ID 1433F_BOVIN Reviewed; 246 AA. AC P68509; P11576; P70198; Q3ZC14; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 04-NOV-2026, entry version 127. DE RecName: Full=14-3-3 protein eta; DE AltName: Full=Protein kinase C inhibitor protein 1; DE Short=KCIP-1; GN Name=YWHAH; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Cerebellum; RX PubMed=2902623; DOI=10.1073/pnas.85.19.7084; RA Ichimura T., Isobe T., Okuyama T., Takahashi N., Araki K., Kuwano R., RA Takahashi Y.; RT "Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a RT protein kinase-dependent activator of tyrosine and tryptophan RT hydroxylases."; RL Proc. Natl. Acad. Sci. U.S.A. 85:7084-7088(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Hypothalamus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP SIMILARITY TO KINASE INHIBITOR. RX PubMed=1970123; DOI=10.1038/344594a0; RA Aitken A., Ellis C.A., Harris A., Sellers L.A., Toker A.; RT "Kinase and neurotransmitters."; RL Nature 344:594-594(1990). RN [4] RP FUNCTION. RX PubMed=7931346; DOI=10.1046/j.1471-4159.1994.63051908.x; RA Tanji M., Horwitz R., Rosenfeld G., Waymire J.C.; RT "Activation of protein kinase C by purified bovine brain 14-3-3: comparison RT with tyrosine hydroxylase activation."; RL J. Neurochem. 63:1908-1916(1994). 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 ECO:0000269|PubMed:7931346}. 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 -!- 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; J03868; AAA30347.1; -; mRNA. DR EMBL; BC102982; AAI02983.1; -; mRNA. DR PIR; A40484; A40484. DR RefSeq; NP_776917.2; NM_174492.2. DR AlphaFoldDB; P68509; -. DR SMR; P68509; -. DR BioGRID; 159404; 1. DR FunCoup; P68509; 1390. DR IntAct; P68509; 2. DR STRING; 9913.ENSBTAP00000041575; -. DR PaxDb; 9913-ENSBTAP00000041575; -. DR PeptideAtlas; P68509; -. DR Ensembl; ENSBTAT00000044059.6; ENSBTAP00000041575.4; ENSBTAG00000031134.6. DR Ensembl; ENSBTAT00085061228; ENSBTAP00085039230; ENSBTAG00085039759. DR Ensembl; ENSBTAT00090083234; ENSBTAP00090047155; ENSBTAG00090039166. DR GeneID; 282126; -. DR KEGG; bta:282126; -. DR CTD; 7533; -. DR VEuPathDB; HostDB:ENSBTAG00000031134; -. DR VGNC; VGNC:97330; YWHAH. DR eggNOG; KOG0841; Eukaryota. DR GeneTree; ENSGT01090000260040; -. DR InParanoid; P68509; -. DR OMA; ARLXVTE; -. DR OrthoDB; 10260625at2759; -. DR Reactome; R-BTA-111447; Activation of BAD and translocation to mitochondria. DR Reactome; R-BTA-5625740; RHO GTPases activate PKNs. DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-BTA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex. DR Proteomes; UP000009136; Chromosome 17. DR Bgee; ENSBTAG00000031134; Expressed in occipital lobe and 107 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0003779; F:actin binding; IEA:Ensembl. DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IEA:Ensembl. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl. DR GO; GO:0017080; F:sodium channel regulator activity; IEA:Ensembl. DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl. DR GO; GO:0006713; P:glucocorticoid catabolic process; IEA:Ensembl. DR GO; GO:0008104; P:intracellular protein localization; IBA:GO_Central. DR GO; GO:0086010; P:membrane depolarization during action potential; IEA:Ensembl. DR GO; GO:0042921; P:nuclear receptor-mediated glucocorticoid signaling pathway; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0002028; P:regulation of sodium ion transport; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd10025; 14-3-3_eta; 1. DR FunFam; 1.20.190.20:FF:000001; 14-3-3 gamma 1; 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 PANTHER; PTHR18860; 14-3-3 PROTEIN; 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. 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_0000058622" 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" FT CONFLICT 141 FT /note="E -> Q (in Ref. 2; AAI02983)" FT /evidence="ECO:0000305" 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 //