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   24-JAN-2024, entry version 185.
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   ComplexPortal; CPX-2417; Beta-catenin destruction complex, Apc2 variant.
DR   ComplexPortal; CPX-2418; Beta-catenin destruction complex, Apc variant.
DR   DIP; DIP-20929N; -.
DR   IntAct; Q9V407; 2.
DR   MINT; Q9V407; -.
DR   STRING; 7227.FBpp0084919; -.
DR   iPTMnet; Q9V407; -.
DR   PaxDb; 7227-FBpp0084919; -.
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   AGR; FB:FBgn0026597; -.
DR   CTD; 43565; -.
DR   FlyBase; FBgn0026597; Axn.
DR   VEuPathDB; VectorBase:FBgn0026597; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   InParanoid; Q9V407; -.
DR   OMA; YVYTAST; -.
DR   OrthoDB; 4256282at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; Q9V407; baseline and differential.
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:0030707; P:follicle cell of egg chamber development; 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:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR   GO; GO:1900117; P:regulation of execution phase of apoptosis; 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; 1.10.196.10; -; 1.
DR   Gene3D; 2.40.240.130; -; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 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; AXIN; 1.
DR   PANTHER; PTHR46102:SF2; AXIN; 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; Regulator of G-protein signaling, RGS; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50841; DIX; 1.
DR   PROSITE; PS50132; RGS; 1.
DR   Genevisible; Q9V407; DM.
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
//