Dbfetch
ID 1433T_RAT Reviewed; 245 AA. AC P68255; P35216; DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=14-3-3 protein theta; DE AltName: Full=14-3-3 protein tau; GN Name=Ywhaq; 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 [MRNA]. RC STRAIN=Wistar; TISSUE=Brain; RX PubMed=7984035; DOI=10.1016/0169-328x(94)90285-2; RA Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H., RA Inoue Y.; RT "Molecular cloning of rat cDNAs for the zeta and theta subtypes of 14-3-3 RT protein and differential distributions of their mRNAs in the brain."; RL Brain Res. Mol. Brain Res. 25:113-121(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; 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 [3] RP PROTEIN SEQUENCE OF 4-9; 12-18; 28-49; 61-68; 84-115; 128-157; 159-167 AND RP 194-222, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathways. Binds to a CC large number of partners, usually by recognition of a phosphoserine or CC phosphothreonine motif. Binding generally results in the modulation of CC the activity of the binding partner. Negatively regulates the kinase CC activity of PDPK1 (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer. Interacts with CDK16 (By similarity). Interacts CC with RGS7 (phosphorylated form). Interacts with SSH1. Interacts with CC CDKN1B ('Thr-198' phosphorylated form); the interaction translocates CC CDKN1B to the cytoplasm. Interacts with GAB2. Interacts with the 'Ser- CC 241' phosphorylated form of PDPK1. Interacts with the 'Thr-369' CC phosphorylated form of DAPK2 (By similarity). Interacts with PI4KB, CC TBC1D22A and TBC1D22B (By similarity). Interacts with SLITRK1 (By CC similarity). Interacts with RIPOR2 (By similarity). Interacts with CC INAVA; the interaction increases upon PRR (pattern recognition CC receptor) stimulation and is required for cellular signaling pathway CC activation and cytokine secretion (By similarity). Interacts with CC MARK2, MARK3 and MARK4 (By similarity). Interacts with MEFV (By CC similarity). {ECO:0000250|UniProtKB:P27348, CC ECO:0000250|UniProtKB:P68254}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. 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; D17614; BAA04533.1; -; mRNA. DR EMBL; BC062409; AAH62409.1; -; mRNA. DR PIR; I52647; S59927. DR RefSeq; NP_037185.1; NM_013053.1. DR AlphaFoldDB; P68255; -. DR SMR; P68255; -. DR BioGRID; 247608; 14. DR DIP; DIP-947N; -. DR IntAct; P68255; 8. DR MINT; P68255; -. DR STRING; 10116.ENSRNOP00000072011; -. DR GlyGen; P68255; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P68255; -. DR PhosphoSitePlus; P68255; -. DR jPOST; P68255; -. DR PaxDb; 10116-ENSRNOP00000011501; -. DR Ensembl; ENSRNOT00000115392.1; ENSRNOP00000077932.1; ENSRNOG00000051650.2. DR Ensembl; ENSRNOT00055009259; ENSRNOP00055007100; ENSRNOG00055005734. DR Ensembl; ENSRNOT00060014863; ENSRNOP00060011509; ENSRNOG00060008854. DR Ensembl; ENSRNOT00065016571; ENSRNOP00065012614; ENSRNOG00065010266. DR GeneID; 25577; -. DR KEGG; rno:25577; -. DR AGR; RGD:3979; -. DR CTD; 10971; -. DR RGD; 3979; Ywhaq. DR eggNOG; KOG0841; Eukaryota. DR GeneTree; ENSGT01090000260040; -. DR HOGENOM; CLU_058290_1_0_1; -. DR InParanoid; P68255; -. DR OMA; NPKRACE; -. DR OrthoDB; 920089at2759; -. DR PhylomeDB; P68255; -. DR TreeFam; TF102002; -. DR Reactome; R-RNO-111447; Activation of BAD and translocation to mitochondria. DR Reactome; R-RNO-5625740; RHO GTPases activate PKNs. DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-RNO-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex. DR Reactome; R-RNO-9614399; Regulation of localization of FOXO transcription factors. DR PRO; PR:P68255; -. DR Proteomes; UP000002494; Chromosome 6. DR Bgee; ENSRNOG00000051650; Expressed in cerebellum and 20 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:0045202; C:synapse; IDA:SynGO. DR GO; GO:0071889; F:14-3-3 protein binding; IPI:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:0034766; P:negative regulation of monoatomic ion transmembrane transport; IMP:RGD. DR GO; GO:0006605; P:protein targeting; ISO:RGD. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:RGD. DR CDD; cd10023; 14-3-3_theta; 1. DR Gene3D; 1.20.190.20; 14-3-3 domain; 1. DR InterPro; IPR000308; 14-3-3. DR InterPro; IPR023409; 14-3-3_CS. DR InterPro; IPR036815; 14-3-3_dom_sf. DR InterPro; IPR023410; 14-3-3_domain. DR InterPro; IPR042584; 14-3-3_theta. DR PANTHER; PTHR18860; 14-3-3 PROTEIN; 1. DR PANTHER; PTHR18860:SF3; 14-3-3 PROTEIN THETA; 1. DR Pfam; PF00244; 14-3-3; 1. DR PIRSF; PIRSF000868; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR SMART; SM00101; 14_3_3; 1. DR SUPFAM; SSF48445; 14-3-3 protein; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. DR Genevisible; P68255; RN. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond; KW Nitration; Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..245 FT /note="14-3-3 protein theta" FT /id="PRO_0000058640" FT SITE 56 FT /note="Interaction with phosphoserine on interacting FT protein" FT /evidence="ECO:0000250" FT SITE 127 FT /note="Interaction with phosphoserine on interacting FT protein" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P27348" FT MOD_RES 3 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P27348" FT MOD_RES 49 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P27348" FT MOD_RES 68 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P27348" FT MOD_RES 82 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9CQV8" FT MOD_RES 92 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P68254" FT MOD_RES 104 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9CQV8" FT MOD_RES 115 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P27348" FT MOD_RES 232 FT /note="Phosphoserine; by CK1" FT /evidence="ECO:0000250|UniProtKB:P27348, ECO:0000305" FT CROSSLNK 49 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P27348" SQ SEQUENCE 245 AA; 27778 MW; E30471260E8B366E CRC64; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIENSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN //