1433G_RAT
ID 1433G_RAT Reviewed; 247 AA.
AC P61983; A0JPM0; O70457; P35214; Q9UDP2; Q9UN99;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=14-3-3 protein gamma;
DE Contains:
DE RecName: Full=14-3-3 protein gamma, N-terminally processed;
GN Name=Ywhag;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Brown Norway, and Wistar; TISSUE=Brain;
RX PubMed=8381897; DOI=10.1016/0169-328x(93)90082-z;
RA Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H.;
RT "Molecular cloning of rat cDNAs for beta and gamma subtypes of 14-3-3
RT protein and developmental changes in expression of their mRNAs in the
RT nervous system.";
RL Brain Res. Mol. Brain Res. 17:135-146(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 5-10; 13-56; 62-69; 78-83; 89-120; 133-142 AND 126-247,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 144-162, INTERACTION WITH AANAT, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=11427721; DOI=10.1073/pnas.141118798;
RA Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
RA Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
RA Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
RT "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-
RT binding switch in melatonin synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-133 AND SER-215, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
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, SAMSN1 and SIRT2 (By
CC similarity). Interacts with PKA-phosphorylated AANAT. 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, ECO:0000269|PubMed:11427721}.
CC -!- INTERACTION:
CC P61983; Q5S007: LRRK2; Xeno; NbExp=6; IntAct=EBI-359821, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Localized in neurons, and axonally transported to
CC the nerve terminals. May be also present, at lower levels, in various
CC other tissues. {ECO:0000269|PubMed:8381897}.
CC -!- PTM: Phosphorylated by various PKC isozymes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; D17447; BAA04261.1; -; mRNA.
DR EMBL; S55305; AAA13844.1; -; mRNA.
DR EMBL; BC127496; AAI27497.1; -; mRNA.
DR PIR; B49023; B49023.
DR RefSeq; NP_062249.1; NM_019376.2.
DR RefSeq; XP_006249246.2; XM_006249184.3.
DR AlphaFoldDB; P61983; -.
DR SMR; P61983; -.
DR BioGRID; 248553; 8.
DR IntAct; P61983; 8.
DR MINT; P61983; -.
DR STRING; 10116.ENSRNOP00000001954; -.
DR iPTMnet; P61983; -.
DR PhosphoSitePlus; P61983; -.
DR SwissPalm; P61983; -.
DR jPOST; P61983; -.
DR PaxDb; P61983; -.
DR PRIDE; P61983; -.
DR Ensembl; ENSRNOT00000001954; ENSRNOP00000001954; ENSRNOG00000001436.
DR GeneID; 56010; -.
DR KEGG; rno:56010; -.
DR UCSC; RGD:62002; rat.
DR CTD; 7532; -.
DR RGD; 62002; Ywhag.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; P61983; -.
DR OMA; MANTERD; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P61983; -.
DR TreeFam; TF102003; -.
DR Reactome; R-RNO-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
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-8854518; AURKA Activation by TPX2.
DR Reactome; R-RNO-9614399; Regulation of localization of FOXO transcription factors.
DR PRO; PR:P61983; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001436; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; P61983; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0030234; F:enzyme regulator activity; TAS:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:RGD.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; ISO:RGD.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
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 CHAIN 1..247
FT /note="14-3-3 protein gamma"
FT /id="PRO_0000058609"
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_0000367910"
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:0007744|PubMed:22673903"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; 28303 MW; B0D16C6DE1F4455D CRC64;
MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW
RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK
VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS
VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD
DGGEGNN
