ID   F6YNJ2_HORSE            Unreviewed;       862 AA.
AC   F6YNJ2;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 3.
DT   02-SEP-2026, entry version 93.
DE   RecName: Full=Axin-1 {ECO:0000256|ARBA:ARBA00013892};
DE   AltName: Full=Axis inhibition protein 1 {ECO:0000256|ARBA:ARBA00032466};
GN   Name=AXIN1 {ECO:0000313|Ensembl:ENSECAP00000021225.3,
GN   ECO:0000313|VGNC:VGNC:15716};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000021225.3, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000021225.3, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000021225.3,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000021225.3}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000021225.3};
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; F6YNJ2; -.
DR   Ensembl; ENSECAT00000025514.3; ENSECAP00000021225.3; ENSECAG00000023674.4.
DR   VGNC; VGNC:15716; AXIN1.
DR   GeneTree; ENSGT00940000156947; -.
DR   Proteomes; UP000002281; Chromosome 13.
DR   Bgee; ENSECAG00000023674; Expressed in retina and 23 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019899; F:enzyme binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:InterPro.
DR   CDD; cd11582; Axin_TNKS_binding; 1.
DR   CDD; cd08707; RGS_Axin; 1.
DR   FunFam; 1.10.167.10:FF:000003; Axin 1; 1.
DR   FunFam; 1.10.196.10:FF:000002; Axin 1; 1.
DR   FunFam; 2.40.240.130:FF:000002; Axin 1; 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   4: Predicted;
KW   ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW   Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|PROSITE-
KW   ProRule:PRU00069}.
FT   DOMAIN          119..242
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   DOMAIN          780..862
FT                   /note="DIX"
FT                   /evidence="ECO:0000259|PROSITE:PS50841"
FT   REGION          44..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          677..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          748..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..372
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..575
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..757
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   862 AA;  95688 MW;  66457CDFD6730474 CRC64;
     MLTKDRLIHF GAVSTDVLGC SPRCSLTQSP KMSVQEQGFP LDLGASFTED APRPPVPGEE
     GELVSTDPRP VSHSFCSGKG PGIKGETSTA TPRRSDLDLG YEPEGSASPT PPYLKWAESL
     HSLLDDQDGI NLFRTFLKQE DCADLLDFWF ACSGFRKLEP CDSNEEKRLK LAKAIYRKYI
     LDNNGIVSRQ TKPATKSFIK DCIMKQLIDP AMFDQAQTEI QSTMEENTYP SFLKSDIYLE
     YTRTGSESPK LCSDQSSGSG TGKGIPGYLP TLNEDEEWKC DQDVDEDDGR DPGPPGRLTQ
     KLLLETAAPR ASASRRYSEG REFRYGSWRE PVNPYYVNSG YALAPATSAN DSEQQSLSSD
     ADSLSLTDSS VDGVPPYRIR KQHRREMQES VQVNGRVPLP HIPRTYRMPK EIRVEPQKFA
     AELIHRLEAI QRTREAEEKL EERLKRVRME EEGEDGDVSC GPPGASHKLP SAPAWHHFPP
     RYADMGCTGL RDAHEENPES ILDEHVQRVM RTPGCQSPGP GHRSPDSVHV PKVPGVLGGI
     APGHGKHALK SGAKLDAAGL HLHRHSHHHG HHGLARPKEQ AEAEAARRVQ SSFSWALEQH
     GHTAKPRSHS ESVGAAHITS DGLTYSGKAG TTCKRNTKKA ESGKSMGAEA PGPSEDAEKN
     QKIMQWIIEG EKEISRHRKA GHGSSGTKKQ QGHESSRPLS IERPGAVHPW VSAQLRNSVQ
     PSHLFIQDPT MPPNPAPNPL TQLEEARRRL EEEEKRASKL PSKQRMKSQR KVGSSSTQPC
     DSIVVAYYFC GEPIPYRTLV RGRAVTLGQF KELLTKKGNY RYYFKKVSDE FDCGVVFEEV
     REDEAVLPVF EEKIIGKVEK VD
//