CESA6_ARATH
ID CESA6_ARATH Reviewed; 1084 AA.
AC Q94JQ6; O65338; Q0WNG4; Q9FGF9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cellulose synthase A catalytic subunit 6 [UDP-forming];
DE Short=AtCesA6;
DE EC=2.4.1.12;
DE AltName: Full=AraxCelA;
DE AltName: Full=Isoxaben-resistant protein 2;
DE AltName: Full=Protein PROCUSTE 1;
DE AltName: Full=Protein QUILL;
GN Name=CESA6; Synonyms=IXR2, PRC1, QUI; OrderedLocusNames=At5g64740;
GN ORFNames=MVP7.7;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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] OF 1-771.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-1084.
RC STRAIN=cv. Columbia;
RA Wu L., Joshi C.P., Chiang V.L.;
RT "AraxCelA, a new member of cellulose synthase gene family from Arabidopsis
RT thaliana.";
RL (er) Plant Gene Register PGR98-114(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 637-1084.
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 [6]
RP FUNCTION.
RX PubMed=7743935; DOI=10.1242/dev.121.4.1237;
RA Hauser M.-T., Morikami A., Benfey P.N.;
RT "Conditional root expansion mutants of Arabidopsis.";
RL Development 121:1237-1252(1995).
RN [7]
RP FUNCTION.
RX PubMed=8625819; DOI=10.1242/dev.122.2.683;
RA Desnos T., Orbovic V., Bellini C., Kronenberger J., Caboche M., Traas J.,
RA Hoefte H.;
RT "Procuste1 mutants identify two distinct genetic pathways controlling
RT hypocotyl cell elongation, respectively in dark- and light-grown
RT Arabidopsis seedlings.";
RL Development 122:683-693(1996).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11178255; DOI=10.1186/gb-2000-1-4-reviews3001;
RA Richmond T.;
RT "Higher plant cellulose synthases.";
RL Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11148287; DOI=10.2307/3871238;
RA Fagard M., Desnos T., Desprez T., Goubet F., Refregier G., Mouille G.,
RA McCann M., Rayon C., Vernhettes S., Hoefte H.;
RT "PROCUSTE1 encodes a cellulose synthase required for normal cell elongation
RT specifically in roots and dark-grown hypocotyls of Arabidopsis.";
RL Plant Cell 12:2409-2423(2000).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ARG-1064.
RX PubMed=11842152; DOI=10.1104/pp.010822;
RA Desprez T., Vernhettes S., Fagard M., Refregier G., Desnos T., Aletti E.,
RA Py N., Pelletier S., Hoefte H.;
RT "Resistance against herbicide isoxaben and cellulose deficiency caused by
RT distinct mutations in same cellulose synthase isoform CESA6.";
RL Plant Physiol. 128:482-490(2002).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=12481071; DOI=10.1104/pp.102.010603;
RA Beeckman T., Przemeck G.K.H., Stamatiou G., Lau R., Terryn N., De Rycke R.,
RA Inze D., Berleth T.;
RT "Genetic complexity of cellulose synthase A gene function in Arabidopsis
RT embryogenesis.";
RL Plant Physiol. 130:1883-1893(2002).
RN [12]
RP FUNCTION.
RX PubMed=16627697; DOI=10.1126/science.1126551;
RA Paredez A.R., Somerville C.R., Ehrhardt D.W.;
RT "Visualization of cellulose synthase demonstrates functional association
RT with microtubules.";
RL Science 312:1491-1495(2006).
RN [13]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17878302; DOI=10.1073/pnas.0706592104;
RA Persson S., Paredez A., Carroll A., Palsdottir H., Doblin M.,
RA Poindexter P., Khitrov N., Auer M., Somerville C.R.;
RT "Genetic evidence for three unique components in primary cell-wall
RT cellulose synthase complexes in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15566-15571(2007).
RN [14]
RP FUNCTION, AND INTERACTION WITH CESA1 AND CESA3.
RX PubMed=17878303; DOI=10.1073/pnas.0706569104;
RA Desprez T., Juraniec M., Crowell E.F., Jouy H., Pochylova Z., Parcy F.,
RA Hoefte H., Gonneau M., Vernhettes S.;
RT "Organization of cellulose synthase complexes involved in primary cell wall
RT synthesis in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15572-15577(2007).
RN [15]
RP INTERACTION WITH CSI1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=20616083; DOI=10.1073/pnas.1007092107;
RA Gu Y., Kaplinsky N., Bringmann M., Cobb A., Carroll A., Sampathkumar A.,
RA Baskin T.I., Persson S., Somerville C.R.;
RT "Identification of a cellulose synthase-associated protein required for
RT cellulose biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12866-12871(2010).
RN [16]
RP INTERACTION WITH CSI1 AND CSI3.
RX PubMed=24368796; DOI=10.1105/tpc.113.116715;
RA Lei L., Li S., Du J., Bashline L., Gu Y.;
RT "Cellulose synthase INTERACTIVE3 regulates cellulose biosynthesis in both a
RT microtubule-dependent and microtubule-independent manner in Arabidopsis.";
RL Plant Cell 25:4912-4923(2013).
RN [17]
RP INTERACTION WITH STL1 AND STL2, AND LACK OF INTERACTION WITH GOT1.
RX PubMed=27277162; DOI=10.1038/ncomms11656;
RA Zhang Y., Nikolovski N., Sorieul M., Vellosillo T., McFarlane H.E.,
RA Dupree R., Kesten C., Schneider R., Driemeier C., Lathe R., Lampugnani E.,
RA Yu X., Ivakov A., Doblin M.S., Mortimer J.C., Brown S.P., Persson S.,
RA Dupree P.;
RT "Golgi-localized STELLO proteins regulate the assembly and trafficking of
RT cellulose synthase complexes in Arabidopsis.";
RL Nat. Commun. 7:11656-11656(2016).
RN [18]
RP S-ACYLATION.
RX PubMed=27387950; DOI=10.1126/science.aaf4009;
RA Kumar M., Wightman R., Atanassov I., Gupta A., Hurst C.H., Hemsley P.A.,
RA Turner S.;
RT "S-acylation of the cellulose synthase complex is essential for its plasma
RT membrane localization.";
RL Science 353:166-169(2016).
CC -!- FUNCTION: Catalytic subunit of cellulose synthase terminal complexes
CC ('rosettes'), required for beta-1,4-glucan microfibril crystallization,
CC a major mechanism of the cell wall formation. Involved in the primary
CC cell wall formation. The presence of each protein CESA1 and CESA6 is
CC critical for cell expansion. The hypocotyl elongation is based on a
CC CESA6-dependent cell elongation in dark and a CESA6-independent cell
CC elongation in light. The transition between these two mechanisms
CC requires photosynthesis and PHYB, but not CRY1. The CESA6-dependent
CC cell elongation seems to be independent of gibberellic acid, auxin and
CC ethylene. May be involved in sensitivity to isoxaben. Associates with
CC and moves along cortical microtubules for the process of cellulose
CC deposition. {ECO:0000269|PubMed:11148287, ECO:0000269|PubMed:11842152,
CC ECO:0000269|PubMed:16627697, ECO:0000269|PubMed:17878302,
CC ECO:0000269|PubMed:17878303, ECO:0000269|PubMed:7743935,
CC ECO:0000269|PubMed:8625819}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
CC -!- SUBUNIT: Interacts with CESA1 and CESA3. Interacts with STL1 and STL2,
CC but not with GOT1 (PubMed:27277162). Binds to CSI1 and CSI3
CC (PubMed:20616083, PubMed:24368796). {ECO:0000269|PubMed:17878302,
CC ECO:0000269|PubMed:17878303, ECO:0000269|PubMed:20616083,
CC ECO:0000269|PubMed:24368796, ECO:0000269|PubMed:27277162}.
CC -!- INTERACTION:
CC Q94JQ6; Q941L0: CESA3; NbExp=2; IntAct=EBI-15659159, EBI-4448240;
CC Q94JQ6; F4IIM1: CSI1; NbExp=2; IntAct=EBI-15659159, EBI-4430539;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20616083};
CC Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with CSI1
CC in a dynamic way. {ECO:0000269|PubMed:20616083}.
CC -!- TISSUE SPECIFICITY: Expressed in germinating seeds, seedlings, roots,
CC stems, leaves and flowers. Not present in mature flowers.
CC {ECO:0000269|PubMed:11148287, ECO:0000269|PubMed:12481071}.
CC -!- DEVELOPMENTAL STAGE: Not found in embryos. Higher levels in tissues
CC undergoing primary cell wall formation, and drop of expression when
CC secondary wall synthesis takes place. High levels in developing
CC seedlings and elongating stems, with a decrease at later growth stages.
CC {ECO:0000269|PubMed:11148287}.
CC -!- PTM: S-acylated. {ECO:0000269|PubMed:27387950}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC29067.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK53023.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB025637; BAB10307.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97945.1; -; Genomic_DNA.
DR EMBL; AK229477; BAF01335.1; -; mRNA.
DR EMBL; AF062485; AAC29067.1; ALT_INIT; mRNA.
DR EMBL; AF375439; AAK53023.1; ALT_FRAME; mRNA.
DR EMBL; AY143957; AAN28896.1; -; mRNA.
DR PIR; T52028; T52028.
DR RefSeq; NP_201279.1; NM_125870.3.
DR AlphaFoldDB; Q94JQ6; -.
DR SMR; Q94JQ6; -.
DR BioGRID; 21837; 11.
DR DIP; DIP-46438N; -.
DR IntAct; Q94JQ6; 3.
DR STRING; 3702.AT5G64740.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.3.1.4; the glycan glucosyl transferase (opgh) family.
DR iPTMnet; Q94JQ6; -.
DR SwissPalm; Q94JQ6; -.
DR PaxDb; Q94JQ6; -.
DR PRIDE; Q94JQ6; -.
DR ProteomicsDB; 223952; -.
DR EnsemblPlants; AT5G64740.1; AT5G64740.1; AT5G64740.
DR GeneID; 836595; -.
DR Gramene; AT5G64740.1; AT5G64740.1; AT5G64740.
DR KEGG; ath:AT5G64740; -.
DR Araport; AT5G64740; -.
DR TAIR; locus:2176090; AT5G64740.
DR eggNOG; ENOG502QQGG; Eukaryota.
DR HOGENOM; CLU_001418_0_2_1; -.
DR InParanoid; Q94JQ6; -.
DR OMA; FPMMDEG; -.
DR OrthoDB; 679241at2759; -.
DR PhylomeDB; Q94JQ6; -.
DR BioCyc; MetaCyc:MON-2363; -.
DR BRENDA; 2.4.1.12; 399.
DR UniPathway; UPA00695; -.
DR PRO; PR:Q94JQ6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94JQ6; baseline and differential.
DR Genevisible; Q94JQ6; AT.
DR GO; GO:0010330; C:cellulose synthase complex; NAS:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0016759; F:cellulose synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:TAIR.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR027934; CES_Znf_RING.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF03552; Cellulose_synt; 1.
DR Pfam; PF14569; zf-UDP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell wall biogenesis/degradation;
KW Cellulose biosynthesis; Coiled coil; Glycoprotein; Glycosyltransferase;
KW Lipoprotein; Membrane; Metal-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..1084
FT /note="Cellulose synthase A catalytic subunit 6 [UDP-
FT forming]"
FT /id="PRO_0000166372"
FT TOPO_DOM 1..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 890..894
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 916..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 931..951
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 952..980
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 981..1001
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1002..1012
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1013..1033
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1034..1042
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1043..1063
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1064..1084
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 39..85
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 450..476
FT /evidence="ECO:0000255"
FT COILED 675..703
FT /evidence="ECO:0000255"
FT ACT_SITE 396
FT /evidence="ECO:0000255"
FT ACT_SITE 785
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 562
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 564
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O48946"
FT CARBOHYD 958
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 1064
FT /note="R->W: In ixr2-1; confers resistance to the herbicide
FT isoxaben. Can complement prc1."
FT /evidence="ECO:0000269|PubMed:11842152"
FT CONFLICT 198
FT /note="P -> R (in Ref. 4; AAC29067)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="P -> L (in Ref. 4; AAC29067)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="R -> M (in Ref. 4; AAC29067)"
FT /evidence="ECO:0000305"
FT CONFLICT 706..710
FT /note="VTKGS -> GHKVL (in Ref. 4; AAC29067)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="E -> Q (in Ref. 4; AAC29067)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="F -> Y (in Ref. 4; AAC29067)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="M -> L (in Ref. 4; AAC29067)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="C -> R (in Ref. 4; AAC29067)"
FT /evidence="ECO:0000305"
FT CONFLICT 790
FT /note="F -> S (in Ref. 4; AAC29067)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="S -> H (in Ref. 4; AAC29067)"
FT /evidence="ECO:0000305"
FT CONFLICT 810
FT /note="K -> E (in Ref. 5; AAK53023/AAN28896)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1084 AA; 122502 MW; 1520439A5053608C CRC64;
MNTGGRLIAG SHNRNEFVLI NADENARIRS VQELSGQTCQ ICRDEIELTV DGEPFVACNE
CAFPVCRPCY EYERREGNQA CPQCKTRFKR LKGSPRVEGD EEEDDIDDLD NEFEYGNNGI
GFDQVSEGMS ISRRNSGFPQ SDLDSAPPGS QIPLLTYGDE DVEISSDRHA LIVPPSLGGH
GNRVHPVSLS DPTVAAHPRP MVPQKDLAVY GYGSVAWKDR MEEWKRKQNE KLQVVRHEGD
PDFEDGDDAD FPMMDEGRQP LSRKIPIKSS KINPYRMLIV LRLVILGLFF HYRILHPVKD
AYALWLISVI CEIWFAVSWV LDQFPKWYPI ERETYLDRLS LRYEKEGKPS GLSPVDVFVS
TVDPLKEPPL ITANTVLSIL AVDYPVDKVA CYVSDDGAAM LTFEALSETA EFARKWVPFC
KKYCIEPRAP EWYFCHKMDY LKNKVHPAFV RERRAMKRDY EEFKVKINAL VATAQKVPED
GWTMQDGTPW PGNSVRDHPG MIQVFLGSDG VRDVENNELP RLVYVSREKR PGFDHHKKAG
AMNSLIRVSG VLSNAPYLLN VDCDHYINNS KALREAMCFM MDPQSGKKIC YVQFPQRFDG
IDRHDRYSNR NVVFFDINMK GLDGLQGPIY VGTGCVFRRQ ALYGFDAPKK KKGPRKTCNC
WPKWCLLCFG SRKNRKAKTV AADKKKKNRE ASKQIHALEN IEEGRVTKGS NVEQSTEAMQ
MKLEKKFGQS PVFVASARME NGGMARNASP ACLLKEAIQV ISCGYEDKTE WGKEIGWIYG
SVTEDILTGF KMHSHGWRSV YCTPKLAAFK GSAPINLSDR LHQVLRWALG SVEIFLSRHC
PIWYGYGGGL KWLERLSYIN SVVYPWTSLP LIVYCSLPAI CLLTGKFIVP EISNYASILF
MALFSSIAIT GILEMQWGKV GIDDWWRNEQ FWVIGGVSAH LFALFQGLLK VLAGVDTNFT
VTSKAADDGE FSDLYLFKWT SLLIPPMTLL IINVIGVIVG VSDAISNGYD SWGPLFGRLF
FALWVIIHLY PFLKGLLGKQ DRMPTIIVVW SILLASILTL LWVRVNPFVA KGGPILEICG
LDCL
