ID B1MT45_PLEMO Unreviewed; 867 AA. AC B1MT45; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 59. 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:ACA51082.1}; OS Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; OC Pitheciidae; Callicebinae; Plecturocebus. OX NCBI_TaxID=9523 {ECO:0000313|EMBL:ACA51082.1}; RN [1] {ECO:0000313|EMBL:ACA51082.1} 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 (MAR-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; DP000617; ACA51082.1; -; Genomic_DNA. DR AlphaFoldDB; B1MT45; -. 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..81 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 215..239 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 251..289 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 412..435 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 480..500 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 531..629 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 646..672 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 215..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 654..668 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 867 AA; 96062 MW; D9044402B379180E CRC64; MNVQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDPRPA SYSFCSGKGI GLKGETSTAT PRRSDLDLGY EPEGSASPTP PHLKWAESLH SLLDDQDGIS LFRTFLKQEG CADLLDFWFA CTGFRKLEPC DSNEEKRLKL ARAIYRKYIL DNNGIVSRQT KPATKSFIKG CIMKQLIDPA MFDQAQTEIQ ATMEENTYPS FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGISGYLPT LNEDEEWKCD QDVDEDDGRD TAPPGRLPQK LLLETAAPRA SSSRRYSEGR EFRYGSWREP VNPYYVNAGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK QHRREMQESV QVNGRVPLPH IPRTYRMPKE VRVEPQKFAE ELIHRLEAVQ RTREAEEKLE ERLKRVRMEE EGEDGDSSSG PPGPCHKLPL TATWYHFPPR CVDVGCAGLR DAHEENPESI LDEHVQRVLR TPGRQSPGPG HRSPDSGHVA KMPVVLGGAA SGHGKHAPKS GAKLDAAGLH HHRHVHHHVH HGIARPKEQV EAEAARRAQS SFAWGPEQHI HGAKPRGYSE SVGAAPNTSD GLGHSGKVGM ACKRNAKKAE SGKNASTEMQ GAPEDAEKNQ KIMQWIIEGE KEISRHRRAG HGSSGTRKPQ SHENSRPLSL ERSGAVHPWA GPQLRTSVQP SHLFIQDPTM PPHPAPNPLT QLEEARRRLE EEEKRASRAP SKQRYVQEVM RRGRACVRPA CAPVLRVVPA VSDMELSETE ARSQRKAGGG SAQACDSIVV AYYFCGEPIP YRTLVRGRAV TLGQFKELLT KKGSYRYYFK KVSDEFDCGV VFEEVREDGA VLPVFEEKII GKVEKVD //