1433G_BOVIN
ID 1433G_BOVIN Reviewed; 247 AA.
AC P68252; P29359;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=14-3-3 protein gamma;
DE AltName: Full=Protein kinase C inhibitor protein 1;
DE Short=KCIP-1;
DE Contains:
DE RecName: Full=14-3-3 protein gamma, N-terminally processed;
GN Name=YWHAG;
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].
RA Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J.,
RA McConnell D.G.;
RT "Expression of 14-3-3 proteins in bovine retinal photoreceptors.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-246.
RX PubMed=1671102; DOI=10.1016/0022-2836(91)90616-e;
RA Isobe T., Ichimura T., Sunaya T., Okuyama T., Takahashi N., Kuwano R.,
RA Takahashi Y.;
RT "Distinct forms of the protein kinase-dependent activator of tyrosine and
RT tryptophan hydroxylases.";
RL J. Mol. Biol. 217:125-132(1991).
RN [3]
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. {ECO:0000269|PubMed:7931346}.
CC -!- SUBUNIT: Homodimer. Interacts with MDM4 (phosphorylated); negatively
CC regulates MDM4 activity toward TP53. Interacts with RAF1, SSH1 and
CC CRTC2/TORC2. Interacts with ABL1 (phosphorylated form); the interaction
CC retains it in the cytoplasm. Interacts with GAB2 and SAMSN1. Interacts
CC with PKA-phosphorylated AANAT and SIRT2 (By similarity). Interacts with
CC the 'Thr-369' phosphorylated form of DAPK2 (By similarity). Interacts
CC with PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with
CC SLITRK1 (By similarity). Interacts with LRRK2; this interaction is
CC dependent on LRRK2 phosphorylation (By similarity). Interacts with
CC MARK2 and MARK3 (By similarity). Interacts with MEFV (By similarity).
CC Interacts with ENDOG, TSC2 and PIK3C3; interaction with ENDOG weakens
CC its interaction with TSC2 and PIK3C3 (By similarity). Interacts with TH
CC (phosphorylated form); one YWHAG dimer bounds to one TH tetramer, this
CC interaction may influence the phosphorylation and dephosphorylation of
CC TH (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P61981,
CC ECO:0000250|UniProtKB:P61982}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; AF043737; AAC02091.1; -; mRNA.
DR PIR; S13610; S13610.
DR AlphaFoldDB; P68252; -.
DR SMR; P68252; -.
DR STRING; 9913.ENSBTAP00000005327; -.
DR PaxDb; P68252; -.
DR PeptideAtlas; P68252; -.
DR PRIDE; P68252; -.
DR eggNOG; KOG0841; Eukaryota.
DR InParanoid; P68252; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISS:AgBase.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
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 CHAIN 1..247
FT /note="14-3-3 protein gamma"
FT /id="PRO_0000058605"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT CHAIN 2..247
FT /note="14-3-3 protein gamma, N-terminally processed"
FT /id="PRO_0000367906"
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 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 2
FT /note="N-acetylvaline; in 14-3-3 protein gamma, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 133
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P61983"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61983"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
SQ SEQUENCE 247 AA; 28253 MW; A481633DFAF4455D CRC64;
MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW
RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQIESK
VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS
VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD
DGGEGNN
