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P10351

- XDH_DROME

UniProt

P10351 - XDH_DROME

Protein

Xanthine dehydrogenase

Gene

ry

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (20 Jun 2003)
      Previous versions | rss
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    Functioni

    Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid By similarity.By similarity

    Catalytic activityi

    Xanthine + NAD+ + H2O = urate + NADH.
    Hypoxanthine + NAD+ + H2O = xanthine + NADH.

    Cofactori

    Binds 2 2Fe-2S clusters.By similarity
    FAD.By similarity
    Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi43 – 431Iron-sulfur 1By similarity
    Metal bindingi48 – 481Iron-sulfur 1By similarity
    Metal bindingi51 – 511Iron-sulfur 1By similarity
    Metal bindingi73 – 731Iron-sulfur 1By similarity
    Metal bindingi113 – 1131Iron-sulfur 2By similarity
    Metal bindingi116 – 1161Iron-sulfur 2By similarity
    Metal bindingi148 – 1481Iron-sulfur 2By similarity
    Metal bindingi150 – 1501Iron-sulfur 2By similarity
    Binding sitei335 – 3351FADBy similarity
    Binding sitei358 – 3581FADBy similarity
    Binding sitei406 – 4061FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei424 – 4241FADBy similarity
    Metal bindingi772 – 7721MolybdenumBy similarity
    Metal bindingi803 – 8031Molybdenum; via carbonyl oxygenBy similarity
    Binding sitei807 – 8071SubstrateBy similarity
    Binding sitei885 – 8851SubstrateBy similarity
    Metal bindingi917 – 9171Molybdenum; via amide nitrogenBy similarity
    Binding sitei919 – 9191SubstrateBy similarity
    Metal bindingi1084 – 10841Molybdenum; via amide nitrogenBy similarity
    Active sitei1267 – 12671Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi255 – 2628FADBy similarity
    Nucleotide bindingi345 – 3495FADBy similarity

    GO - Molecular functioni

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
    2. electron carrier activity Source: InterPro
    3. flavin adenine dinucleotide binding Source: UniProtKB
    4. iron ion binding Source: InterPro
    5. molybdopterin cofactor binding Source: UniProtKB
    6. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
    7. xanthine dehydrogenase activity Source: UniProtKB
    8. xanthine oxidase activity Source: InterPro

    GO - Biological processi

    1. arginine metabolic process Source: FlyBase
    2. compound eye pigmentation Source: FlyBase
    3. determination of adult lifespan Source: FlyBase
    4. glycerophospholipid metabolic process Source: FlyBase
    5. purine nucleobase metabolic process Source: FlyBase
    6. pyrimidine nucleobase metabolic process Source: FlyBase
    7. tryptophan metabolic process Source: FlyBase
    8. xanthine catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

    Enzyme and pathway databases

    ReactomeiREACT_180681. Vitamins B6 activation to pyridoxal phosphate.
    REACT_207989. Purine catabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xanthine dehydrogenase (EC:1.17.1.4)
    Short name:
    XD
    Alternative name(s):
    Protein rosy locus
    Gene namesi
    Name:ry
    Synonyms:XDH
    ORF Names:CG7642
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0003308. ry.

    Subcellular locationi

    Peroxisome By similarity

    GO - Cellular componenti

    1. microtubule associated complex Source: FlyBase
    2. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13351335Xanthine dehydrogenasePRO_0000166079Add
    BLAST

    Proteomic databases

    PaxDbiP10351.

    Expressioni

    Gene expression databases

    BgeeiP10351.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiP10351. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP10351.
    SMRiP10351. Positions 6-165, 193-529, 573-1317.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 91882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini227 – 416190FAD-binding PCMH-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the xanthine dehydrogenase family.Curated
    Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
    Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG4630.
    GeneTreeiENSGT00390000003772.
    InParanoidiP10351.
    KOiK00106.
    OMAiFHMENSY.
    OrthoDBiEOG7QRQSZ.
    PhylomeDBiP10351.

    Family and domain databases

    Gene3Di1.10.150.120. 1 hit.
    3.10.20.30. 1 hit.
    3.30.365.10. 6 hits.
    3.30.43.10. 1 hit.
    3.30.465.10. 1 hit.
    3.90.1170.50. 1 hit.
    InterProiIPR002888. 2Fe-2S-bd.
    IPR001041. 2Fe-2S_ferredoxin-type.
    IPR006058. 2Fe2S_fd_BS.
    IPR000674. Ald_Oxase/Xan_DH_a/b.
    IPR016208. Ald_Oxase/xanthine_DH.
    IPR008274. AldOxase/xan_DH_Mopterin-bd.
    IPR012675. Beta-grasp_dom.
    IPR005107. CO_DH_flav_C.
    IPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR016167. FAD-bd_2_sub1.
    IPR002346. Mopterin_DH_FAD-bd.
    IPR022407. OxRdtase_Mopterin_BS.
    IPR014307. Xanthine_DH_ssu.
    [Graphical view]
    PfamiPF01315. Ald_Xan_dh_C. 1 hit.
    PF02738. Ald_Xan_dh_C2. 1 hit.
    PF03450. CO_deh_flav_C. 1 hit.
    PF00941. FAD_binding_5. 1 hit.
    PF00111. Fer2. 1 hit.
    PF01799. Fer2_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
    SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
    SM01092. CO_deh_flav_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF47741. SSF47741. 1 hit.
    SSF54292. SSF54292. 1 hit.
    SSF54665. SSF54665. 1 hit.
    SSF55447. SSF55447. 1 hit.
    SSF56003. SSF56003. 1 hit.
    SSF56176. SSF56176. 1 hit.
    TIGRFAMsiTIGR02963. xanthine_xdhA. 1 hit.
    PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    PS51387. FAD_PCMH. 1 hit.
    PS00559. MOLYBDOPTERIN_EUK. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10351-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNSVLVFFV NGKKVTEVSP DPECTLLTFL REKLRLCGTK LGCAEGGCGA     50
    CTVMVSRLDR RANKIRHLAV NACLTPVCSM HGCAVTTVEG IGSTKTRLHP 100
    VQERLAKAHG SQCGFCTPGI VMSMYALLRN AEQPSMRDLE VAFQGNLCRC 150
    TGYRPILEGY KTFTKEFACG MGEKCCKVSG KGCGTDAETD DKLFERSEFQ 200
    PLDPSQEPIF PPELQLSDAF DSQSLIFSSD RVTWYRPTNL EELLQLKAKH 250
    PAAKLVVGNT EVGVEVKFKH FLYPHLINPT QVKELLEIKE NQDGIYFGAA 300
    VSLMEIDALL RQRIEQLPES ETRLFQCTVD MLHYFAGKQI RNVACLGGNI 350
    MTGSPISDMN PVLSAAGAQL EVASFVDGKL QKRSVHMGTG FFTGYRRNVI 400
    EAHEVLLGIH FRKTTPDQYI VAFKQARRRD DDIAIVNAAI NVRFEEKSNI 450
    VAEISMAFGG MAPTTVLAPR TSQLMVGQEW SHQLVERVAE SLCTELPLAA 500
    SAPGGMIAYR RALVVSLFFK AYLAISLKLS KSGITSSDAL PSEERSGAET 550
    FHTPVLKSAQ LFERVCSDQP ICDPIGRPKV HAAALKQATG EAIYTDDIPR 600
    MDGEVYLAFV LSTKPRAKIT KLDASEALAL DGVHQFFCYK DLTEHENEVG 650
    PVFHDEHVFA AGEVHCYGQI VGAIAADNKA LAQRAARLVK VEYEELSPVI 700
    VTIEQAIEHK SYFPDYPRFV TKGNVEEALA QADHTFEGTC RMGGQEHFYL 750
    ETHAALAVPR DSDELELFCS TQHPSEVQKL VAHVTALPAH RVVCRAKRLG 800
    GGFGGKESRG ISVALPVALA AYRMGRPVRC MLDRDEDMLI TGTRHPFLFK 850
    YKVGFTKEGL ITACDIECYN NAGWSMDLSF SVLERAMFHF ENCYRIPNVR 900
    VGGWVCKTNL PSNTAFRGFG GPQGMYAGEH IIRDVARIVG RDVVDVMRLN 950
    FYKTGDYTHY HQQLEHFPIE RCLEDCLKQS RYDEKRQEIA RFNRENRWRK 1000
    RGMAVVPTKY GIAFGVMHLN QAGSLINIYG DGSVLLSHGG VEIGQGLNTK 1050
    MIQCAARALG IPSELIHISE TATDKVPNTS PTAASVGSDL NGMAVLDACE 1100
    KLNKRLAPIK EALPGGTWKE WINKAYFDRV SLSATGFYAM PGIGYHPETN 1150
    PNARTYSYYT NGVGVTVVEI DCLTGDHQVL STDIVMDIGS SLNPAIDIGQ 1200
    IEGAFMQGYG LFTLEELMYS PQGMLYSRGP GMYKLPGFAD IPGEFNVSLL 1250
    TGAPNPRAVY SSKAVGEPPL FIGSSAFFAI KEAIAAARED QGLSGDFPLE 1300
    APSTSARIRI ACQDKFTELL EIPEPGSFTP WNIVP 1335
    Length:1,335
    Mass (Da):146,927
    Last modified:June 20, 2003 - v2
    Checksum:i230368EA59B30AD8
    GO

    Sequence cautioni

    The sequence AAM11042.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061A → P in CAA68409. 1 PublicationCurated
    Sequence conflicti106 – 1061A → P no nucleotide entry (PubMed:3036645)Curated
    Sequence conflicti316 – 3161Q → L in CAA68409. 1 PublicationCurated
    Sequence conflicti316 – 3161Q → L no nucleotide entry (PubMed:3036646)Curated
    Sequence conflicti542 – 5421S → P in CAA68409. 1 PublicationCurated
    Sequence conflicti542 – 5421S → P no nucleotide entry (PubMed:3036646)Curated
    Sequence conflicti709 – 7091H → L in CAA68409. 1 PublicationCurated
    Sequence conflicti709 – 7091H → L no nucleotide entry (PubMed:3036646)Curated
    Sequence conflicti730 – 7301A → S in CAA68409. 1 PublicationCurated
    Sequence conflicti730 – 7301A → S no nucleotide entry (PubMed:3036646)Curated
    Sequence conflicti988 – 9881E → D in CAA68409. 1 PublicationCurated
    Sequence conflicti988 – 9881E → D no nucleotide entry (PubMed:3036646)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00308 Genomic DNA. Translation: CAA68409.1.
    AE014297 Genomic DNA. Translation: AAF54895.1.
    BT015293 mRNA. Translation: AAT94522.1.
    AY094689 mRNA. Translation: AAM11042.1. Different initiation.
    PIRiS07245.
    RefSeqiNP_524337.1. NM_079613.3.
    UniGeneiDm.2436.

    Genome annotation databases

    EnsemblMetazoaiFBtr0082704; FBpp0082172; FBgn0003308.
    GeneIDi41605.
    KEGGidme:Dmel_CG7642.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00308 Genomic DNA. Translation: CAA68409.1 .
    AE014297 Genomic DNA. Translation: AAF54895.1 .
    BT015293 mRNA. Translation: AAT94522.1 .
    AY094689 mRNA. Translation: AAM11042.1 . Different initiation.
    PIRi S07245.
    RefSeqi NP_524337.1. NM_079613.3.
    UniGenei Dm.2436.

    3D structure databases

    ProteinModelPortali P10351.
    SMRi P10351. Positions 6-165, 193-529, 573-1317.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P10351. 1 interaction.

    Proteomic databases

    PaxDbi P10351.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0082704 ; FBpp0082172 ; FBgn0003308 .
    GeneIDi 41605.
    KEGGi dme:Dmel_CG7642.

    Organism-specific databases

    CTDi 41605.
    FlyBasei FBgn0003308. ry.

    Phylogenomic databases

    eggNOGi COG4630.
    GeneTreei ENSGT00390000003772.
    InParanoidi P10351.
    KOi K00106.
    OMAi FHMENSY.
    OrthoDBi EOG7QRQSZ.
    PhylomeDBi P10351.

    Enzyme and pathway databases

    Reactomei REACT_180681. Vitamins B6 activation to pyridoxal phosphate.
    REACT_207989. Purine catabolism.

    Miscellaneous databases

    GenomeRNAii 41605.
    NextBioi 824612.
    PROi P10351.

    Gene expression databases

    Bgeei P10351.

    Family and domain databases

    Gene3Di 1.10.150.120. 1 hit.
    3.10.20.30. 1 hit.
    3.30.365.10. 6 hits.
    3.30.43.10. 1 hit.
    3.30.465.10. 1 hit.
    3.90.1170.50. 1 hit.
    InterProi IPR002888. 2Fe-2S-bd.
    IPR001041. 2Fe-2S_ferredoxin-type.
    IPR006058. 2Fe2S_fd_BS.
    IPR000674. Ald_Oxase/Xan_DH_a/b.
    IPR016208. Ald_Oxase/xanthine_DH.
    IPR008274. AldOxase/xan_DH_Mopterin-bd.
    IPR012675. Beta-grasp_dom.
    IPR005107. CO_DH_flav_C.
    IPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR016167. FAD-bd_2_sub1.
    IPR002346. Mopterin_DH_FAD-bd.
    IPR022407. OxRdtase_Mopterin_BS.
    IPR014307. Xanthine_DH_ssu.
    [Graphical view ]
    Pfami PF01315. Ald_Xan_dh_C. 1 hit.
    PF02738. Ald_Xan_dh_C2. 1 hit.
    PF03450. CO_deh_flav_C. 1 hit.
    PF00941. FAD_binding_5. 1 hit.
    PF00111. Fer2. 1 hit.
    PF01799. Fer2_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000127. Xanthine_DH. 1 hit.
    SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
    SM01092. CO_deh_flav_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47741. SSF47741. 1 hit.
    SSF54292. SSF54292. 1 hit.
    SSF54665. SSF54665. 1 hit.
    SSF55447. SSF55447. 1 hit.
    SSF56003. SSF56003. 1 hit.
    SSF56176. SSF56176. 1 hit.
    TIGRFAMsi TIGR02963. xanthine_xdhA. 1 hit.
    PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    PS51387. FAD_PCMH. 1 hit.
    PS00559. MOLYBDOPTERIN_EUK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Riley M.A.
      Submitted (FEB-1987) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Canton-S.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.
    5. "Mutations affecting expression of the rosy locus in Drosophila melanogaster."
      Lee C.S., Curtis D., Gray M., Bender W.
      Genetics 116:55-66(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-231, FUNCTION.
      Strain: Canton-S.
    6. "Sequence of the structural gene for xanthine dehydrogenase (rosy locus) in Drosophila melanogaster."
      Keith T.P., Riley M.A., Kreitman M., Lewontin R.C., Curtis D., Chambers G.
      Genetics 116:67-73(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-1335.
      Strain: Canton-S.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 544-1335.
      Strain: Berkeley.
      Tissue: Head.

    Entry informationi

    Entry nameiXDH_DROME
    AccessioniPrimary (citable) accession number: P10351
    Secondary accession number(s): Q6AWF5, Q8SXC4, Q9VFZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: June 20, 2003
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3