1433F_BOVIN
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 03-AUG-2022, entry version 110.
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=10.1038/44594a0;
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}.
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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 IntAct; P68509; 2.
DR MINT; P68509; -.
DR STRING; 9913.ENSBTAP00000041575; -.
DR PaxDb; P68509; -.
DR PeptideAtlas; P68509; -.
DR PRIDE; P68509; -.
DR Ensembl; ENSBTAT00000044059; ENSBTAP00000041575; ENSBTAG00000031134.
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; ENSGT01050000244817; -.
DR InParanoid; P68509; -.
DR OMA; IKNCDES; -.
DR OrthoDB; 1176818at2759; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000031134; Expressed in occipital lobe and 107 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0019904; F:protein domain specific 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:0042921; P:glucocorticoid receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
DR GO; GO:0086010; P:membrane depolarization during action potential; IEA:Ensembl.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IEA:Ensembl.
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_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
