XDH1_ARATH
ID XDH1_ARATH Reviewed; 1361 AA.
AC Q8GUQ8; Q9SW46;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Xanthine dehydrogenase 1;
DE Short=AtXDH1;
DE EC=1.17.1.4 {ECO:0000269|PubMed:14726515};
GN Name=XDH1; OrderedLocusNames=At4g34890; ORFNames=T11I11.130;
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], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=14726515; DOI=10.1074/jbc.m312929200;
RA Hesberg C., Haensch R., Mendel R.R., Bittner F.;
RT "Tandem orientation of duplicated xanthine dehydrogenase genes from
RT Arabidopsis thaliana: differential gene expression and enzyme activities.";
RL J. Biol. Chem. 279:13547-13554(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 FUNCTION, AND INDUCTION.
RX PubMed=15941399; DOI=10.1111/j.1365-313x.2005.02422.x;
RA Yesbergenova Z., Yang G., Oron E., Soffer D., Fluhr R., Sagi M.;
RT "The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have
RT distinct reactive oxygen species signatures and are induced by drought and
RT abscisic acid.";
RL Plant J. 42:862-876(2005).
RN [5]
RP FUNCTION.
RX PubMed=17872919; DOI=10.1093/pcp/pcm119;
RA Nakagawa A., Sakamoto S., Takahashi M., Morikawa H., Sakamoto A.;
RT "The RNAi-mediated silencing of xanthine dehydrogenase impairs growth and
RT fertility and accelerates leaf senescence in transgenic Arabidopsis
RT plants.";
RL Plant Cell Physiol. 48:1484-1495(2007).
RN [6]
RP FUNCTION.
RX PubMed=18266920; DOI=10.1111/j.1365-313x.2008.03440.x;
RA Brychkova G., Alikulov Z., Fluhr R., Sagi M.;
RT "A critical role for ureides in dark and senescence-induced purine
RT remobilization is unmasked in the Atxdh1 Arabidopsis mutant.";
RL Plant J. 54:496-509(2008).
RN [7]
RP FUNCTION.
RX PubMed=20153325; DOI=10.1016/j.febslet.2010.02.023;
RA Watanabe S., Nakagawa A., Izumi S., Shimada H., Sakamoto A.;
RT "RNA interference-mediated suppression of xanthine dehydrogenase reveals
RT the role of purine metabolism in drought tolerance in Arabidopsis.";
RL FEBS Lett. 584:1181-1186(2010).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF TRP-364; TYR-421; GLU-831; ARG-909 AND
RP GLU-1297.
RX PubMed=19915948; DOI=10.1007/s11103-009-9570-2;
RA Zarepour M., Kaspari K., Stagge S., Rethmeier R., Mendel R.R., Bittner F.;
RT "Xanthine dehydrogenase AtXDH1 from Arabidopsis thaliana is a potent
RT producer of superoxide anions via its NADH oxidase activity.";
RL Plant Mol. Biol. 72:301-310(2010).
CC -!- FUNCTION: Key enzyme involved in purine catabolism. Catalyzes the
CC oxidation of hypoxanthine to xanthine and the oxidation of xanthine to
CC urate. Regulates the level of ureides and plays an important role
CC during plant growth and development, senescence and response to
CC stresses. Possesses NADH oxidase activity and may contribute to the
CC generation of superoxide anions in planta.
CC {ECO:0000269|PubMed:14726515, ECO:0000269|PubMed:15941399,
CC ECO:0000269|PubMed:17872919, ECO:0000269|PubMed:18266920,
CC ECO:0000269|PubMed:19915948, ECO:0000269|PubMed:20153325}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + xanthine = H(+) + NADH + urate;
CC Xref=Rhea:RHEA:16669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17712, ChEBI:CHEBI:17775, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.4;
CC Evidence={ECO:0000269|PubMed:14726515};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hypoxanthine + NAD(+) = H(+) + NADH + xanthine;
CC Xref=Rhea:RHEA:24670, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17368, ChEBI:CHEBI:17712, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.4;
CC Evidence={ECO:0000269|PubMed:14726515};
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 -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:14726515}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:14726515}.
CC -!- INDUCTION: By salt and drought stresses, and abscisic (ABA) treatment.
CC Down-regulated by cold and freezing stresses.
CC {ECO:0000269|PubMed:14726515, ECO:0000269|PubMed:15941399}.
CC -!- MISCELLANEOUS: Plants silencing simultaneously XDH1 and XDH2 show
CC reduced growth, impaired silique development, increased seed sterility,
CC precocious senescence of mature leaves and overaccumulation of
CC xanthine. {ECO:0000305|PubMed:17872919}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45450.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80206.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY171562; AAO11781.1; -; mRNA.
DR EMBL; AL079347; CAB45450.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161586; CAB80206.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86434.1; -; Genomic_DNA.
DR PIR; T10235; T10235.
DR RefSeq; NP_195215.2; NM_119655.4.
DR AlphaFoldDB; Q8GUQ8; -.
DR SMR; Q8GUQ8; -.
DR BioGRID; 14923; 2.
DR STRING; 3702.AT4G34890.1; -.
DR iPTMnet; Q8GUQ8; -.
DR PaxDb; Q8GUQ8; -.
DR PRIDE; Q8GUQ8; -.
DR ProteomicsDB; 243096; -.
DR EnsemblPlants; AT4G34890.1; AT4G34890.1; AT4G34890.
DR GeneID; 829641; -.
DR Gramene; AT4G34890.1; AT4G34890.1; AT4G34890.
DR KEGG; ath:AT4G34890; -.
DR Araport; AT4G34890; -.
DR TAIR; locus:2116900; AT4G34890.
DR eggNOG; KOG0430; Eukaryota.
DR HOGENOM; CLU_001681_1_2_1; -.
DR InParanoid; Q8GUQ8; -.
DR OMA; DIGYVWG; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; Q8GUQ8; -.
DR BioCyc; ARA:AT4G34890-MON; -.
DR BioCyc; MetaCyc:AT4G34890-MON; -.
DR BRENDA; 1.17.1.4; 399.
DR PRO; PR:Q8GUQ8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GUQ8; baseline and differential.
DR Genevisible; Q8GUQ8; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IDA:TAIR.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IMP:TAIR.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0042554; P:superoxide anion generation; IMP:TAIR.
DR GO; GO:0046110; P:xanthine metabolic process; IMP:TAIR.
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; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..1361
FT /note="Xanthine dehydrogenase 1"
FT /id="PRO_0000417457"
FT DOMAIN 15..101
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 257..442
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1297
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 58
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 61
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 83
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 123
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 126
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 159
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 161
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 285..292
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 375..379
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 796
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT BINDING 827
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT BINDING 831
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 909
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 941
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT BINDING 943
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1039
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1108
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT MUTAGEN 364
FT /note="W->A: Decreases activity 8-fold."
FT /evidence="ECO:0000269|PubMed:19915948"
FT MUTAGEN 421
FT /note="Y->A: Decreases activity 4-fold."
FT /evidence="ECO:0000269|PubMed:19915948"
FT MUTAGEN 831
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19915948"
FT MUTAGEN 909
FT /note="R->A: Decreases activity 12-fold."
FT /evidence="ECO:0000269|PubMed:19915948"
FT MUTAGEN 1297
FT /note="E->A: Decreases activity 40-fold."
FT /evidence="ECO:0000269|PubMed:19915948"
SQ SEQUENCE 1361 AA; 149196 MW; BF72FE23A1D59C88 CRC64;
MGSLKKDGEI GDEFTEALLY VNGVRRVLPD GLAHMTLLEY LRDLGLTGTK LGCGEGGCGA
CTVMVSSYDR KSKTSVHYAV NACLAPLYSV EGMHVISIEG LGHRKLGLHP VQESLASSHG
SQCGFCTPGF IMSMYSLLRS SKNSPSEEEI EECLAGNLCR CTGYRPIVDA FRVFAKSDDA
LYCGVSSLSL QDGSTICPST GKPCSCGSKT TNEVASCNED RFQSISYSDI DGAKYTDKEL
IFPPELLLRK LTPLKLRGNG GITWYRPVCL QNLLELKANY PDAKLLVGNT EVGIEMRLKR
LQYQVLISVA QVPELNALNV NDNGIEVGSA LRLSELLRLF RKIVKERPAH ETSACKAFIE
QLKWFAGTQI RNVACIGGNI CTASPISDLN PLWMASRAEF RITNCNGDVR SIPAKDFFLG
YRKVDMGSNE ILLSVFLPWT RPLEYVKEFK QAHRRDDDIA IVNGGMRVFL EDKGQQLFVS
DASIAYGGVA PLSLCARKTE EFLIGKNWNK DLLQDALKVI QSDVVIKEDA PGGMVEFRKS
LTLSFFFKFF LWVSHNVNNA NSAIETFPPS HMSAVQPVPR LSRIGKQDYE TVKQGTSVGS
SEVHLSARMQ VTGEAEYTDD TPVPPNTLHA AFVLSKVPHA RILSIDDSAA KSSSGFVGLF
LAKDIPGDNM IGPIVPDEEL FATDVVTCVG QVIGVVVADT HENAKTAAGK VDVRYEELPA
ILSIKEAINA KSFHPNTEKR LRKGDVELCF QSGQCDRVIE GEVQMGGQEH FYLEPNGSLV
WTVDGGSEVH MISSTQAPQK HQKYVSHVLG LPMSKVVCKT KRIGGGFGGK ETRSAFIAAA
ASVPSYLLNR PVKLILDRDV DMMITGHRHS FLGKYKVGFT NEGKILALDL EIYNNGGNSL
DLSLSVLERA MFHSDNVYEI PHVRIVGNVC FTNFPSNTAF RGFGGPQGML ITENWIQRIA
AELNKSPEEI KEMNFQVEGS VTHYCQTLQH CTLHQLWKEL KVSCNFLKAR READEFNSHN
RWKKRGVAMV PTKFGISFTT KFMNQAGALV HVYTDGTVLV THGGVEMGQG LHTKVAQVAA
SAFNIPLSSV FVSETSTDKV PNASPTAASA SSDMYGAAVL DACEQIIARM EPVASKHNFN
TFTELVSACY FQRIDLSAHG FHIVPDLGFD WISGKGNAFR YYTYGAAFAE VEIDTLTGDF
HTRAADIMLD LGYSLNPAID VGQIEGAFVQ GLGWVALEEL KWGDAAHKWI KPGSLLTCGP
GNYKIPSIND MPFNLNVSLL KGNPNTKAIH SSKAVGEPPF FLASSVFFAI KEAIKAARTE
VGLTDWFPLE SPATPERIRM ACFDEFSAPF VNSDFYPNLS V
