ALDO3_ARATH
ID ALDO3_ARATH Reviewed; 1332 AA.
AC Q7G9P4; O64429; Q7GD73; Q9SIG7; Q9SLZ2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Abscisic-aldehyde oxidase;
DE EC=1.2.3.14 {ECO:0000269|PubMed:10972874, ECO:0000305|PubMed:11050171};
DE AltName: Full=Aldehyde oxidase 3;
DE Short=AO-3;
DE Short=AtAO-3;
DE Short=AtAO4;
DE AltName: Full=Indole-3-acetaldehyde oxidase;
DE Short=IAA oxidase;
DE EC=1.2.3.7 {ECO:0000305|PubMed:10972874};
GN Name=AAO3; Synonyms=AO4; OrderedLocusNames=At2g27150; ORFNames=F20F1.2;
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], SUBUNIT, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RX PubMed=15064376; DOI=10.1104/pp.103.036970;
RA Koiwai H., Nakaminami K., Seo M., Mitsuhashi W., Toyomasu T., Koshiba T.;
RT "Tissue-specific localization of an abscisic acid biosynthetic enzyme,
RT AAO3, in Arabidopsis.";
RL Plant Physiol. 134:1697-1707(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 [MRNA] OF 347-1332, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RX PubMed=9615466; DOI=10.1093/oxfordjournals.pcp.a029387;
RA Sekimoto H., Seo M., Kawakami N., Komano T., Desloire S., Liotenberg S.,
RA Marion-Poll A., Caboche M., Kamiya Y., Koshiba T.;
RT "Molecular cloning and characterization of aldehyde oxidases in Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 39:433-442(1998).
RN [5]
RP TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=9489015; DOI=10.1104/pp.116.2.687;
RA Seo M., Akaba S., Oritani T., Delarue M., Bellini C., Caboche M.,
RA Koshiba T.;
RT "Higher activity of an aldehyde oxidase in the auxin-overproducing
RT superroot1 mutant of Arabidopsis thaliana.";
RL Plant Physiol. 116:687-693(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION,
RP TISSUE SPECIFICITY, AND SUBUNIT.
RX PubMed=10972874; DOI=10.1046/j.1365-313x.2000.00812.x;
RA Seo M., Koiwai H., Akaba S., Komano T., Oritani T., Kamiya Y., Koshiba T.;
RT "Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana.";
RL Plant J. 23:481-488(2000).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTANT AAO3.
RX PubMed=11050171; DOI=10.1073/pnas.220426197;
RA Seo M., Peeters A.J.M., Koiwai H., Oritani T., Marion-Poll A.,
RA Zeevaart J.A.D., Koornneef M., Kamiya Y., Koshiba T.;
RT "The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final
RT step in abscisic acid biosynthesis in leaves.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12908-12913(2000).
RN [8]
RP INDUCTION.
RX PubMed=11779861; DOI=10.1074/jbc.m109275200;
RA Xiong L., Lee H., Ishitani M., Zhu J.-K.;
RT "Regulation of osmotic stress-responsive gene expression by the LOS6/ABA1
RT locus in Arabidopsis.";
RL J. Biol. Chem. 277:8588-8596(2002).
RN [9]
RP INDUCTION.
RX PubMed=12417697; DOI=10.1105/tpc.006494;
RA Cheng W.-H., Endo A., Zhou L., Penney J., Chen H.-C., Arroyo A., Leon P.,
RA Nambara E., Asami T., Seo M., Koshiba T., Sheen J.;
RT "A unique short-chain dehydrogenase/reductase in Arabidopsis glucose
RT signaling and abscisic acid biosynthesis and functions.";
RL Plant Cell 14:2723-2743(2002).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15574845; DOI=10.1093/pcp/pch198;
RA Seo M., Aoki H., Koiwai H., Kamiya Y., Nambara E., Koshiba T.;
RT "Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene family
RT revealed a major role of AAO3 in ABA biosynthesis in seeds.";
RL Plant Cell Physiol. 45:1694-1703(2004).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 821-LEU--LYS-826.
RX PubMed=15122034; DOI=10.1104/pp.103.036590;
RA Gonzalez-Guzman M., Abia D., Salinas J., Serrano R., Rodriguez P.L.;
RT "Two new alleles of the abscisic aldehyde oxidase 3 gene reveal its role in
RT abscisic acid biosynthesis in seeds.";
RL Plant Physiol. 135:325-333(2004).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY SALT STRESS AND ABA.
RC STRAIN=cv. Columbia;
RX PubMed=16930325; DOI=10.1111/j.1365-3040.2006.01576.x;
RA Barrero J.M., Rodriguez P.L., Quesada V., Piqueras P., Ponce M.R.,
RA Micol J.L.;
RT "Both abscisic acid (ABA)-dependent and ABA-independent pathways govern the
RT induction of NCED3, AAO3 and ABA1 in response to salt stress.";
RL Plant Cell Environ. 29:2000-2008(2006).
RN [13]
RP INTERACTION WITH PUB44.
RX PubMed=19309463; DOI=10.1111/j.1365-313x.2009.03846.x;
RA Raab S., Drechsel G., Zarepour M., Hartung W., Koshiba T., Bittner F.,
RA Hoth S.;
RT "Identification of a novel E3 ubiquitin ligase that is required for
RT suppression of premature senescence in Arabidopsis.";
RL Plant J. 59:39-51(2009).
CC -!- FUNCTION: In higher plants aldehyde oxidases (AO) appear to be
CC homo- and heterodimeric assemblies of AO subunits with probably
CC different physiological functions. AO-delta may be involved in the last
CC step of abscisic acid biosynthesis, at least in leaves and seeds. In
CC vitro, AO-delta oxidizes abscisic aldehyde to abscisic acid (ABA)
CC (PubMed:10972874). In vitro, AO-delta also uses 1-naphthaldehyde,
CC indole-3-aldehyde (IAld), benzaldehyde and cinnamaldehyde as substrate;
CC the AAO2-AAO3 dimer also uses abscisic aldehyde as substrate.
CC {ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:11050171,
CC ECO:0000269|PubMed:15122034, ECO:0000269|PubMed:15574845,
CC ECO:0000269|PubMed:16930325}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-cis-(+)-abscisic aldehyde + H2O + O2 = 2-cis-(+)-abscisate +
CC H(+) + H2O2; Xref=Rhea:RHEA:20529, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:31157, ChEBI:CHEBI:37569; EC=1.2.3.14;
CC Evidence={ECO:0000269|PubMed:10972874, ECO:0000305|PubMed:11050171};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20530;
CC Evidence={ECO:0000305|PubMed:10972874, ECO:0000305|PubMed:11050171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-naphthaldehyde + H2O + O2 = 1-naphthoate + H(+) + H2O2;
CC Xref=Rhea:RHEA:58968, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:36298,
CC ChEBI:CHEBI:52367; Evidence={ECO:0000305|PubMed:10972874,
CC ECO:0000305|PubMed:11050171};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58969;
CC Evidence={ECO:0000269|PubMed:10972874, ECO:0000305|PubMed:11050171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + indole-3-acetaldehyde + O2 = (indol-3-yl)acetate + H(+)
CC + H2O2; Xref=Rhea:RHEA:16277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18086,
CC ChEBI:CHEBI:30854; EC=1.2.3.7;
CC Evidence={ECO:0000305|PubMed:10972874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16278;
CC Evidence={ECO:0000305|PubMed:10972874};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.51 uM for abscisic aldehyde {ECO:0000269|PubMed:10972874};
CC KM=34 uM for indole-3-aldehyde {ECO:0000269|PubMed:10972874};
CC KM=44 uM for benzaldehyde {ECO:0000269|PubMed:10972874};
CC KM=1.8 uM for 1-naphthaldehyde {ECO:0000269|PubMed:10972874};
CC KM=700 uM for cinnamaldehyde {ECO:0000269|PubMed:10972874};
CC Note=All these kinetic values were obtained with AO-delta dimer.;
CC -!- SUBUNIT: Aldehyde oxidases (AO) are homodimers and heterodimers of AO
CC subunits. AO-delta is a AAO3 homodimer. AAO3 also forms a dimer with
CC AAO2. Interacts with PUB44, and this interaction probably results in
CC targeting of this protein to the proteasome.
CC {ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:15064376,
CC ECO:0000269|PubMed:19309463}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular tissues of all organs,
CC particularly in phloem companion cells and xylem parenchymatic cells.
CC Highly expressed in roots and rosettes, and to lower extent in
CC seedlings, stems and flowers. Expressed at very low levels in siliques
CC and dry seeds. Also detected in root dividing cells (tips and
CC primordia), in mesophyll cells and inside the guard cells.
CC {ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:11050171,
CC ECO:0000269|PubMed:15064376, ECO:0000269|PubMed:15122034,
CC ECO:0000269|PubMed:15574845, ECO:0000269|PubMed:9489015,
CC ECO:0000269|PubMed:9615466}.
CC -!- INDUCTION: Transcripts are induced by dehydration, in rosettes but not
CC in roots. Induction by cold, ABA, sodium chloride (NaCl) and
CC polyethylene glycol (PEG) is dependent of the zeaxanthin epoxidase ABA1
CC protein (ZEP). Induction by glucose requires the short chain alcohol
CC dehydrogenase ABA2 protein. Repressed by mannitol.
CC {ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:11779861,
CC ECO:0000269|PubMed:12417697, ECO:0000269|PubMed:15064376,
CC ECO:0000269|PubMed:16930325}.
CC -!- DISRUPTION PHENOTYPE: Impaired abscisic acid (ABA) biosynthesis.
CC {ECO:0000269|PubMed:16930325}.
CC -!- MISCELLANEOUS: In vitro, cannot discriminate between (+) and (-)
CC enantiomers of abscisic acid and leads respectively to (+) and (-) cis-
CC ABA.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AB016622; BAA82672.1; -; mRNA.
DR EMBL; AC007154; AAD22498.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07944.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07945.1; -; Genomic_DNA.
DR EMBL; AB010080; BAA28630.1; -; mRNA.
DR PIR; D84669; D84669.
DR PIR; T52176; T52176.
DR RefSeq; NP_001077966.1; NM_001084497.1.
DR RefSeq; NP_180283.1; NM_128273.3.
DR AlphaFoldDB; Q7G9P4; -.
DR SMR; Q7G9P4; -.
DR STRING; 3702.AT2G27150.2; -.
DR iPTMnet; Q7G9P4; -.
DR PaxDb; Q7G9P4; -.
DR PRIDE; Q7G9P4; -.
DR ProteomicsDB; 244792; -.
DR EnsemblPlants; AT2G27150.1; AT2G27150.1; AT2G27150.
DR EnsemblPlants; AT2G27150.2; AT2G27150.2; AT2G27150.
DR GeneID; 817257; -.
DR Gramene; AT2G27150.1; AT2G27150.1; AT2G27150.
DR Gramene; AT2G27150.2; AT2G27150.2; AT2G27150.
DR KEGG; ath:AT2G27150; -.
DR Araport; AT2G27150; -.
DR TAIR; locus:2045149; AT2G27150.
DR eggNOG; KOG0430; Eukaryota.
DR HOGENOM; CLU_001681_1_1_1; -.
DR InParanoid; Q7G9P4; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; Q7G9P4; -.
DR BioCyc; ARA:AT2G27150-MON; -.
DR BioCyc; MetaCyc:AT2G27150-MON; -.
DR BRENDA; 1.2.3.14; 399.
DR SABIO-RK; Q7G9P4; -.
DR PRO; PR:Q7G9P4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7G9P4; baseline and differential.
DR Genevisible; Q7G9P4; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010293; F:abscisic aldehyde oxidase activity; IDA:TAIR.
DR GO; GO:0004031; F:aldehyde oxidase activity; IDA:TAIR.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050302; F:indole-3-acetaldehyde oxidase activity; IDA:TAIR.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0009688; P:abscisic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR PIRSF; PIRSF000127; Xanthine_DH; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Abscisic acid biosynthesis; Auxin biosynthesis; Cytoplasm; FAD;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..1332
FT /note="Abscisic-aldehyde oxidase"
FT /id="PRO_0000166111"
FT DOMAIN 1..88
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 219..400
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT MUTAGEN 821..826
FT /note="LQRPVK->WDLDQ: In aao3-3; wilty phenotype in rosette
FT leaves, reduced ABA levels, reduced dormancy, abnormal
FT water loss and abnormal response to water deficit."
FT /evidence="ECO:0000269|PubMed:15122034"
SQ SEQUENCE 1332 AA; 146701 MW; 084ED4BEE64B121B CRC64;
MDLEFAVNGE RFKIDSVDPS TTLLEFLRLN TPFKSVKLGC GEGGCGACLV VLSKYDPELD
QVKECCINSC LTLLCSVNGC SITTSEGLGN TKKGFHPIHK RFAGFHASQC GFCTPGMCIS
LYSSLANAEN NSSKDFTVSE AEKSVSGNLC RCTGYRPIVD ACKSFASDVD IEDLGLNSFW
KKGESKEVMF KNLPPYNPKD HLVTFPEFLK KKEKVDNGSD HLKYRWTTPF SVAELHNIME
AANSGDSLKL VVGNTGTGYY KDEERFDRYI DISNIPEMSM IKKDEKGIEI GAAVTISNAI
DALEKESKSS YVFKKMATHM EKIGNRSIRN SGSIGGNLVM AQSRKFPSDV TTLLLAVDAS
VYMLNGRKTE KVTLQEFLEL SPVLDSKRVL LKVEIPSWTA PSGDDTEFLF ESYRAAPRSI
GNALPYLNAA FLALVSRQEA SRKGVTVEKC FLAFGSYGGD HSIRAIEVET FLTGKLLSYS
VLYEAVGLLK GIIVPGKDTL HSEYRKSLAV GYLFEFFYPL IESGHRICSL DSGNKHNNSH
VDTVKSLPFL SSSQQVLESN EFKPIGEAVI KVGAALQASG EAVFVDDIPT LPDCLHGAFI
YSTEPLAKIK SLSFRENVTP TGVFAVLTFK DIPQQGQNIG SKTLFGPGPL FADELTRCAG
QRIALVVADT QKHADMAAKL AVVEYDTKNL EQPILTVEDA VKRSSFFEVH PMFYPEPVGD
VIKGMEEAER KIISSELRLG SQYFFYMEPQ TALALPDEDN CVKVFSSSQA PEYVHSVIAT
CLGIQEHNVR VITRRVGGGF GGKAVKSMPV ATACALGAYK LQRPVKMFLN RKTDMIMAGG
RHPMKINYNV GFRSDGKLTA LELTMLIDAG LEPDVSPIMP RNIMGPLRKY DWGALSFDVK
VCKTNCLSRT AMRAPGEVQG SYIAESIIEN VASSLQMDVD AVRKINLHTY DSLRKFYNHI
AGDPDEYTLP LLWEKLEISS KFKERSEMVK EFNLCNVWRK RGISRVPIVH QVMQRPTPGK
VSILSDGSVV VEVGGIEIGQ GLWTKVQQMV AYGLGMVKCE GNEKLLDRIR VVQSDTLGMI
QGGFTAGSTT SESSCEAVRL CCVILVERLK PIMDQMMMEK SGSVTWNILI QQAYGQYINL
SASTLYKPEY SSMEYLNYGV GVSEVEVDLV TGKTEILRSD IIYDCGKSLN PAVDLGQTEG
AFVQGIGFFM MEEYTTDEKG LVVQQGTWDY KIPTVDTIPK HFNVEIVNTG HHKNRVLSSK
ASGEPPLLLA ASVHCATRSA IREARKHSLS SNFIDGSDSE FELPVPATMP VVKSLCGLYS
VEKYLQGKIK GQ
