1433T_RAT
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 03-AUG-2022, entry version 149.
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}.
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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; 10.
DR DIP; DIP-947N; -.
DR IntAct; P68255; 8.
DR MINT; P68255; -.
DR STRING; 10116.ENSRNOP00000011501; -.
DR iPTMnet; P68255; -.
DR PhosphoSitePlus; P68255; -.
DR jPOST; P68255; -.
DR PaxDb; P68255; -.
DR PRIDE; P68255; -.
DR Ensembl; ENSRNOT00000115392; ENSRNOP00000077932; ENSRNOG00000051650.
DR GeneID; 25577; -.
DR KEGG; rno:25577; -.
DR CTD; 10971; -.
DR RGD; 3979; Ywhaq.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; P68255; -.
DR OMA; FEMATTI; -.
DR OrthoDB; 1176818at2759; -.
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 tissues.
DR Genevisible; P68255; RN.
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:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0034766; P:negative regulation of ion transmembrane transport; IMP:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
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; -; 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; PTHR18860; 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; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
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
