AXN_DROME
ID AXN_DROME Reviewed; 745 AA.
AC Q9V407; Q9XYC1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Axin;
DE AltName: Full=Axis inhibition protein;
DE AltName: Full=d-Axin;
DE Short=dAxin;
GN Name=Axn; ORFNames=CG7926;
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 [MRNA].
RC TISSUE=Embryo;
RX PubMed=10073940; DOI=10.1126/science.283.5408.1739;
RA Hamada F., Tomoyasu Y., Takatsu Y., Nakamura M., Nagai S., Suzuki A.,
RA Fujita F., Shibuya H., Toyoshima K., Ueno N., Akiyama T.;
RT "Negative regulation of Wingless signaling by D-axin, a Drosophila homolog
RT of axin.";
RL Science 283:1739-1742(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ruel L., Anthopoulos N., Goncalves J., Manoukian A.S., Woodgett J.R.;
RT "A Drosophila homolog of the axin gene is involved in the transduction of
RT the wingless signal regulating the stability of the armadillo protein.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=10457025; DOI=10.1242/dev.126.18.4165;
RA Willert K., Logan C.Y., Arora A., Fish M., Nusse R.;
RT "A Drosophila Axin homolog, Daxin, inhibits Wnt signaling.";
RL Development 126:4165-4173(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-513; SER-517 AND SER-522, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Inhibitor of the WG signaling pathway. Down-regulates beta-
CC catenin (armadillo=ARM). Probably facilitate the phosphorylation of
CC beta-catenin and APC by GSK3B (zeste-white 3=ZW3).
CC {ECO:0000269|PubMed:10457025}.
CC -!- SUBUNIT: Interacts with ZW3 and ARM. The interaction between AXN and
CC ARM occurs via the armadillo repeats contained in ARM.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed throughout the development.
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DR EMBL; AF086811; AAD24886.1; -; mRNA.
DR EMBL; AF091813; AAF21293.1; -; mRNA.
DR EMBL; AE014297; AAF56993.1; -; Genomic_DNA.
DR RefSeq; NP_733336.1; NM_170457.3.
DR RefSeq; NP_733337.1; NM_170458.2.
DR AlphaFoldDB; Q9V407; -.
DR SMR; Q9V407; -.
DR BioGRID; 68421; 37.
DR DIP; DIP-20929N; -.
DR IntAct; Q9V407; 2.
DR MINT; Q9V407; -.
DR STRING; 7227.FBpp0084919; -.
DR iPTMnet; Q9V407; -.
DR PaxDb; Q9V407; -.
DR PRIDE; Q9V407; -.
DR EnsemblMetazoa; FBtr0085553; FBpp0084919; FBgn0026597.
DR EnsemblMetazoa; FBtr0085555; FBpp0084921; FBgn0026597.
DR GeneID; 43565; -.
DR KEGG; dme:Dmel_CG7926; -.
DR UCSC; CG7926-RA; d. melanogaster.
DR CTD; 43565; -.
DR FlyBase; FBgn0026597; Axn.
DR VEuPathDB; VectorBase:FBgn0026597; -.
DR eggNOG; KOG3589; Eukaryota.
DR InParanoid; Q9V407; -.
DR OMA; YVYTAST; -.
DR OrthoDB; 1481971at2759; -.
DR PhylomeDB; Q9V407; -.
DR Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-DME-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-DME-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-DME-209155; Phosphorylation of AXN and APC.
DR Reactome; R-DME-209190; Phosphorylation of CI.
DR Reactome; R-DME-209214; Phosphorylation of SMO.
DR Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
DR Reactome; R-DME-209396; Phosphorylation of ARM.
DR Reactome; R-DME-209413; Assembly of the 'destruction complex'.
DR Reactome; R-DME-209440; Recruitment of the 'destruction complex' to the receptor complex, the degradation of AXN and release of ARM.
DR Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
DR Reactome; R-DME-432553; Phosphorylation of PER and TIM.
DR Reactome; R-DME-4641257; Degradation of AXIN.
DR Reactome; R-DME-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR SignaLink; Q9V407; -.
DR BioGRID-ORCS; 43565; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43565; -.
DR PRO; PR:Q9V407; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0026597; Expressed in wing disc and 26 other tissues.
DR ExpressionAtlas; Q9V407; baseline and differential.
DR Genevisible; Q9V407; DM.
DR GO; GO:0030877; C:beta-catenin destruction complex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:1990909; C:Wnt signalosome; IDA:FlyBase.
DR GO; GO:0008013; F:beta-catenin binding; IDA:FlyBase.
DR GO; GO:0060090; F:molecular adaptor activity; IGI:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:FlyBase.
DR GO; GO:0005102; F:signaling receptor binding; IPI:FlyBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0048468; P:cell development; IBA:GO_Central.
DR GO; GO:0035293; P:chitin-based larval cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0007450; P:dorsal/ventral pattern formation, imaginal disc; IMP:FlyBase.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0005977; P:glycogen metabolic process; IMP:FlyBase.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0010941; P:regulation of cell death; IGI:FlyBase.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR Gene3D; 2.40.240.130; -; 1.
DR InterPro; IPR043581; Axin-like.
DR InterPro; IPR014936; Axin_b-cat-bd.
DR InterPro; IPR001158; DIX.
DR InterPro; IPR038207; DIX_dom_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46102; PTHR46102; 1.
DR Pfam; PF08833; Axin_b-cat_bind; 1.
DR Pfam; PF00778; DIX; 1.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00021; DAX; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..745
FT /note="Axin"
FT /id="PRO_0000220894"
FT DOMAIN 54..172
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 663..745
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 513
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 454
FT /note="R -> Q (in Ref. 1; AAD24886)"
FT /evidence="ECO:0000305"
FT CONFLICT 644..645
FT /note="Missing (in Ref. 1; AAD24886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 745 AA; 81718 MW; 31A502528CEE84BA CRC64;
MSGHPSGIRK HDDNECSGPR PPVPGEESRV KKMTEGVADT SKNSSPSYLN WARTLNHLLE
DRDGVELFKK YVEEEAPAYN DHLNFYFACE GLKQQTDPEK IKQIIGAIYR FLRKSQLSIS
DDLRAQIKAI KTNPEIPLSP HIFDPMQRHV EVTIRDNIYP TFLCSEMYIL YIQQMSAQQE
RCTSSGATGS GSAGSSGSGG SSLAGACALP PTTASGKQQL PQLVPPGAFI NLPVSSVSGP
PAGTCSASGS VYGPSTSASS SGSISATDTL PRSSTLPTLH EDSVLSLCDD FEKVQMQEGG
GSLGSGSVGA GARAPDYPIR LTRDLLIATQ KRRLEIRPPG AHGYVYNPST TNTSYVPNSR
VDSERASVSS GGRTDSDTMS ISSCSMDGRP YIQRRHSSTE SKAIRQSAMA NKETNTFQVI
PRTQRLHSNE HRPLKEEELV SLLIPKLEEV KRKRDLEERA RERNPGAALL TNERSSASDR
AFAEAIREKF ALDEDNDQDI LDQHVSRVWK DQTPHRSPGT MSPCPPIPSR RRTATHDSGM
VSDGAMSLSG HSMKHSKSMP DHSSCSRKLT NKWPSMNTDS GISMFSADTV TKYKDASSRS
GSSTASKLEE AKRRLEDEPR RSRRYAQPPM QHLSQQPLAS FSSSSSGGSI SLPHQPPPLP
AKPPETIVVF SFCEEPVPYR IKIPGTQPTL RQFKDYLPRR GHFRFFFKTH CEDPDSPVIQ
EEIVNDSDIL PLFGDKAMGL VKPSD
