ID TX1B3_MOUSE Reviewed; 124 AA. AC Q9DBG9; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 02-SEP-2026, entry version 169. DE RecName: Full=Tax1-binding protein 3; DE AltName: Full=Tax interaction protein 1; DE Short=TIP-1; GN Name=Tax1bp3 {ECO:0000312|MGI:MGI:1923531}; 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; RN [1] {ECO:0000312|EMBL:BAB23703.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB23703.1}, and NOD RC {ECO:0000312|EMBL:BAE41827.1}; RC TISSUE=Bone marrow {ECO:0000312|EMBL:BAE29879.1}, Heart RC {ECO:0000312|EMBL:BAE40411.1}, and Liver RC {ECO:0000312|EMBL:BAB23703.1}; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] {ECO:0000312|EMBL:AAH08166.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH94314.1}, and NMRI RC {ECO:0000312|EMBL:AAH08166.1}; RC TISSUE=Brain {ECO:0000312|EMBL:AAH94314.1}, and Mammary gland RC {ECO:0000312|EMBL:AAH08166.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; 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). RN [4] {ECO:0000305} RP FUNCTION, INTERACTION WITH CTNNB1, AND SUBCELLULAR LOCATION. RX PubMed=12874278; DOI=10.1074/jbc.m306324200; RA Kanamori M., Sandy P., Marzinotto S., Benetti R., Kai C., Hayashizaki Y., RA Schneider C., Suzuki H.; RT "The PDZ protein tax-interacting protein-1 inhibits beta-catenin RT transcriptional activity and growth of colorectal cancer cells."; RL J. Biol. Chem. 278:38758-38764(2003). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH CTNNB1, AND RP INTERACTION WITH CTNNB1. RX PubMed=18835279; DOI=10.1016/j.jmb.2008.09.034; RA Zhang J., Yan X., Shi C., Yang X., Guo Y., Tian C., Long J., Shen Y.; RT "Structural basis of beta-catenin recognition by Tax-interacting RT protein-1."; RL J. Mol. Biol. 384:255-263(2008). CC -!- FUNCTION: May regulate a number of protein-protein interactions by CC competing for PDZ domain binding sites. Binds CTNNB1 and may thereby CC act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A CC for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play CC a role in the Rho signaling pathway (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:12874278}. CC -!- SUBUNIT: Interacts (via its PDZ domain) with GLS2. Interacts (via its CC PDZ domain) with RTKN (via the C-terminal region); this interaction CC facilitates Rho-mediated activation of the FOS serum response element CC (SRE). Interacts (via PDZ domain) with ARHGEF16. Interacts (via PDZ CC domain) with KCNJ4 (via C-terminus). Competes with LIN7A for KCNJ4 CC binding (By similarity). Interacts (via its PDZ domain) with CTNNB1; CC this interaction inhibits the transcriptional activity of CTNNB1. CC Interacts with ADGRB2 (By similarity). {ECO:0000250|UniProtKB:O14907, CC ECO:0000269|PubMed:12874278, ECO:0000269|PubMed:18835279}. CC -!- INTERACTION: CC Q9DBG9; Q02248: Ctnnb1; NbExp=6; IntAct=EBI-1161647, EBI-397872; CC Q9DBG9; P35222: CTNNB1; Xeno; NbExp=3; IntAct=EBI-1161647, EBI-491549; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12874278}. Nucleus CC {ECO:0000269|PubMed:12874278}. Cell membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. CC Note=Recruited to the cell membrane by interaction with membrane CC proteins. {ECO:0000250}. 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; AK004963; BAB23703.1; -; mRNA. DR EMBL; AK150816; BAE29879.1; -; mRNA. DR EMBL; AK168533; BAE40411.1; -; mRNA. DR EMBL; AK170485; BAE41827.1; -; mRNA. DR EMBL; AL670399; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008166; AAH08166.1; -; mRNA. DR EMBL; BC094314; AAH94314.1; -; mRNA. DR CCDS; CCDS25000.1; -. DR RefSeq; NP_083840.1; NM_029564.2. DR PDB; 3DIW; X-ray; 2.10 A; A/B=1-124. DR PDB; 3DJ1; X-ray; 1.80 A; A/B=1-124. DR PDB; 3DJ3; X-ray; 2.40 A; A/B/C/D=1-112. DR AlphaFoldDB; Q9DBG9; -. DR BMRB; Q9DBG9; -. DR SMR; Q9DBG9; -. DR BioGRID; 218059; 5. DR ELM; Q9DBG9; -. DR FunCoup; Q9DBG9; 3049. DR IntAct; Q9DBG9; 4. DR STRING; 10090.ENSMUSP00000047410; -. DR GlyGen; Q9DBG9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9DBG9; -. DR PhosphoSitePlus; Q9DBG9; -. DR PaxDb; 10090-ENSMUSP00000047410; -. DR PeptideAtlas; Q9DBG9; -. DR ProteomicsDB; 298070; -. DR Pumba; Q9DBG9; -. DR Antibodypedia; 23095; 141 antibodies from 29 providers. DR DNASU; 76281; -. DR Ensembl; ENSMUST00000040687.12; ENSMUSP00000047410.6; ENSMUSG00000040158.13. DR GeneID; 76281; -. DR KEGG; mmu:76281; -. DR UCSC; uc007kac.1; mouse. DR AGR; MGI:1923531; -. DR CTD; 30851; -. DR MGI; MGI:1923531; Tax1bp3. DR VEuPathDB; HostDB:ENSMUSG00000040158; -. DR eggNOG; KOG3553; Eukaryota. DR GeneTree; ENSGT00390000002877; -. DR HOGENOM; CLU_130477_0_0_1; -. DR InParanoid; Q9DBG9; -. DR OMA; NDFTMVT; -. DR OrthoDB; 10033291at2759; -. DR PhylomeDB; Q9DBG9; -. DR BioGRID-ORCS; 76281; 3 hits in 76 CRISPR screens. DR EvolutionaryTrace; Q9DBG9; -. DR PRO; PR:Q9DBG9; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q9DBG9; protein. DR Bgee; ENSMUSG00000040158; Expressed in ileum and 65 other cell types or tissues. DR ExpressionAtlas; Q9DBG9; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; ISO:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0001650; C:fibrillar center; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008013; F:beta-catenin binding; IPI:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI. DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; ISS:UniProtKB. DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:GO_Central. DR GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB. DR CDD; cd10822; PDZ_TAX1BP3-like; 1. DR FunFam; 2.30.42.10:FF:000121; Tax1-binding protein 3; 1. DR Gene3D; 2.30.42.10; -; 1. DR IDEAL; IID50015; -. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR050614; Synaptic_Scaffolding_LAP-MAGUK. DR InterPro; IPR017268; Tax1-binding_p3. DR PANTHER; PTHR23119; DISCS LARGE; 1. DR PANTHER; PTHR23119:SF50; PDZ DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00595; PDZ; 1. DR PIRSF; PIRSF037712; Tax1-binding_p3; 1. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR PROSITE; PS50106; PDZ; 1. DR PDBsum; 3DIW; -. DR PDBsum; 3DJ1; -. DR PDBsum; 3DJ3; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell membrane; Cytoplasm; Membrane; Nucleus; KW Phosphoprotein; Reference proteome; Wnt signaling pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:O14907" FT CHAIN 2..124 FT /note="Tax1-binding protein 3" FT /id="PRO_0000233944" FT DOMAIN 15..112 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:O14907" FT MOD_RES 61 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O14907" FT STRAND 14..19 FT /evidence="ECO:0007829|PDB:3DJ1" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:3DJ1" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:3DJ1" FT STRAND 30..35 FT /evidence="ECO:0007829|PDB:3DJ1" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:3DJ1" FT STRAND 48..51 FT /evidence="ECO:0007829|PDB:3DJ3" FT STRAND 55..60 FT /evidence="ECO:0007829|PDB:3DJ1" FT HELIX 65..69 FT /evidence="ECO:0007829|PDB:3DJ1" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:3DJ1" FT HELIX 90..97 FT /evidence="ECO:0007829|PDB:3DJ1" FT STRAND 103..110 FT /evidence="ECO:0007829|PDB:3DJ1" FT HELIX 112..115 FT /evidence="ECO:0007829|PDB:3DJ1" FT HELIX 116..122 FT /evidence="ECO:0007829|PDB:3DJ1" SQ SEQUENCE 124 AA; 13723 MW; F3FBD0F475F69FCD CRC64; MSYTPGQPVT AVVQRVEIHK LRQGENLILG FSIGGGIDQD PSQNPFSEDK TDKGIYVTRV SEGGPAEIAG LQIGDKIMQV NGWDMTMVTH DQARKRLTKR SEEVVRLLVT RQSLQKAVQQ SMLS //