ID   TX1B3_RAT               Reviewed;          98 AA.
AC   Q4QQV1;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Tax1-binding protein 3;
GN   Name=Tax1bp3 {ECO:0000312|EMBL:AAH97976.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=16855024; DOI=10.1091/mbc.e06-02-0129;
RA   Alewine C., Olsen O., Wade J.B., Welling P.A.;
RT   "TIP-1 has PDZ scaffold antagonist activity.";
RL   Mol. Biol. Cell 17:4200-4211(2006).
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   -!- 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 (By
CC       similarity). Interacts with ADGRB2. {ECO:0000250|UniProtKB:O14907,
CC       ECO:0000250|UniProtKB:Q9DBG9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Note=Recruited to the cell membrane by
CC       interaction with membrane proteins. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in kidney distal convoluted tubules (at
CC       protein level). {ECO:0000269|PubMed:16855024}.
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DR   EMBL; BC097976; AAH97976.1; -; mRNA.
DR   RefSeq; NP_001020590.1; NM_001025419.1.
DR   AlphaFoldDB; Q4QQV1; -.
DR   SMR; Q4QQV1; -.
DR   STRING; 10116.ENSRNOP00000053298; -.
DR   PaxDb; Q4QQV1; -.
DR   GeneID; 360564; -.
DR   KEGG; rno:360564; -.
DR   CTD; 30851; -.
DR   RGD; 1308924; Tax1bp3.
DR   VEuPathDB; HostDB:ENSRNOG00000019357; -.
DR   eggNOG; KOG3553; Eukaryota.
DR   HOGENOM; CLU_130477_1_0_1; -.
DR   InParanoid; Q4QQV1; -.
DR   OMA; LHMLVAR; -.
DR   Reactome; R-RNO-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR   ChiTaRS; Tax1bp3; rat.
DR   PRO; PR:Q4QQV1; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000019357; Expressed in jejunum and 19 other tissues.
DR   ExpressionAtlas; Q4QQV1; baseline and differential.
DR   Genevisible; Q4QQV1; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR   GO; GO:0090630; P:activation of GTPase activity; ISO:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
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; ISS: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; -; 2.
DR   InterPro; IPR036034; PDZ_sf.
DR   SUPFAM; SSF50156; SSF50156; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Cytoplasm; Membrane; Nucleus;
KW   Reference proteome; Wnt signaling pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O14907"
FT   CHAIN           2..98
FT                   /note="Tax1-binding protein 3"
FT                   /id="PRO_0000233945"
FT   DOMAIN          12..87
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14907"
SQ   SEQUENCE   98 AA;  11050 MW;  C58A4ECC5F0E1EC1 CRC64;
     MSYIPGQPVT AVVQRVEIHK LRQGENLILG FSIGGGIDQD PSQNPFSEDK TDKVNGWDMT
     MVTHDQARKR LTKRSEEVVR LLVTRQSLQK AVQQSMLS