1433F_RAT
ID 1433F_RAT Reviewed; 246 AA.
AC P68511; P11576; P70198;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=14-3-3 protein eta;
GN Name=Ywhah;
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].
RX PubMed=1649368; DOI=10.1016/0169-328x(91)90105-7;
RA Watanabe M., Isobe T., Okuyama T., Ichimura T., Kuwano R., Takahashi Y.,
RA Kondo H.;
RT "Molecular cloning of cDNA to rat 14-3-3 eta chain polypeptide and the
RT neuronal expression of the mRNA in the central nervous system.";
RL Brain Res. Mol. Brain Res. 10:151-158(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 13-56; 62-69; 111-120; 126-132; 144-155; 163-172 AND
RP 197-227, 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 (By similarity). Interacts with many nuclear hormone
CC receptors and cofactors including AR, ESR1, ESR2, MC2R, NR3C1, NRIP1,
CC PPARBP and THRA. Interacts with ABL1 (phosphorylated form); the
CC interaction retains it in the cytoplasm. Weakly interacts with CDKN1B.
CC Interacts with ARHGEF28 and CDK16. Interacts with GAB2 (By similarity).
CC Interacts with KCNK18 in a phosphorylation-dependent manner. Interacts
CC with SAMSN1 (By similarity). Interacts with the 'Ser-241'
CC phosphorylated form of PDPK1 (By similarity). Interacts with the 'Thr-
CC 369' phosphorylated form of DAPK2 (By similarity). Interacts with
CC PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with SLITRK1
CC (By similarity). Interacts with MEFV (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P68510, ECO:0000250|UniProtKB:Q04917}.
CC -!- INTERACTION:
CC P68511; Q3MUI1: Numb; NbExp=3; IntAct=EBI-444647, EBI-7007865;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated on Ser-59 by protein kinase C delta type catalytic
CC subunit in a sphingosine-dependent fashion. {ECO:0000250}.
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; D17445; BAA04259.1; -; mRNA.
DR EMBL; BC081825; AAH81825.1; -; mRNA.
DR PIR; A60031; A60031.
DR RefSeq; NP_037184.1; NM_013052.1.
DR AlphaFoldDB; P68511; -.
DR SMR; P68511; -.
DR BioGRID; 247607; 5.
DR DIP; DIP-299N; -.
DR IntAct; P68511; 8.
DR MINT; P68511; -.
DR STRING; 10116.ENSRNOP00000024388; -.
DR iPTMnet; P68511; -.
DR PhosphoSitePlus; P68511; -.
DR jPOST; P68511; -.
DR PaxDb; P68511; -.
DR PRIDE; P68511; -.
DR Ensembl; ENSRNOT00000085735; ENSRNOP00000075701; ENSRNOG00000055471.
DR GeneID; 25576; -.
DR KEGG; rno:25576; -.
DR UCSC; RGD:3978; rat.
DR CTD; 7533; -.
DR RGD; 3978; Ywhah.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; P68511; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P68511; -.
DR TreeFam; TF102003; -.
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 PRO; PR:P68511; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000055471; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; P68511; baseline and differential.
DR Genevisible; P68511; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0017080; F:sodium channel regulator activity; ISS:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0006713; P:glucocorticoid catabolic process; ISO:RGD.
DR GO; GO:0042921; P:glucocorticoid receptor signaling pathway; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR GO; GO:0086010; P:membrane depolarization during action potential; ISS:BHF-UCL.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; ISS:BHF-UCL.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 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; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q04917"
FT CHAIN 2..246
FT /note="14-3-3 protein eta"
FT /id="PRO_0000058625"
FT SITE 57
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 132
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q04917"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04917"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68510"
SQ SEQUENCE 246 AA; 28212 MW; C12F62B4ABA76DA3 CRC64;
MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW
RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LALLDKFLIK NCNDFQYESK
VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEHMQPTHP IRLGLALNFS
VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE
EAGEGN
