ID   AXNR_XENLA              Reviewed;         706 AA.
AC   Q9PTP2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Axin-related protein;
DE            Short=xARP;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAF22574.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH AXIN1 AND DVL2,
RP   IDENTIFICATION IN A COMPLEX WITH CTNNB1 AND GSK3B, SUBCELLULAR LOCATION,
RP   AND DEVELOPMENTAL STAGE.
RC   TISSUE=Ovary {ECO:0000312|EMBL:AAF22574.1};
RX   PubMed=10688669; DOI=10.1128/mcb.20.6.2228-2238.2000;
RA   Itoh K., Antipova A., Ratcliffe M.J., Sokol S.Y.;
RT   "Interaction of dishevelled and Xenopus axin-related protein is required
RT   for wnt signal transduction.";
RL   Mol. Cell. Biol. 20:2228-2238(2000).
CC   -!- FUNCTION: Regulates the wnt signaling pathway by interacting with
CC       dvl2/dsh, which displaces gsk3b from the axnr-gsk3b complex and thus
CC       prevents degradation of ctnnb1/beta-catenin.
CC       {ECO:0000269|PubMed:10688669}.
CC   -!- SUBUNIT: Interacts with dvl2/dsh via DIX domains in both proteins.
CC       Forms a complex with ctnnb1/beta-catenin and gsk3b. Also forms
CC       heterodimers with mouse Axin1. {ECO:0000269|PubMed:10688669}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10688669}.
CC       Cytoplasmic vesicle {ECO:0000269|PubMed:10688669}.
CC   -!- DEVELOPMENTAL STAGE: Expressed maternally.
CC       {ECO:0000269|PubMed:10688669}.
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DR   EMBL; AF140243; AAF22574.1; -; mRNA.
DR   RefSeq; NP_001079086.1; NM_001085617.1.
DR   AlphaFoldDB; Q9PTP2; -.
DR   SMR; Q9PTP2; -.
DR   PRIDE; Q9PTP2; -.
DR   GeneID; 373619; -.
DR   KEGG; xla:373619; -.
DR   CTD; 373619; -.
DR   Xenbase; XB-GENE-6252887; axin2.L.
DR   OrthoDB; 1481971at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 373619; Expressed in gastrula and 18 other tissues.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:InterPro.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; IPI:UniProtKB.
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; 2.
DR   Pfam; PF08833; Axin_b-cat_bind; 1.
DR   Pfam; PF00778; DIX; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
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; Cytoplasmic vesicle; Developmental protein; Reference proteome;
KW   Wnt signaling pathway.
FT   CHAIN           1..706
FT                   /note="Axin-related protein"
FT                   /id="PRO_0000286587"
FT   DOMAIN          72..191
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   DOMAIN          624..706
FT                   /note="DIX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT   REGION          278..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   706 AA;  79196 MW;  C3D0AF0D9540F162 CRC64;
     MSSAGVLTCI PDSGPIFRET SLRPPVPGQE TNNFKPEKFT MDSQHLKHKE DFNREAEGCV
     AHDSRFSRWG RSLNLLLDDQ DGATLFRMYL EGEGLGDLLT FWFACNGFRA MDPLEPKTSK
     TAKAIYRWYV QNSSAVSGRL KPTTRTQVKE CVKNHQLNKT VFDQAQQEIQ RAMEQEAFTS
     FLQSDICKEY ARGVEDSPTP ESPGPGLPTL TEDEEFGGLH HFSSGMGKIN RAFSRIPPRN
     QRSHFRKLEQ TYQYFAPAAS INDSEISSDA LTEDSMSMTD GSVDGIPPYR SKKQREIHRS
     VSANGKVSLP FVPRTMRPPA EMMPTSPAEF AAKLTIALEK VKKQRDAEEK LEEKLQRLKE
     EEEIADYDIP SSSHETVPGA ALEDDPQSIL DDHVSRVLKT PANLSPRSQS PFVQRKGKFQ
     PAFSKGQTST SCHLRPKVPQ GMEATSTLAS ELRSSVSSQL PRSSRKPEGC TQPHRPEEGT
     SAAVLTTPLS PEQEAERNHS VLQWVLDSAK LMKKHHRETA SVTPCPELKK ATHRAASQPA
     HLFLQDTSMP PLTAPNTLDQ LEEARRRLVE DKRVPKLHKS RCVQSTTLKE KGKTAESVPS
     SGFSTLKLSE EQKTAKKPSS ECPGQGLAIV YYFCGERIPY MIRTKEPSLT LQEFKELLSK
     KGSNKYYFKK ESHEFECNAV FQEVSEEDAV LPLFEEKIIC KVERAC