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   27-MAR-2024, entry version 203.
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};
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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; 7227-FBpp0082172; -.
DR   DNASU; 41605; -.
DR   EnsemblMetazoa; FBtr0082704; FBpp0082172; FBgn0003308.
DR   GeneID; 41605; -.
DR   KEGG; dme:Dmel_CG7642; -.
DR   AGR; FB:FBgn0003308; -.
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; PHPTQER; -.
DR   OrthoDB; 3715804at2759; -.
DR   PhylomeDB; P10351; -.
DR   Reactome; R-DME-74259; Purine catabolism.
DR   Reactome; R-DME-964975; Vitamin 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 cell types or tissues.
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:0004854; F:xanthine dehydrogenase activity; IMP:FlyBase.
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; 3.30.465.10; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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-like.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
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   NCBIfam; TIGR02963; xanthine_xdhA; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11908:SF100; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 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   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_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; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 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.
DR   Genevisible; P10351; DM.
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
//