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Q9V407

- AXN_DROME

UniProt

Q9V407 - AXN_DROME

Protein

Axin

Gene

Axn

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Inhibitor of the WG signaling pathway. Down-regulates beta-catenin (armadillo=ARM). Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B (zeste-white 3=ZW3).1 Publication

    GO - Molecular functioni

    1. beta-catenin binding Source: FlyBase
    2. GTPase activator activity Source: RefGenome
    3. protein kinase binding Source: FlyBase
    4. signal transducer activity Source: InterPro

    GO - Biological processi

    1. eye-antennal disc morphogenesis Source: FlyBase
    2. heart development Source: FlyBase
    3. imaginal disc-derived wing morphogenesis Source: FlyBase
    4. imaginal disc pattern formation Source: FlyBase
    5. negative regulation of Wnt signaling pathway Source: FlyBase
    6. oogenesis Source: FlyBase
    7. phagocytosis Source: FlyBase
    8. positive regulation of GTPase activity Source: GOC
    9. somatic stem cell maintenance Source: FlyBase
    10. termination of G-protein coupled receptor signaling pathway Source: InterPro
    11. Wnt signaling pathway Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_207070. TCF dependent signaling in response to WNT.
    REACT_215026. degradation of AXIN.
    REACT_220429. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    SignaLinkiQ9V407.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Axin
    Alternative name(s):
    Axis inhibition protein
    d-Axin
    Short name:
    dAxin
    Gene namesi
    Name:Axn
    ORF Names:CG7926
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0026597. Axn.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase
    2. nucleus Source: FlyBase
    3. plasma membrane Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 745745AxinPRO_0000220894Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei513 – 5131Phosphothreonine1 Publication
    Modified residuei517 – 5171Phosphoserine1 Publication
    Modified residuei522 – 5221Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9V407.
    PRIDEiQ9V407.

    Expressioni

    Developmental stagei

    Ubiquitously expressed throughout the development.

    Gene expression databases

    BgeeiQ9V407.

    Interactioni

    Subunit structurei

    Interacts with ZW3 and ARM. The interaction between AXN and ARM occurs via the armadillo repeats contained in ARM.

    Protein-protein interaction databases

    BioGridi68421. 14 interactions.
    DIPiDIP-20929N.
    IntActiQ9V407. 1 interaction.
    MINTiMINT-926493.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9V407.
    SMRiQ9V407. Positions 46-171, 663-745.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini54 – 172119RGSPROSITE-ProRule annotationAdd
    BLAST
    Domaini663 – 74583DIXPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi640 – 6467Poly-Ser

    Sequence similaritiesi

    Contains 1 DIX domain.PROSITE-ProRule annotation
    Contains 1 RGS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG238205.
    GeneTreeiENSGT00390000010011.
    InParanoidiQ9V407.
    KOiK02157.
    OMAiRQSAMAN.
    OrthoDBiEOG79PJQ0.
    PhylomeDBiQ9V407.

    Family and domain databases

    Gene3Di1.10.196.10. 2 hits.
    InterProiIPR014936. Axin_b-cat-bd.
    IPR001158. DIX.
    IPR024066. Regulat_G_prot_signal_dom1.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF08833. Axin_b-cat_bind. 1 hit.
    PF00778. DIX. 1 hit.
    PF00615. RGS. 1 hit.
    [Graphical view]
    SMARTiSM00315. RGS. 1 hit.
    [Graphical view]
    SUPFAMiSSF48097. SSF48097. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS50841. DIX. 1 hit.
    PS50132. RGS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9V407-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGHPSGIRK HDDNECSGPR PPVPGEESRV KKMTEGVADT SKNSSPSYLN    50
    WARTLNHLLE DRDGVELFKK YVEEEAPAYN DHLNFYFACE GLKQQTDPEK 100
    IKQIIGAIYR FLRKSQLSIS DDLRAQIKAI KTNPEIPLSP HIFDPMQRHV 150
    EVTIRDNIYP TFLCSEMYIL YIQQMSAQQE RCTSSGATGS GSAGSSGSGG 200
    SSLAGACALP PTTASGKQQL PQLVPPGAFI NLPVSSVSGP PAGTCSASGS 250
    VYGPSTSASS SGSISATDTL PRSSTLPTLH EDSVLSLCDD FEKVQMQEGG 300
    GSLGSGSVGA GARAPDYPIR LTRDLLIATQ KRRLEIRPPG AHGYVYNPST 350
    TNTSYVPNSR VDSERASVSS GGRTDSDTMS ISSCSMDGRP YIQRRHSSTE 400
    SKAIRQSAMA NKETNTFQVI PRTQRLHSNE HRPLKEEELV SLLIPKLEEV 450
    KRKRDLEERA RERNPGAALL TNERSSASDR AFAEAIREKF ALDEDNDQDI 500
    LDQHVSRVWK DQTPHRSPGT MSPCPPIPSR RRTATHDSGM VSDGAMSLSG 550
    HSMKHSKSMP DHSSCSRKLT NKWPSMNTDS GISMFSADTV TKYKDASSRS 600
    GSSTASKLEE AKRRLEDEPR RSRRYAQPPM QHLSQQPLAS FSSSSSGGSI 650
    SLPHQPPPLP AKPPETIVVF SFCEEPVPYR IKIPGTQPTL RQFKDYLPRR 700
    GHFRFFFKTH CEDPDSPVIQ EEIVNDSDIL PLFGDKAMGL VKPSD 745
    Length:745
    Mass (Da):81,718
    Last modified:May 1, 2000 - v1
    Checksum:i31A502528CEE84BA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti454 – 4541R → Q in AAD24886. (PubMed:10073940)Curated
    Sequence conflicti644 – 6452Missing in AAD24886. (PubMed:10073940)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF086811 mRNA. Translation: AAD24886.1.
    AF091813 mRNA. Translation: AAF21293.1.
    AE014297 Genomic DNA. Translation: AAF56993.1.
    RefSeqiNP_733336.1. NM_170457.3.
    NP_733337.1. NM_170458.2.
    UniGeneiDm.7154.

    Genome annotation databases

    EnsemblMetazoaiFBtr0085553; FBpp0084919; FBgn0026597.
    FBtr0085555; FBpp0084921; FBgn0026597.
    GeneIDi43565.
    KEGGidme:Dmel_CG7926.
    UCSCiCG7926-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF086811 mRNA. Translation: AAD24886.1 .
    AF091813 mRNA. Translation: AAF21293.1 .
    AE014297 Genomic DNA. Translation: AAF56993.1 .
    RefSeqi NP_733336.1. NM_170457.3.
    NP_733337.1. NM_170458.2.
    UniGenei Dm.7154.

    3D structure databases

    ProteinModelPortali Q9V407.
    SMRi Q9V407. Positions 46-171, 663-745.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68421. 14 interactions.
    DIPi DIP-20929N.
    IntActi Q9V407. 1 interaction.
    MINTi MINT-926493.

    Proteomic databases

    PaxDbi Q9V407.
    PRIDEi Q9V407.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0085553 ; FBpp0084919 ; FBgn0026597 .
    FBtr0085555 ; FBpp0084921 ; FBgn0026597 .
    GeneIDi 43565.
    KEGGi dme:Dmel_CG7926.
    UCSCi CG7926-RA. d. melanogaster.

    Organism-specific databases

    CTDi 43565.
    FlyBasei FBgn0026597. Axn.

    Phylogenomic databases

    eggNOGi NOG238205.
    GeneTreei ENSGT00390000010011.
    InParanoidi Q9V407.
    KOi K02157.
    OMAi RQSAMAN.
    OrthoDBi EOG79PJQ0.
    PhylomeDBi Q9V407.

    Enzyme and pathway databases

    Reactomei REACT_207070. TCF dependent signaling in response to WNT.
    REACT_215026. degradation of AXIN.
    REACT_220429. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    SignaLinki Q9V407.

    Miscellaneous databases

    GenomeRNAii 43565.
    NextBioi 834579.
    PROi Q9V407.

    Gene expression databases

    Bgeei Q9V407.

    Family and domain databases

    Gene3Di 1.10.196.10. 2 hits.
    InterProi IPR014936. Axin_b-cat-bd.
    IPR001158. DIX.
    IPR024066. Regulat_G_prot_signal_dom1.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF08833. Axin_b-cat_bind. 1 hit.
    PF00778. DIX. 1 hit.
    PF00615. RGS. 1 hit.
    [Graphical view ]
    SMARTi SM00315. RGS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48097. SSF48097. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50841. DIX. 1 hit.
    PS50132. RGS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Negative regulation of Wingless signaling by D-axin, a Drosophila homolog of axin."
      Hamada F., Tomoyasu Y., Takatsu Y., Nakamura M., Nagai S., Suzuki A., Fujita F., Shibuya H., Toyoshima K., Ueno N., Akiyama T.
      Science 283:1739-1742(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Embryo.
    2. "A Drosophila homolog of the axin gene is involved in the transduction of the wingless signal regulating the stability of the armadillo protein."
      Ruel L., Anthopoulos N., Goncalves J., Manoukian A.S., Woodgett J.R.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. "A Drosophila Axin homolog, Daxin, inhibits Wnt signaling."
      Willert K., Logan C.Y., Arora A., Fish M., Nusse R.
      Development 126:4165-4173(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-513; SER-517 AND SER-522, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiAXN_DROME
    AccessioniPrimary (citable) accession number: Q9V407
    Secondary accession number(s): Q9XYC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 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