XDH_DROME
ID XDH_DROME Reviewed; 1335 AA.
AC P10351; Q6AWF5; Q8SXC4; Q9VFZ9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Xanthine dehydrogenase;
DE Short=XD;
DE EC=1.17.1.4;
DE AltName: Full=Protein rosy locus;
GN Name=ry; Synonyms=XDH; ORFNames=CG7642;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RA Riley M.A.;
RL Submitted (FEB-1987) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-231, AND FUNCTION.
RC STRAIN=Canton-S;
RX PubMed=3036645; DOI=10.1093/genetics/116.1.55;
RA Lee C.S., Curtis D., Gray M., Bender W.;
RT "Mutations affecting expression of the rosy locus in Drosophila
RT melanogaster.";
RL Genetics 116:55-66(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-1335.
RC STRAIN=Canton-S;
RX PubMed=3036646; DOI=10.1093/genetics/116.1.67;
RA Keith T.P., Riley M.A., Kreitman M., Lewontin R.C., Curtis D., Chambers G.;
RT "Sequence of the structural gene for xanthine dehydrogenase (rosy locus) in
RT Drosophila melanogaster.";
RL Genetics 116:67-73(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 544-1335.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Key enzyme in purine degradation. Catalyzes the oxidation of
CC hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric
CC acid (By similarity). {ECO:0000250, ECO:0000269|PubMed:3036645}.
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 -!- 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 -!- 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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P22985};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000250|UniProtKB:P22985};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM11042.1; Type=Erroneous initiation; 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; Y00308; CAA68409.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54895.1; -; Genomic_DNA.
DR EMBL; BT015293; AAT94522.1; -; mRNA.
DR EMBL; AY094689; AAM11042.1; ALT_INIT; mRNA.
DR PIR; S07245; S07245.
DR RefSeq; NP_524337.1; NM_079613.3.
DR AlphaFoldDB; P10351; -.
DR SMR; P10351; -.
DR BioGRID; 66692; 7.
DR IntAct; P10351; 4.
DR STRING; 7227.FBpp0082172; -.
DR PaxDb; P10351; -.
DR PRIDE; P10351; -.
DR DNASU; 41605; -.
DR EnsemblMetazoa; FBtr0082704; FBpp0082172; FBgn0003308.
DR GeneID; 41605; -.
DR KEGG; dme:Dmel_CG7642; -.
DR CTD; 41605; -.
DR FlyBase; FBgn0003308; ry.
DR VEuPathDB; VectorBase:FBgn0003308; -.
DR eggNOG; KOG0430; Eukaryota.
DR GeneTree; ENSGT00950000183114; -.
DR HOGENOM; CLU_001681_1_2_1; -.
DR InParanoid; P10351; -.
DR OMA; DIGYVWG; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; P10351; -.
DR Reactome; R-DME-74259; Purine catabolism.
DR Reactome; R-DME-964975; Vitamins B6 activation to pyridoxal phosphate.
DR Reactome; R-DME-9748787; Azathioprine ADME.
DR SignaLink; P10351; -.
DR BioGRID-ORCS; 41605; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41605; -.
DR PRO; PR:P10351; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003308; Expressed in adult Malpighian tubule (Drosophila) and 42 other tissues.
DR Genevisible; P10351; DM.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IMP:FlyBase.
DR GO; GO:0004855; F:xanthine oxidase activity; IEA:InterPro.
DR GO; GO:0006525; P:arginine metabolic process; IMP:FlyBase.
DR GO; GO:0048072; P:compound eye pigmentation; TAS:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IMP:FlyBase.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IMP:FlyBase.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IMP:FlyBase.
DR GO; GO:0006568; P:tryptophan metabolic process; IMP:FlyBase.
DR GO; GO:0009115; P:xanthine catabolic process; ISS:UniProtKB.
DR CDD; cd00207; fer2; 1.
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 InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR InterPro; IPR014307; Xanthine_DH_ssu.
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 TIGRFAMs; TIGR02963; xanthine_xdhA; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW NAD; Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..1335
FT /note="Xanthine dehydrogenase"
FT /id="PRO_0000166079"
FT DOMAIN 4..91
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 227..416
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1267
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 113
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 116
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 148
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 150
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 255..262
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 345..349
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 772
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 803
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 807
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 885
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 917
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 919
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1084
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 CONFLICT 106
FT /note="A -> P (in Ref. 1; CAA68409 and 5; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="Q -> L (in Ref. 1; CAA68409 and 6; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="S -> P (in Ref. 1; CAA68409 and 6; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="H -> L (in Ref. 1; CAA68409 and 6; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="A -> S (in Ref. 1; CAA68409 and 6; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 988
FT /note="E -> D (in Ref. 1; CAA68409 and 6; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1335 AA; 146927 MW; 230368EA59B30AD8 CRC64;
MSNSVLVFFV NGKKVTEVSP DPECTLLTFL REKLRLCGTK LGCAEGGCGA CTVMVSRLDR
RANKIRHLAV NACLTPVCSM HGCAVTTVEG IGSTKTRLHP VQERLAKAHG SQCGFCTPGI
VMSMYALLRN AEQPSMRDLE VAFQGNLCRC TGYRPILEGY KTFTKEFACG MGEKCCKVSG
KGCGTDAETD DKLFERSEFQ PLDPSQEPIF PPELQLSDAF DSQSLIFSSD RVTWYRPTNL
EELLQLKAKH PAAKLVVGNT EVGVEVKFKH FLYPHLINPT QVKELLEIKE NQDGIYFGAA
VSLMEIDALL RQRIEQLPES ETRLFQCTVD MLHYFAGKQI RNVACLGGNI MTGSPISDMN
PVLSAAGAQL EVASFVDGKL QKRSVHMGTG FFTGYRRNVI EAHEVLLGIH FRKTTPDQYI
VAFKQARRRD DDIAIVNAAI NVRFEEKSNI VAEISMAFGG MAPTTVLAPR TSQLMVGQEW
SHQLVERVAE SLCTELPLAA SAPGGMIAYR RALVVSLFFK AYLAISLKLS KSGITSSDAL
PSEERSGAET FHTPVLKSAQ LFERVCSDQP ICDPIGRPKV HAAALKQATG EAIYTDDIPR
MDGEVYLAFV LSTKPRAKIT KLDASEALAL DGVHQFFCYK DLTEHENEVG PVFHDEHVFA
AGEVHCYGQI VGAIAADNKA LAQRAARLVK VEYEELSPVI VTIEQAIEHK SYFPDYPRFV
TKGNVEEALA QADHTFEGTC RMGGQEHFYL ETHAALAVPR DSDELELFCS TQHPSEVQKL
VAHVTALPAH RVVCRAKRLG GGFGGKESRG ISVALPVALA AYRMGRPVRC MLDRDEDMLI
TGTRHPFLFK YKVGFTKEGL ITACDIECYN NAGWSMDLSF SVLERAMFHF ENCYRIPNVR
VGGWVCKTNL PSNTAFRGFG GPQGMYAGEH IIRDVARIVG RDVVDVMRLN FYKTGDYTHY
HQQLEHFPIE RCLEDCLKQS RYDEKRQEIA RFNRENRWRK RGMAVVPTKY GIAFGVMHLN
QAGSLINIYG DGSVLLSHGG VEIGQGLNTK MIQCAARALG IPSELIHISE TATDKVPNTS
PTAASVGSDL NGMAVLDACE KLNKRLAPIK EALPGGTWKE WINKAYFDRV SLSATGFYAM
PGIGYHPETN PNARTYSYYT NGVGVTVVEI DCLTGDHQVL STDIVMDIGS SLNPAIDIGQ
IEGAFMQGYG LFTLEELMYS PQGMLYSRGP GMYKLPGFAD IPGEFNVSLL TGAPNPRAVY
SSKAVGEPPL FIGSSAFFAI KEAIAAARED QGLSGDFPLE APSTSARIRI ACQDKFTELL
EIPEPGSFTP WNIVP
