ID B2KHW4_RHIFE Unreviewed; 867 AA. AC B2KHW4; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 55. 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|EMBL:ACC62122.1}; OS Rhinolophus ferrumequinum (Greater horseshoe bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae; OC Rhinolophinae; Rhinolophus. OX NCBI_TaxID=59479 {ECO:0000313|EMBL:ACC62122.1}; RN [1] {ECO:0000313|EMBL:ACC62122.1} RP NUCLEOTIDE SEQUENCE. RA Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C., RA Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M., RA Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N., RA Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B., RA Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R., RA Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C., RA Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C., RA Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K., RA Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J., RA Tsipouri V., Young A., Green E.D.; RT "NISC Comparative Sequencing Initiative."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane CC {ECO:0000256|ARBA:ARBA00004370}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. 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; DP000696; ACC62122.1; -; Genomic_DNA. DR AlphaFoldDB; B2KHW4; -. 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:UniProt. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:InterPro. 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 4: Predicted; KW ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}; KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|PROSITE- KW ProRule:PRU00069}. FT DOMAIN 88..211 FT /note="RGS" FT /evidence="ECO:0000259|PROSITE:PS50132" FT DOMAIN 785..867 FT /note="DIX" FT /evidence="ECO:0000259|PROSITE:PS50841" FT REGION 1..79 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 216..245 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 315..344 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 416..439 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 532..628 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 646..669 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 216..231 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 315..339 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 867 AA; 96285 MW; 491753CF6000DD9E CRC64; MNIQEQGFPL DLGTSFTEDA PRPPVPGEEG ELVSTDPRPV SHSFCSGKGV GIKGETSTAT PRRSDLDLGY EPEGSASPTP PYLKWAESLH SLLDDQDGIN LFRTFLKQED CADLLDFWFA CSGFRKLEPC DSNEEKRLKL AKAIYRKYIL DHNGIVSRQT KPATKSFIKD CIMKQLIDPA MFDQAQTEIQ STMEENTYPS FLKSDIYLEY TRTGSESPKL CSDQSSGSGT GKGVPGYLPT LNEDEEWKCD QDVDEDDGRD PAPPGRLTQK LLLETAAPRA SSSRRYSEGR EFRYGSWREP VNPYYVNSGY ALAPATSTND SEQQSLSSDA DSLSLTDSSV DGIPPYRIRK QHRREVQESV QVNGRVLLPH IPRTYRIPKE IRVEPQKFAA ELIHRLEAVQ RTREAEEKLE ERLKRVRMEE EGEEGDMSSA PPGTSHKLPS APAWHHFPPR YSDVGCSGLR DAHEENPESI LDEHVQRVMR TPGCQSPGPG HRSPDSAHMP KLSGVLGAAA LGHGKHVPKS GAKLEAVGLH VHRHSHHHSH HGVARPKEPA EAEAPRRTQS SFAWGVELHS HTGKPRSHLE SMGAAPNASD SLAHSGKAGT TSKRNAKKAE SGKSASAEVP GSSEDAEKNQ KIMQWIIEGE KEISRHRKAG HGSSGVKKQQ AHESSRPLSI ERPGAVHPWV SAQLRNSVQP SHLFIQDPTM PPNPAPNPLT QLEEARRRLE EEEKRASKVP SKQRYVQEVI QRGRSCVRPA CTPMLSVVPA VSDMELSETE MKSQRKAGGG STQTCDSIVV AYYFCGEPIP YRTLVRGRAV TLGQFKELLT KKGNYRYYFK KVSDEFDCGV VFEEVREDEA VLPVFEEKII GKVEKVD //