AXIN1_XENLA
ID AXIN1_XENLA Reviewed; 842 AA.
AC Q9YGY0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Axin-1;
DE AltName: Full=Axis inhibition protein 1;
DE Short=xAxin;
GN Name=axin1; Synonyms=axin, axn;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=10072781; DOI=10.1016/s0925-4773(98)00203-2;
RA Hedgepeth C.M., Deardorff M.A., Klein P.S.;
RT "Xenopus axin interacts with glycogen synthase kinase-3 beta and is
RT expressed in the anterior midbrain.";
RL Mech. Dev. 80:147-151(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 435-504 IN COMPLEX WITH HUMAN
RP BETA-CATENIN.
RX PubMed=14600025; DOI=10.1101/gad.1142603;
RA Xing Y., Clements W.K., Kimelman D., Xu W.;
RT "Crystal structure of a beta-catenin/axin complex suggests a mechanism for
RT the beta-catenin destruction complex.";
RL Genes Dev. 17:2753-2764(2003).
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 (By similarity). Interacts with hwa; leading to
CC promote the tankyrase-mediated degradation of axin1 (By similarity).
CC {ECO:0000250|UniProtKB:O35625, ECO:0000250|UniProtKB:P57094}.
CC -!- INTERACTION:
CC Q9YGY0; P70039: apc; NbExp=2; IntAct=EBI-1037449, EBI-8069633;
CC Q9YGY0; A0A0H5BJW1: wdr26.L; NbExp=3; IntAct=EBI-1037449, EBI-11786127;
CC Q9YGY0; P35222: CTNNB1; Xeno; NbExp=2; IntAct=EBI-1037449, EBI-491549;
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: Weakly and ubiquitously expressed throughout early
CC development, and highly expressed in the anterior mesencephalon
CC adjacent to the forebrain-midbrain boundary.
CC {ECO:0000269|PubMed:10072781}.
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}.
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DR EMBL; AF097313; AAC71036.1; -; mRNA.
DR RefSeq; NP_001081874.1; NM_001088405.1.
DR PDB; 1QZ7; X-ray; 2.20 A; B=435-504.
DR PDBsum; 1QZ7; -.
DR AlphaFoldDB; Q9YGY0; -.
DR SMR; Q9YGY0; -.
DR BioGRID; 99432; 1.
DR DIP; DIP-36387N; -.
DR ELM; Q9YGY0; -.
DR IntAct; Q9YGY0; 3.
DR MINT; Q9YGY0; -.
DR GeneID; 398097; -.
DR KEGG; xla:398097; -.
DR CTD; 398097; -.
DR Xenbase; XB-GENE-17339457; axin1.L.
DR OrthoDB; 1481971at2759; -.
DR EvolutionaryTrace; Q9YGY0; -.
DR PRO; PR:Q9YGY0; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR GO; GO:0030877; C:beta-catenin destruction complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008013; F:beta-catenin binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:InterPro.
DR GO; GO:2000054; P:negative regulation of Wnt signaling pathway involved in dorsal/ventral axis specification; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd11582; Axin_TNKS_binding; 1.
DR DisProt; DP00954; -.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 2.
DR Gene3D; 2.40.240.130; -; 1.
DR IDEAL; IID50017; -.
DR InterPro; IPR043581; Axin-like.
DR InterPro; IPR029797; AXIN1.
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; PTHR46102; 1.
DR PANTHER; PTHR46102:SF3; PTHR46102:SF3; 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; SSF48097; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Cell membrane; Cytoplasm;
KW Developmental protein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..842
FT /note="Axin-1"
FT /id="PRO_0000220892"
FT DOMAIN 88..211
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 760..842
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..344
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 414..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..508
FT /note="Interaction with beta-catenin"
FT REGION 482..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 471..480
FT /evidence="ECO:0007829|PDB:1QZ7"
SQ SEQUENCE 842 AA; 94460 MW; BDA152734C97191E CRC64;
MSVKGKGFPL DLGGSFTEDA PRPPVPGEEG ELITTDQRPF SHTYYSLKND GIKNETSTAT
PRRPDLDLGY EPEGSASPTP PYLKWAESLH SLLDDQDGIH LFRTFLQQEN CADLLDFWFA
CSGFRKLEPN DSKVEKRLKL AKAIYKKYVL DSNGIVSRQI KPATKSFIKD CVLRQQIDPA
MFDQAQMEIQ SMMEDNTYPV FLKSDIYLEY TTIGGESPKN YSDQSSGSGT GKGPSGYLPT
LNEDEEWRCD QGGEHERERE CIPSSLFSQK LALDSSSHCA GSNRRLSDGR EFRPGTWREP
VNPYYVNTGY AGAPVTSAND SEQQSMSSDA DTMSLTDSSV DGIPPYRLRK HYRREMQESA
NANGRGPLPH IPRTYHMPKD IHVDPEKFAA ELISRLEGVL RDREAEQKLE ERLKRVRAEE
EGDDGDVSSG PSVISHKLPS GPPMHHFNSR YSETGCVGMQ IRDAHEENPE SILDEHVQRV
MKTPGCQSPG TGRHSPKSRS PDGHLSKTLP GSLGTMQTGH GKHSSKSTAK VDSGNLHHHK
HVYHHVHHHG GVKPKEQIDG ESTQRVQTNF PWNVESHNYA TKSRNYAESM GMAPNPMDSL
AYSGKVSMLS KRNAKKADLG KSESASHEMP VVPEDSERHQ KILQWIMEGE KEIIRHKKSN
HSSSSAKKQP PTELARPLSI ERPGAVHPWV SAQLRNVVQP SHPFIQDPTM PPNPAPNPLT
QLVSKPGARL EEEEKKAAKM PQKQRLKPQK KNVSAPSQPC DNIVVAYYFC GEPIPYRTMV
KGRVVTLGQF KELLTKKGNY RYYFKKVSDE FDCGVVFEEV REDDMILPIY EEKIIGQVEK
ID
