ID Q7TMI9_MOUSE Unreviewed; 435 AA. AC Q7TMI9; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 29-MAY-2024, entry version 96. DE RecName: Full=Axin-1 {ECO:0000256|ARBA:ARBA00013892}; DE AltName: Full=Axis inhibition protein 1 {ECO:0000256|ARBA:ARBA00032466}; DE Flags: Fragment; GN Name=Axin1 {ECO:0000313|EMBL:AAH55491.1, ECO:0000313|MGI:MGI:1096327}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH55491.1}; RN [1] {ECO:0000313|EMBL:AAH55491.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N {ECO:0000313|EMBL:AAH55491.1}; RC TISSUE=Mammary tumor. C3 {ECO:0000313|EMBL:AAH55491.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. CC Membrane {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; BC055491; AAH55491.1; -; mRNA. DR AlphaFoldDB; Q7TMI9; -. DR PeptideAtlas; Q7TMI9; -. DR AGR; MGI:1096327; -. DR MGI; MGI:1096327; Axin1. DR ChiTaRS; Axin1; mouse. DR GO; GO:0030877; C:beta-catenin destruction complex; IEA:TreeGrafter. 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:TreeGrafter. DR GO; GO:0070411; F:I-SMAD binding; IEA:TreeGrafter. DR GO; GO:0042802; F:identical protein binding; IEA:TreeGrafter. DR GO; GO:0060090; F:molecular adaptor activity; IEA:TreeGrafter. DR GO; GO:0019901; F:protein kinase binding; IEA:TreeGrafter. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:TreeGrafter. DR GO; GO:0048468; P:cell development; IEA:TreeGrafter. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:InterPro. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:TreeGrafter. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 2.40.240.130; -; 1. DR InterPro; IPR043581; Axin-like. DR InterPro; IPR014936; Axin_b-cat-bd. DR InterPro; IPR001158; DIX. DR InterPro; IPR038207; DIX_dom_sf. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR46102; AXIN; 1. DR PANTHER; PTHR46102:SF3; AXIN-1; 1. DR Pfam; PF08833; Axin_b-cat_bind; 1. DR Pfam; PF00778; DIX; 1. DR SMART; SM00021; DAX; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50841; DIX; 1. PE 2: Evidence at transcript level; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|PROSITE- KW ProRule:PRU00069}. FT DOMAIN 353..435 FT /note="DIX" FT /evidence="ECO:0000259|PROSITE:PS50841" FT REGION 20..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 137..232 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 250..276 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 321..350 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAH55491.1" SQ SEQUENCE 435 AA; 48456 MW; C8E468789A2A880C CRC64; IHRLEAVQRT REAEEKLEER LKRVRMEEEG EDGEMPSGPM ASHKLPSVPA WHHFPPRYVD MGCSGLRDAH EENPESILDE HVQRVMRTPG CQSPGPGHRS PDSGHVAKTA VLGGTASGHG KHVPKLGLKL DTAGLHHHRH VHHHVHHNSA RPKEQMEAEV ARRVQSSFSW GPETHGHAKP RSYSENAGTT LSAGDLAFGG KTSAPSKRNT KKAESGKNAN AEVPSTTEDA EKNQKIMQWI IEGEKEISRH RKAGHGSSGL RKQQAHESSR PLSIERPGAV HPWVSAQLRN SVQPSHLFIQ DPTMPPNPAP NPLTQLEEAR RRLEEEEKRA NKLPSKQRTK SQRKAGGGSA PPCDSIVVAY YFCGEPIPYR TLVRGRAVTL GQFKELLTKK GSYRYYFKKV SDEFDCGVVF EEVREDEAVL PVFEEKIIGK VEKVD //