., Teng Q., Zhong R., Ye Z.H.;
RT "The Arabidopsis DUF231 domain-containing protein ESK1 mediates 2-O- and 3-
RT O-acetylation of xylosyl residues in xylan.";
RL Plant Cell Physiol. 54:1186-1199(2013).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30083810; DOI=10.1007/s00425-018-2972-0;
RA Zhong R., Cui D., Ye Z.H.;
RT "Xyloglucan O-acetyltransferases from Arabidopsis thaliana and Populus
RT trichocarpa catalyze acetylation of fucosylated galactose residues on
RT xyloglucan side chains.";
RL Planta 248:1159-1171(2018).
RN [12]
RP 3D-STRUCTURE MODELING.
RX PubMed=20657172; DOI=10.4161/psb.5.8.12414;
RA Bischoff V., Selbig J., Scheible W.R.;
RT "Involvement of TBL/DUF231 proteins into cell wall biology.";
RL Plant Signal. Behav. 5:1057-1059(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), FUNCTION, ACTIVE SITES, DISULFIDE
RP BONDS, ACETYLATION AT SER-216, GLYCOSYLATION AT ASN-151; ASN-241; ASN-255;
RP ASN-393; ASN-412 AND ASN-425, AND MUTAGENESIS OF ASP-215; SER-216; ARG-219;
RP ASN-220; HIS-437; ASP-462 AND HIS-465.
RX PubMed=32354790; DOI=10.1105/tpc.20.00028;
RA Lunin V.V., Wang H.T., Bharadwaj V.S., Alahuhta M., Pena M.J., Yang J.Y.,
RA Archer-Hartmann S.A., Azadi P., Himmel M.E., Moremen K.W., York W.S.,
RA Bomble Y.J., Urbanowicz B.R.;
RT "Molecular mechanism of polysaccharide acetylation by the Arabidopsis xylan
RT O-acetyltransferase XOAT1.";
RL Plant Cell 32:2367-2382(2020).
CC -!- FUNCTION: Xylan acetyltransferase required for 2-O- and 3-O-
CC monoacetylation of xylosyl residues in xylan (PubMed:23659919,
CC PubMed:30083810, PubMed:32354790). Catalyzes the 2-O-acetylation of
CC xylan, followed by nonenzymatic acetyl migration to the O-3 position,
CC resulting in products that are monoacetylated at both O-2 and O-3
CC positions (PubMed:32354790). Is necessary for the formation of the
CC functional xylem, which is required for water transport to aerial
CC tissues (PubMed:21408051, PubMed:23340742). Acts as negative regulator
CC of cold acclimation (PubMed:17316173). Involved in water economy as
CC well as salt tolerance (PubMed:19061521, PubMed:19054354). Regulated at
CC the transcriptional level by NAC012/SND1 (Probable).
CC {ECO:0000269|PubMed:17316173, ECO:0000269|PubMed:19054354,
CC ECO:0000269|PubMed:19061521, ECO:0000269|PubMed:21408051,
CC ECO:0000269|PubMed:23340742, ECO:0000269|PubMed:23659919,
CC ECO:0000269|PubMed:30083810, ECO:0000269|PubMed:32354790, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, young seedlings, leaves, stems,
CC flowers and developing siliques. Specifically expressed in secondary
CC wall-forming cells, xylem and interfascicular fibers.
CC {ECO:0000269|PubMed:17316173, ECO:0000269|PubMed:21408051,
CC ECO:0000269|PubMed:23340742, ECO:0000269|PubMed:23659919}.
CC -!- INDUCTION: Not induced during cold acclimation.
CC {ECO:0000269|PubMed:17316173}.
CC -!- DISRUPTION PHENOTYPE: Strong constitutive freezing tolerance. Altered
CC vascular apparatus morphology, and reduced xylan acetylation and
CC secondary wall thickening. Reduced rosette-leaf growth and
CC inflorescence size. {ECO:0000269|PubMed:17316173,
CC ECO:0000269|PubMed:21408051, ECO:0000269|PubMed:23340742,
CC ECO:0000269|PubMed:23659919}.
CC -!- MISCELLANEOUS: Contains 2 motifs that are conserved in esterases, but
CC it is unlikely that this protein belongs to the catalytically active
CC pectin esterases. {ECO:0000305|PubMed:20657172}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
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DR EMBL; AL163832; CAB87853.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79464.1; -; Genomic_DNA.
DR EMBL; AK118662; BAC43257.1; -; mRNA.
DR PIR; T49211; T49211.
DR RefSeq; NP_191158.1; NM_115457.3.
DR PDB; 6CCI; X-ray; 1.85 A; A=1-487.
DR PDBsum; 6CCI; -.
DR AlphaFoldDB; Q9LY46; -.
DR SMR; Q9LY46; -.
DR BioGRID; 10081; 4.
DR IntAct; Q9LY46; 4.
DR STRING; 3702.AT3G55990.1; -.
DR PaxDb; Q9LY46; -.
DR PRIDE; Q9LY46; -.
DR ProteomicsDB; 234143; -.
DR EnsemblPlants; AT3G55990.1; AT3G55990.1; AT3G55990.
DR GeneID; 824765; -.
DR Gramene; AT3G55990.1; AT3G55990.1; AT3G55990.
DR KEGG; ath:AT3G55990; -.
DR Araport; AT3G55990; -.
DR TAIR; locus:2082078; AT3G55990.
DR eggNOG; ENOG502QUBK; Eukaryota.
DR HOGENOM; CLU_020953_3_2_1; -.
DR InParanoid; Q9LY46; -.
DR OMA; PEMKILH; -.
DR OrthoDB; 492414at2759; -.
DR PhylomeDB; Q9LY46; -.
DR PRO; PR:Q9LY46; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY46; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; 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:0016413; F:O-acetyltransferase activity; IDA:TAIR.
DR GO; GO:1990538; F:xylan O-acetyltransferase activity; IDA:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0050826; P:response to freezing; IMP:TAIR.
DR GO; GO:0045492; P:xylan biosynthetic process; IDA:TAIR.
DR InterPro; IPR026057; PC-Esterase.
DR InterPro; IPR029962; TBL.
DR InterPro; IPR025846; TBL_N.
DR InterPro; IPR029979; XOAT1.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR PANTHER; PTHR32285:SF296; PTHR32285:SF296; 1.
DR Pfam; PF13839; PC-Esterase; 1.
DR Pfam; PF14416; PMR5N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..487
FT /note="Xylan O-acetyltransferase 1"
FT /id="PRO_0000425394"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..487
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 214..216
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT MOTIF 462..465
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT ACT_SITE 216
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:32354790"
FT ACT_SITE 462
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:32354790"
FT ACT_SITE 465
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:32354790"
FT MOD_RES 216
FT /note="O-acetylserine"
FT /evidence="ECO:0000269|PubMed:32354790"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:32354790, ECO:0007744|PDB:6CCI"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:32354790, ECO:0007744|PDB:6CCI"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:32354790, ECO:0007744|PDB:6CCI"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:32354790, ECO:0007744|PDB:6CCI"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:32354790, ECO:0007744|PDB:6CCI"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:32354790, ECO:0007744|PDB:6CCI"
FT DISULFID 140..191
FT /evidence="ECO:0000269|PubMed:32354790,
FT ECO:0007744|PDB:6CCI"
FT DISULFID 162..227
FT /evidence="ECO:0000269|PubMed:32354790,
FT ECO:0007744|PDB:6CCI"
FT DISULFID 171..467
FT /evidence="ECO:0000269|PubMed:32354790,
FT ECO:0007744|PDB:6CCI"
FT DISULFID 384..463
FT /evidence="ECO:0000269|PubMed:32354790,
FT ECO:0007744|PDB:6CCI"
FT MUTAGEN 145
FT /note="G->R: In esk1-1; increased freezing tolerance."
FT /evidence="ECO:0000269|PubMed:17316173"
FT MUTAGEN 214
FT /note="G->E: In esk1-2; increased freezing tolerance."
FT /evidence="ECO:0000269|PubMed:17316173"
FT MUTAGEN 215
FT /note="D->A: Almost abolishes transferase activity."
FT /evidence="ECO:0000269|PubMed:32354790"
FT MUTAGEN 216
FT /note="S->A: Abolishes transferase activity."
FT /evidence="ECO:0000269|PubMed:32354790"
FT MUTAGEN 219
FT /note="R->A: Decreases transferase activity 2-fold."
FT /evidence="ECO:0000269|PubMed:32354790"
FT MUTAGEN 220
FT /note="N->A: No effect on transferase activity."
FT /evidence="ECO:0000269|PubMed:32354790"
FT MUTAGEN 259
FT /note="E->K: In esk1-3; increased freezing tolerance."
FT /evidence="ECO:0000269|PubMed:17316173"
FT MUTAGEN 437
FT /note="H->A: Decreases transferase activity 3-fold."
FT /evidence="ECO:0000269|PubMed:32354790"
FT MUTAGEN 462
FT /note="D->A: Abolishes transferase activity."
FT /evidence="ECO:0000269|PubMed:32354790"
FT MUTAGEN 465
FT /note="H->A: Abolishes transferase activity."
FT /evidence="ECO:0000269|PubMed:32354790"
FT CONFLICT 343
FT /note="M -> I (in Ref. 3; BAC43257)"
FT /evidence="ECO:0000305"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:6CCI"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6CCI"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:6CCI"
FT TURN 171..175
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:6CCI"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 216..230
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:6CCI"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 311..321
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 335..353
FT /evidence="ECO:0007829|PDB:6CCI"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:6CCI"
FT TURN 383..386
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 404..416
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 427..431
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 457..460
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:6CCI"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:6CCI"
FT HELIX 471..484
FT /evidence="ECO:0007829|PDB:6CCI"
SQ SEQUENCE 487 AA; 56695 MW; 3B7D2AFFF79B6AAE CRC64;
MQPWRRKFPL FETGVTMKQR KNSNLSIFVV VFSVFLFGIF MYNEDVKSIA EFPFSTSKPH
DVHDEATPIT EITTLPVQES IKNSDPIQES IKNADSVQDS VKDVAEPVQE EVSKTEEVKK
IELFAATEDE EDVELPPEEC DLFTGEWVFD NETHPLYKED QCEFLTAQVT CMRNGRRDSL
YQNWRWQPRD CSLPKFKAKL LLEKLRNKRM MFVGDSLNRN QWESMVCLVQ SVVPPGRKSL
NKTGSLSVFR VEDYNATVEF YWAPFLVESN SDDPNMHSIL NRIIMPESIE KHGVNWKGVD
FLVFNTYIWW MNTFAMKVLR GSFDKGDTEY EEIERPVAYR RVMRTWGDWV ERNIDPLRTT
VFFASMSPLH IKSLDWENPD GIKCALETTP ILNMSMPFSV GTDYRLFSVA ENVTHSLNVP
VYFLNITKLS EYRKDAHTSV HTIRQGKMLT PEQQADPNTY ADCIHWCLPG LPDTWNEFLY
TRIISRS
