OMT1_ARATH
ID OMT1_ARATH Reviewed; 363 AA.
AC Q9FK25; O49964; Q42170;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Flavone 3'-O-methyltransferase 1;
DE Short=AtOMT1;
DE EC=2.1.1.42;
DE AltName: Full=Acetylserotonin O-methyltransferase OMT1 {ECO:0000305};
DE EC=2.1.1.4 {ECO:0000269|PubMed:25039887};
DE AltName: Full=Caffeate O-methyltransferase 1;
DE EC=2.1.1.68;
DE AltName: Full=Quercetin 3'-O-methyltransferase 1;
GN Name=OMT1; Synonyms=COMT1; OrderedLocusNames=At5g54160; ORFNames=K18G13.3;
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. C24; TISSUE=Leaf;
RX PubMed=9349713; DOI=10.1016/s0167-4781(97)00096-1;
RA Zhang H., Wang J., Goodman H.M.;
RT "An Arabidopsis gene encoding a putative 14-3-3-interacting protein,
RT caffeic acid/5-hydroxyferulic acid O-methyltransferase.";
RL Biochim. Biophys. Acta 1353:199-202(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 285-363.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=10700397; DOI=10.1006/abbi.1999.1681;
RA Muzac I., Wang J., Anzellotti D., Zhang H., Ibrahim R.K.;
RT "Functional expression of an Arabidopsis cDNA clone encoding a flavonol 3'-
RT O-methyltransferase and characterization of the gene product.";
RL Arch. Biochem. Biophys. 375:385-388(2000).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=12777055; DOI=10.1023/a:1023022825098;
RA Goujon T., Sibout R., Pollet B., Maba B., Nussaume L., Bechtold N., Lu F.,
RA Ralph J., Mila I., Barriere Y., Lapierre C., Jouanin L.;
RT "A new Arabidopsis thaliana mutant deficient in the expression of O-
RT methyltransferase impacts lignins and sinapoyl esters.";
RL Plant Mol. Biol. 51:973-989(2003).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Wassilewskija;
RX PubMed=20652169; DOI=10.1039/c004817h;
RA Moinuddin S.G.A., Jourdes M., Laskar D.D., Ki C., Cardenas C.L., Kim K.-W.,
RA Zhang D., Davin L.B., Lewis N.G.;
RT "Insights into lignin primary structure and deconstruction from Arabidopsis
RT thaliana COMT (caffeic acid O-methyl transferase) mutant Atomt1.";
RL Org. Biomol. Chem. 8:3928-3946(2010).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22258746; DOI=10.1007/s00425-011-1586-6;
RA Fellenberg C., van Ohlen M., Handrick V., Vogt T.;
RT "The role of CCoAOMT1 and COMT1 in Arabidopsis anthers.";
RL Planta 236:51-61(2012).
RN [11]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=25039887; DOI=10.1111/jpi.12160;
RA Byeon Y., Lee H.Y., Lee K., Back K.;
RT "Caffeic acid O-methyltransferase is involved in the synthesis of melatonin
RT by methylating N-acetylserotonin in Arabidopsis.";
RL J. Pineal Res. 57:219-227(2014).
RN [13]
RP 3D-STRUCTURE MODELING.
RX PubMed=15331056; DOI=10.1016/j.jmgm.2004.02.001;
RA Yang H., Ahn J.-H., Ibrahim R.K., Lee S., Lim Y.;
RT "The three-dimensional structure of Arabidopsis thaliana O-
RT methyltransferase predicted by homology-based modelling.";
RL J. Mol. Graph. Model. 23:77-87(2004).
CC -!- FUNCTION: Methylates OH residues of flavonoid compounds. Converts
CC quercetin into isorhamnetin. Dihydroquercetin is not a substrate.
CC Catalyzes the methylation of monolignols, the lignin precursors. Does
CC not contribute to the phenylpropanoid pattern of the pollen tryphine,
CC but is probably confined to isorhamnetin glycoside biosynthesis
CC (PubMed:10700397, PubMed:12777055, PubMed:20652169, PubMed:22258746).
CC Involved in melatonin biosynthesis. Can function as acetylserotonin O-
CC methyltransferase. Catalyzes the transfer of a methyl group onto N-
CC acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine)
CC (PubMed:25039887). {ECO:0000269|PubMed:10700397,
CC ECO:0000269|PubMed:12777055, ECO:0000269|PubMed:20652169,
CC ECO:0000269|PubMed:22258746, ECO:0000269|PubMed:25039887}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-hydroxyflavone + S-adenosyl-L-methionine = a 3'-
CC methoxyflavone + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55332, ChEBI:CHEBI:15378, ChEBI:CHEBI:27741,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138730;
CC EC=2.1.1.42; Evidence={ECO:0000269|PubMed:12777055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetylserotonin + S-adenosyl-L-methionine = H(+) + melatonin
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15573, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16796, ChEBI:CHEBI:17697, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; EC=2.1.1.4;
CC Evidence={ECO:0000269|PubMed:25039887};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-caffeate + S-adenosyl-L-methionine = (E)-ferulate + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:20225, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29749, ChEBI:CHEBI:57770, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; EC=2.1.1.68;
CC Evidence={ECO:0000269|PubMed:12777055};
CC -!- ACTIVITY REGULATION: Does not require magnesium. Completely inhibited
CC by 5 mM of either NiSO4 or p-chloromercuribenzoate (pCMB).
CC Acetylserotonin O-methyltransferase activity is inhibited by caffeate
CC (PubMed:25039887). {ECO:0000269|PubMed:10700397,
CC ECO:0000269|PubMed:25039887}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.76 uM for quercetin (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:10700397};
CC KM=3.38 uM for myricetin (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:10700397};
CC KM=24.2 uM for caffeic acid (at pH 7.5)
CC {ECO:0000269|PubMed:20652169};
CC KM=233 uM for N-acetylserotonin (at pH 7.8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:25039887};
CC KM=32 uM for 5-OH ferulic acid (at pH 7.5)
CC {ECO:0000269|PubMed:20652169};
CC KM=19.7 uM for caffeyl aldehyde (at pH 7.5)
CC {ECO:0000269|PubMed:20652169};
CC KM=17.9 uM for 5-OH coniferyl aldehyde (at pH 7.5)
CC {ECO:0000269|PubMed:20652169};
CC KM=51.5 uM for caffeyl alcohol (at pH 7.5)
CC {ECO:0000269|PubMed:20652169};
CC KM=31.6 uM for 5-OH coniferyl alcohol (at pH 7.5)
CC {ECO:0000269|PubMed:20652169};
CC KM=23.7 uM for quercetin (at pH 7.5) {ECO:0000269|PubMed:20652169};
CC Vmax=384.6 pmol/sec/mg enzyme with quercetin as substrate
CC {ECO:0000269|PubMed:10700397};
CC Vmax=227.3 pmol/sec/mg enzyme with myricetin as substrate
CC {ECO:0000269|PubMed:10700397};
CC Vmax=3.8 pmol/sec/ug enzyme with quercetin as substrate (at pH 7.5)
CC {ECO:0000269|PubMed:20652169};
CC Vmax=51.9 pmol/sec/ug enzyme with 5-OH coniferyl alcohol as substrate
CC (at pH 7.5) {ECO:0000269|PubMed:20652169};
CC Vmax=35.3 pmol/sec/ug enzyme with caffeyl alcohol as substrate (at pH
CC 7.5) {ECO:0000269|PubMed:20652169};
CC Vmax=66.2 pmol/sec/ug enzyme with 5-OH coniferyl aldehyde as
CC substrate (at pH 7.5) {ECO:0000269|PubMed:20652169};
CC Vmax=35.9 pmol/sec/ug enzyme with caffeyl aldehyde as substrate (at
CC pH 7.5) {ECO:0000269|PubMed:20652169};
CC Vmax=30.1 pmol/sec/ug enzyme with 5-OH ferulic acid as substrate (at
CC pH 7.5) {ECO:0000269|PubMed:20652169};
CC Vmax=14.6 pmol/sec/ug enzyme with caffeic acid as substrate (at pH
CC 7.5) {ECO:0000269|PubMed:20652169};
CC Vmax=1800 pmol/min/mg enzyme with N-acetylserotonin as substrate (at
CC pH 7.8 and 37 degrees Celsius) {ECO:0000269|PubMed:25039887};
CC pH dependence:
CC Optimum pH is 7.5 (PubMed:10700397, PubMed:20652169). Optimum pH is
CC 7.8 for acetylserotonin O-methyltransferase activity
CC (PubMed:25039887). {ECO:0000269|PubMed:10700397,
CC ECO:0000269|PubMed:20652169, ECO:0000269|PubMed:25039887};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius for acetylserotonin O-
CC methyltransferase activity. {ECO:0000269|PubMed:25039887};
CC -!- PATHWAY: Flavonoid metabolism; quercetin degradation.
CC -!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis;
CC melatonin from serotonin: step 1/2. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10700397}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, stems, flowers and
CC siliques, mostly in vascular tissues. Mostly expressed in the apical
CC part of the stems and in roots. Expressed in the endothecium and the
CC epidermal anther, but not in the tapetum. Also detected in all
CC epidermal tissues of flower organs, including petals, sepals and the
CC tip of the stigma. {ECO:0000269|PubMed:12777055,
CC ECO:0000269|PubMed:22258746}.
CC -!- DEVELOPMENTAL STAGE: Observed in young seedling and progressively
CC restricted to vascular tissues. Present in whole blade of young leaves
CC but confined to the vascular tissues of mature leaves. In stems, mostly
CC present in xylem, mature phloem and differentiating fibers. In
CC siliques, only present in the lignified extremities. Expressed during
CC early and late stages of flower development.
CC {ECO:0000269|PubMed:12777055, ECO:0000269|PubMed:22258746}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of syringyl (S) units in lignins
CC that contain more 5-hydroxyguaiacyl units (5-OH-G), the precursors of
CC S-units. Substitution of sinapyl (S) alcohol-derived substructures by
CC 5-hydroxyconiferyl alcohol (5OHG)-derived moieties in fiber cell walls.
CC No effect on hydroxycinnamic acid amides in pollen.
CC {ECO:0000269|PubMed:12777055, ECO:0000269|PubMed:20652169,
CC ECO:0000269|PubMed:22258746}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; U70424; AAB96879.1; -; mRNA.
DR EMBL; AB013387; BAB11578.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96460.1; -; Genomic_DNA.
DR EMBL; AY062837; AAL32915.1; -; mRNA.
DR EMBL; AY081565; AAM10127.1; -; mRNA.
DR EMBL; AY087297; AAM64849.1; -; mRNA.
DR EMBL; Z27062; CAA81580.1; -; mRNA.
DR RefSeq; NP_200227.1; NM_124796.4.
DR AlphaFoldDB; Q9FK25; -.
DR SMR; Q9FK25; -.
DR BioGRID; 20748; 6.
DR IntAct; Q9FK25; 4.
DR STRING; 3702.AT5G54160.1; -.
DR iPTMnet; Q9FK25; -.
DR PaxDb; Q9FK25; -.
DR PRIDE; Q9FK25; -.
DR ProteomicsDB; 248754; -.
DR EnsemblPlants; AT5G54160.1; AT5G54160.1; AT5G54160.
DR GeneID; 835504; -.
DR Gramene; AT5G54160.1; AT5G54160.1; AT5G54160.
DR KEGG; ath:AT5G54160; -.
DR Araport; AT5G54160; -.
DR TAIR; locus:2153423; AT5G54160.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_12_1_1; -.
DR OMA; CTEPWTW; -.
DR OrthoDB; 817726at2759; -.
DR PhylomeDB; Q9FK25; -.
DR BRENDA; 2.1.1.42; 399.
DR BRENDA; 2.1.1.68; 399.
DR BRENDA; 2.1.1.76; 399.
DR UniPathway; UPA00724; -.
DR UniPathway; UPA00837; UER00815.
DR PRO; PR:Q9FK25; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK25; baseline and differential.
DR Genevisible; Q9FK25; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0017096; F:acetylserotonin O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047763; F:caffeate O-methyltransferase activity; IMP:TAIR.
DR GO; GO:0030744; F:luteolin O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0033799; F:myricetin 3'-O-methyltransferase activity; IDA:TAIR.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0102822; F:quercetin 3'-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030755; F:quercetin 3-O-methyltransferase activity; IDA:TAIR.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0051555; P:flavonol biosynthetic process; IDA:TAIR.
DR GO; GO:0009809; P:lignin biosynthetic process; IMP:TAIR.
DR GO; GO:0030187; P:melatonin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF08100; Dimerisation; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Melatonin biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..363
FT /note="Flavone 3'-O-methyltransferase 1"
FT /id="PRO_0000063217"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT ACT_SITE 295
FT /evidence="ECO:0000305|PubMed:25039887"
FT ACT_SITE 327
FT /evidence="ECO:0000305|PubMed:25039887"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 206
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 249
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 250
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT CONFLICT 229
FT /note="D -> N (in Ref. 1; AAB96879)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="E -> V (in Ref. 6; CAA81580)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="T -> S (in Ref. 6; CAA81580)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="V -> C (in Ref. 6; CAA81580)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 39618 MW; B4380028D89C43DC CRC64;
MGSTAETQLT PVQVTDDEAA LFAMQLASAS VLPMALKSAL ELDLLEIMAK NGSPMSPTEI
ASKLPTKNPE APVMLDRILR LLTSYSVLTC SNRKLSGDGV ERIYGLGPVC KYLTKNEDGV
SIAALCLMNQ DKVLMESWYH LKDAILDGGI PFNKAYGMSA FEYHGTDPRF NKVFNNGMSN
HSTITMKKIL ETYKGFEGLT SLVDVGGGIG ATLKMIVSKY PNLKGINFDL PHVIEDAPSH
PGIEHVGGDM FVSVPKGDAI FMKWICHDWS DEHCVKFLKN CYESLPEDGK VILAECILPE
TPDSSLSTKQ VVHVDCIMLA HNPGGKERTE KEFEALAKAS GFKGIKVVCD AFGVNLIELL
KKL
