ID AXIN1_CHICK Reviewed; 841 AA.
AC O42400;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 24-JAN-2024, entry version 148.
DE RecName: Full=Axin-1;
DE AltName: Full=Axis inhibition protein 1;
GN Name=AXIN1; Synonyms=AXIN, AXN;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=9230313; DOI=10.1016/s0092-8674(00)80324-4;
RA Zeng L., Fagotto F., Zhang T., Hsu W., Vasicek T.J., Perry W.L. III,
RA Lee J.J., Tilghman S.M., Gumbiner B.M., Costantini F.;
RT "The mouse Fused locus encodes Axin, an inhibitor of the Wnt signaling
RT pathway that regulates embryonic axis formation.";
RL Cell 90:181-192(1997).
CC -!- FUNCTION: Component of the beta-catenin destruction complex required
CC for regulating CTNNB1 levels through phosphorylation and
CC ubiquitination, and modulating Wnt-signaling. Controls dorsoventral
CC patterning via two opposing effects; down-regulates CTNNB1 to inhibit
CC the Wnt signaling pathway and ventralize embryos, but also dorsalizes
CC embryos by activating a Wnt-independent JNK signaling pathway.
CC {ECO:0000250|UniProtKB:O15169}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O35625}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15169}. Nucleus
CC {ECO:0000250|UniProtKB:O15169}. Membrane
CC {ECO:0000250|UniProtKB:O35625}. Cell membrane
CC {ECO:0000250|UniProtKB:O35625}.
CC -!- DEVELOPMENTAL STAGE: Expressed at stage 12 to 15.
CC {ECO:0000269|PubMed:9230313}.
CC -!- PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated
CC protein is recognized by RNF146, followed by ubiquitination at 'Lys-48'
CC and subsequent activation of the Wnt signaling pathway.
CC {ECO:0000250|UniProtKB:O15169}.
CC -!- PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its
CC degradation and subsequent activation of the Wnt signaling pathway.
CC {ECO:0000250|UniProtKB:O15169}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF009012; AAC60245.1; -; mRNA.
DR RefSeq; NP_990275.1; NM_204944.2.
DR AlphaFoldDB; O42400; -.
DR SMR; O42400; -.
DR ELM; O42400; -.
DR STRING; 9031.ENSGALP00000074022; -.
DR PaxDb; 9031-ENSGALP00000041347; -.
DR GeneID; 395786; -.
DR KEGG; gga:395786; -.
DR CTD; 8312; -.
DR VEuPathDB; HostDB:geneid_395786; -.
DR eggNOG; KOG3589; Eukaryota.
DR InParanoid; O42400; -.
DR PhylomeDB; O42400; -.
DR PRO; PR:O42400; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0030877; C:beta-catenin destruction complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; ISS:AgBase.
DR GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
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:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd11582; Axin_TNKS_binding; 1.
DR CDD; cd08707; RGS_Axin; 1.
DR Gene3D; 1.10.196.10; -; 2.
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; IPR032101; Axin_TNKS-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:SF3; AXIN-1; 1.
DR Pfam; PF16646; AXIN1_TNKS_BD; 1.
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; Regulator of G-protein signaling, RGS; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50132; RGS; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Cell membrane; Cytoplasm; Developmental protein;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Wnt signaling pathway.
FT CHAIN 1..841
FT /note="Axin-1"
FT /id="PRO_0000220891"
FT DOMAIN 88..211
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 759..841
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..433
FT /note="Interaction with GSK3B"
FT /evidence="ECO:0000250"
FT REGION 434..508
FT /note="Interaction with beta-catenin"
FT /evidence="ECO:0000250"
FT REGION 482..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 94932 MW; 400D0C90E72506FE CRC64;
MNIQGKGFPL DLGRSFTEDA PRPPVPGEEG ELVSTDPRPV SHGFYSSKSD AVRNETSTAT
PRRSDLDLGY EPEGSASPTP PYLKWAESLH SLLDDQDGIN LFRTFLKQED CADLLDFWFA
CSGFRKLEPC VSNEEKRLKL AKAIYKKYIL DNNGIVSRQI KPATKSFIKD CVMKLQIDPD
MFDQAQTEIQ CMIEDNTYPL FLKSDIYLEY TRTGGESPKI YSDPSSGSGT GKGLPGYLPT
LNEDEEWKCD QDTEPEASRD SAPSSRLTQK LLLETATQRA TSTRRYSEGR EFRHGSWREP
VNPYYVNTGY AMAPATSAND SEQQSMSSDA DTMSLTDSSI DGIPPYRLRK QHRREMQESA
KANGRVPLPH IPRTYRMPKD IHVEPEKFAA ELINRLEEVQ KEREAEEKLE ERLKRVRAEE
EGEDADISSG PSVISHKMPS AQPFHHFAPR YSEMGCAGMQ MRDAHEENPE SILDEHVQRV
MKTPGCQSPG PGRHSPKPRS PESGHLGKLS GTLGTIPPGH GKHTTKSGMK LDAANLYHHK
HVYHHIHHHS MMKPKEQIEA EATQRVQNSF AWNVDSHNYA TKSRNYSENL GMAPVPMDSL
GYSGKASLLS KRNIKKTDSG KSDGANYEMP GSPEDVERNQ KILQWIIEGE KEISRHKKTN
HGSSGVKKQL SHDMVRPLSI ERPVAVHPWV SAQLRNVVQP SHPFIQDPTM PPNPAPNPLT
QLEEARRRLE EEEKRAGKLP LKQRLKPQKR PGSGASQPCE NIVVAYYFCG EPIPYRTLVK
GRVVTLGQFK ELLTKKGNYR YYFKKVSDEF DCGVVFEEVR EDDTILPIFE EKIIGKVEKI
D
//
