OMT1_ORYSJ
ID OMT1_ORYSJ Reviewed; 368 AA.
AC Q6ZD89; A0A0P0XBV5; A3BPT2; Q19BJ6; Q75W57;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Flavone 3'-O-methyltransferase 1 {ECO:0000305};
DE Short=OsOMT1 {ECO:0000305};
DE EC=2.1.1.42 {ECO:0000269|PubMed:16412485};
DE AltName: Full=Acetylserotonin O-methyltransferase COMT {ECO:0000305};
DE EC=2.1.1.4 {ECO:0000269|PubMed:26276868};
DE AltName: Full=Caffeate O-methyltransferase 1 {ECO:0000305};
DE Short=OsCOMT1 {ECO:0000303|Ref.16};
DE EC=2.1.1.68 {ECO:0000269|Ref.16};
DE AltName: Full=OsCOMT {ECO:0000303|PubMed:26276868};
DE AltName: Full=Quercetin 3'-O-methyltransferase 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=COMT {ECO:0000305}; Synonyms=ROMT-9 {ECO:0000303|PubMed:16412485};
GN OrderedLocusNames=Os08g0157500, LOC_Os08g06100;
GN ORFNames=OsJ_26105, P0438H08.29;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=16412485; DOI=10.1016/j.phytochem.2005.11.022;
RA Kim B.-G., Lee Y., Hur H.-G., Lim Y., Ahn J.-H.;
RT "Flavonoid 3'-O-methyltransferase from rice: cDNA cloning, characterization
RT and functional expression.";
RL Phytochemistry 67:387-394(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhou J.-M., Ibrahim R.K.;
RT "Characterization of two flavone specific O-methyltransferase genes in
RT wheat and rice.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 3-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=cv. Nipponbare;
RX PubMed=16758443; DOI=10.1002/pmic.200600043;
RA Nozu Y., Tsugita A., Kamijo K.;
RT "Proteomic analysis of rice leaf, stem and root tissues during growth
RT course.";
RL Proteomics 6:3665-3670(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 101-368.
RC STRAIN=cv. Fujiminori;
RA Mase K., Nishikubo N., Satou K., Nakano Y., Kajita S., Katayama Y.;
RT "The cDNA encoding caffeic acid o-methyl transferase expressed in rice
RT stem.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP PROTEIN SEQUENCE OF 185-224.
RX PubMed=10814825; DOI=10.1016/s0168-9452(00)00223-5;
RA Rakwal R., Agrawal G.K., Yonekura M., Kodama O.;
RT "Naringenin 7-O-methyltransferase involved in the biosynthesis of the
RT flavanone phytoalexin sakuranetin from rice (Oryza sativa L.).";
RL Plant Sci. 155:213-221(2000).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION BY PROBENAZOLE.
RX PubMed=17950386; DOI=10.1016/j.phytochem.2007.09.005;
RA Lin Y.Z., Chen H.Y., Kao R., Chang S.P., Chang S.J., Lai E.M.;
RT "Proteomic analysis of rice defense response induced by probenazole.";
RL Phytochemistry 69:715-728(2008).
RN [12]
RP FUNCTION.
RX PubMed=21210840; DOI=10.1111/j.1600-079x.2010.00841.x;
RA Kang K., Kong K., Park S., Natsagdorj U., Kim Y.S., Back K.;
RT "Molecular cloning of a plant N-acetylserotonin methyltransferase and its
RT expression characteristics in rice.";
RL J. Pineal Res. 50:304-309(2011).
RN [13]
RP FUNCTION.
RX PubMed=21912859; DOI=10.1007/s00299-011-1142-7;
RA Hirano K., Aya K., Kondo M., Okuno A., Morinaka Y., Matsuoka M.;
RT "OsCAD2 is the major CAD gene responsible for monolignol biosynthesis in
RT rice culm.";
RL Plant Cell Rep. 31:91-101(2012).
RN [14]
RP SHOWS THAT IT HAS NO NARINGENIN 7-O-METHYLTRANSFERASE ACTIVITY.
RX PubMed=22493492; DOI=10.1074/jbc.m112.351270;
RA Shimizu T., Lin F., Hasegawa M., Okada K., Nojiri H., Yamane H.;
RT "Purification and identification of naringenin 7-o-methyltransferase, a key
RT enzyme in biosynthesis of flavonoid phytoalexin sakuranetin in rice.";
RL J. Biol. Chem. 287:19315-19325(2012).
RN [15]
RP INDUCTION BY UV-C.
RX PubMed=24035516; DOI=10.1016/j.phytochem.2013.08.012;
RA Park H.L., Lee S.W., Jung K.H., Hahn T.R., Cho M.H.;
RT "Transcriptomic analysis of UV-treated rice leaves reveals UV-induced
RT phytoalexin biosynthetic pathways and their regulatory networks in rice.";
RL Phytochemistry 96:57-71(2013).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.5511/plantbiotechnology.13.0219a;
RA Koshiba T., Hirose N., Mukai M., Yamamura M., Hattori T., Suzuki S.,
RA Sakamoto M., Umezawa T.;
RT "Characterization of 5-hydroxyconiferaldehyde O-methyltransferase in Oryza
RT sativa.";
RL Plant Biotechnol. 30:157-167(2013).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=26276868; DOI=10.1093/jxb/erv396;
RA Byeon Y., Choi G.H., Lee H.Y., Back K.;
RT "Melatonin biosynthesis requires N-acetylserotonin methyltransferase
RT activity of caffeic acid O-methyltransferase in rice.";
RL J. Exp. Bot. 66:6917-6925(2015).
CC -!- FUNCTION: Methylates OH residues of flavonoid compounds. Can methylate
CC eriodictyol, luteolin, quercetin and taxifolin (PubMed:16412485).
CC Methylates caffeate to produce ferrulate (PubMed:21210840, Ref.16).
CC Catalyzes the methylation of monolignols, the lignin precursors.
CC Functions cooperatively with CAD2 in the culm internodes for the
CC biosynthesis of monolignols. May be involved in lignin biosynthesis in
CC leaves and roots (PubMed:21912859). Involved in syringyl lignin
CC biosynthesis. Can function as 5-hydroxyconiferaldehyde O-
CC methyltransferase in the biosynthetic pathway to syringyl lignin
CC (Ref.16). Involved in melatonin biosynthesis. Can function as
CC acetylserotonin O-methyltransferase. Catalyzes the transfer of a methyl
CC group onto N-acetylserotonin, producing melatonin (N-acetyl-5-
CC methoxytryptamine) (PubMed:26276868). {ECO:0000269|PubMed:16412485,
CC ECO:0000269|PubMed:21210840, ECO:0000269|PubMed:21912859,
CC ECO:0000269|PubMed:26276868, ECO:0000269|Ref.16}.
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:16412485};
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:26276868};
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:21210840};
CC -!- ACTIVITY REGULATION: Acetylserotonin O-methyltransferase activity is
CC inhibited by quercetin and caffeate. {ECO:0000269|PubMed:26276868}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=61.8 uM for quercetin {ECO:0000269|PubMed:16412485};
CC KM=61.9 uM for luteolin {ECO:0000269|PubMed:16412485};
CC KM=62 uM for eriodictyol {ECO:0000269|PubMed:16412485};
CC KM=201.8 uM for caffeate (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|Ref.16};
CC KM=22.2 uM for 5-hydroxyferulate (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|Ref.16};
CC KM=65.8 uM for caffealdehyde (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|Ref.16};
CC KM=26.4 uM for 5-hydroxyconiferaldehyde (at pH 7.5 and 30 degrees
CC Celsius) {ECO:0000269|Ref.16};
CC KM=50 uM for caffeyl alcohol (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|Ref.16};
CC KM=132.3 uM for 5-hydroxyconiferyl alcohol (at pH 7.5 and 30 degrees
CC Celsius) {ECO:0000269|Ref.16};
CC KM=243 uM for N-acetylserotonin (at pH 7.8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:26276868};
CC Vmax=1250 pmol/sec/mg enzyme with quercetin as substrate
CC {ECO:0000269|PubMed:16412485};
CC Vmax=833 pmol/sec/mg enzyme with luteolin as substrate
CC {ECO:0000269|PubMed:16412485};
CC Vmax=625 pmol/sec/mg enzyme with eriodictyol as substrate
CC {ECO:0000269|PubMed:16412485};
CC Vmax=2.4 nmol/min/mg enzyme with N-acetylserotonin as substrate (at
CC pH 7.8 and 37 degrees Celsius) {ECO:0000269|PubMed:16412485};
CC Note=Measured at pH 7.5 and 37 degrees Celsius for all experiments.
CC {ECO:0000269|PubMed:16412485};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius for acetylserotonin O-
CC methyltransferase activity. {ECO:0000269|PubMed:26276868};
CC -!- PATHWAY: Flavonoid metabolism; quercetin degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9FK25}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26276868}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and stems, and at lower levels
CC in leaves. {ECO:0000269|PubMed:16412485}.
CC -!- INDUCTION: By probenazole (at protein level) (PubMed:17950386). Induced
CC by UV-C (PubMed:24035516). {ECO:0000269|PubMed:17950386,
CC ECO:0000269|PubMed:24035516}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to constitute the naringenin 7-O-
CC methyltransferase (NOMT), a methyltransferase involved in the
CC biosynthesis of the sakuranetin, an inducible defense mechanism of
CC O.sativa against pathogen attack (PubMed:10814825). However, it was
CC later shown that it is not the case (PubMed:22493492).
CC {ECO:0000305|PubMed:10814825, ECO:0000305|PubMed:22493492}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAZ41571.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ288259; ABB90678.1; -; mRNA.
DR EMBL; DQ530257; ABF72191.1; -; mRNA.
DR EMBL; AP004460; BAC99512.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF22945.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT03903.1; -; Genomic_DNA.
DR EMBL; CM000145; EAZ41571.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK064768; BAG89194.1; -; mRNA.
DR EMBL; AB122056; BAD14923.1; -; mRNA.
DR RefSeq; XP_015650053.1; XM_015794567.1.
DR AlphaFoldDB; Q6ZD89; -.
DR SMR; Q6ZD89; -.
DR BioGRID; 813739; 1.
DR STRING; 4530.OS08T0157500-01; -.
DR PaxDb; Q6ZD89; -.
DR PRIDE; Q6ZD89; -.
DR EnsemblPlants; Os08t0157500-01; Os08t0157500-01; Os08g0157500.
DR GeneID; 4344702; -.
DR Gramene; Os08t0157500-01; Os08t0157500-01; Os08g0157500.
DR KEGG; osa:4344702; -.
DR eggNOG; KOG3178; Eukaryota.
DR InParanoid; Q6ZD89; -.
DR OMA; CTEPWTW; -.
DR OrthoDB; 817726at2759; -.
DR BioCyc; MetaCyc:MON-20526; -.
DR BRENDA; 2.1.1.4; 4460.
DR BRENDA; 2.1.1.68; 4460.
DR BRENDA; 2.1.1.76; 4460.
DR PlantReactome; R-OSA-1119316; Phenylpropanoid biosynthesis.
DR PlantReactome; R-OSA-9609573; Tricin biosynthesis.
DR UniPathway; UPA00724; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR ExpressionAtlas; Q6ZD89; baseline and differential.
DR Genevisible; Q6ZD89; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0017096; F:acetylserotonin O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047763; F:caffeate O-methyltransferase activity; IGC:CACAO.
DR GO; GO:0030744; F:luteolin O-methyltransferase activity; IDA:UniProtKB.
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: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:UniProtKB.
DR GO; GO:0009809; P:lignin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030187; P:melatonin biosynthetic process; IMP:UniProtKB.
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 Cytoplasm; Direct protein sequencing; Melatonin biosynthesis;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT PROPEP 1..2
FT /evidence="ECO:0000269|PubMed:16758443"
FT /id="PRO_0000248969"
FT CHAIN 3..368
FT /note="Flavone 3'-O-methyltransferase 1"
FT /id="PRO_0000233699"
FT ACT_SITE 274
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT ACT_SITE 302
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT ACT_SITE 334
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 235
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT CONFLICT 54
FT /note="G -> R (in Ref. 6; EAZ41571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 39749 MW; 2491B4FA7447558E CRC64;
MGSTAADMAA AADEEACMYA LQLASSSILP MTLKNAIELG LLETLQSAAV AGGGGKAALL
TPAEVADKLP SKANPAAADM VDRMLRLLAS YNVVRCEMEE GADGKLSRRY AAAPVCKWLT
PNEDGVSMAA LALMNQDKVL MESWYYLKDA VLDGGIPFNK AYGMTAFEYH GTDARFNRVF
NEGMKNHSVI ITKKLLDLYT GFDAASTVVD VGGGVGATVA AVVSRHPHIR GINYDLPHVI
SEAPPFPGVE HVGGDMFASV PRGGDAILMK WILHDWSDEH CARLLKNCYD ALPEHGKVVV
VECVLPESSD ATAREQGVFH VDMIMLAHNP GGKERYEREF RELARAAGFT GFKATYIYAN
AWAIEFTK
