TX1B3_MOUSE
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 03-AUG-2022, entry version 150.
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
RC NOD {ECO:0000312|EMBL:BAE41827.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:BAE29879.1},
RC Heart {ECO:0000312|EMBL:BAE40411.1}, and
RC Liver {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
RC NMRI {ECO:0000312|EMBL:AAH08166.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH94314.1}, and
RC Mammary gland {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, Pancreas,
RC 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 protein-
RT 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}.
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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 PDBsum; 3DIW; -.
DR PDBsum; 3DJ1; -.
DR PDBsum; 3DJ3; -.
DR AlphaFoldDB; Q9DBG9; -.
DR BMRB; Q9DBG9; -.
DR SMR; Q9DBG9; -.
DR BioGRID; 218059; 4.
DR ELM; Q9DBG9; -.
DR IntAct; Q9DBG9; 4.
DR STRING; 10090.ENSMUSP00000047410; -.
DR iPTMnet; Q9DBG9; -.
DR PhosphoSitePlus; Q9DBG9; -.
DR EPD; Q9DBG9; -.
DR MaxQB; Q9DBG9; -.
DR PaxDb; Q9DBG9; -.
DR PeptideAtlas; Q9DBG9; -.
DR PRIDE; Q9DBG9; -.
DR ProteomicsDB; 298070; -.
DR Antibodypedia; 23095; 133 antibodies from 26 providers.
DR DNASU; 76281; -.
DR Ensembl; ENSMUST00000040687; ENSMUSP00000047410; ENSMUSG00000040158.
DR GeneID; 76281; -.
DR KEGG; mmu:76281; -.
DR UCSC; uc007kac.1; mouse.
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; LHMLVAR; -.
DR OrthoDB; 1471323at2759; -.
DR PhylomeDB; Q9DBG9; -.
DR TreeFam; TF318964; -.
DR Reactome; R-MMU-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR BioGRID-ORCS; 76281; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Tax1bp3; mouse.
DR EvolutionaryTrace; Q9DBG9; -.
DR PRO; PR:Q9DBG9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9DBG9; protein.
DR Bgee; ENSMUSG00000040158; Expressed in ileum and 62 other tissues.
DR ExpressionAtlas; Q9DBG9; baseline and differential.
DR Genevisible; Q9DBG9; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISO: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:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR IDEAL; IID50015; -.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR017268; Tax1-binding_p3.
DR Pfam; PF00595; PDZ; 1.
DR PIRSF; PIRSF037712; Tax1-binding_p3; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
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
