1433G_SHEEP
ID 1433G_SHEEP Reviewed; 158 AA.
AC P68253; P29359;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=14-3-3 protein gamma;
DE AltName: Full=Protein kinase C inhibitor protein 1;
DE Short=KCIP-1;
DE Flags: Fragments;
GN Name=YWHAG;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1317796; DOI=10.1111/j.1432-1033.1992.tb16946.x;
RA Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.;
RT "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) from
RT sheep brain. Amino acid sequence of phosphorylated forms.";
RL Eur. J. Biochem. 206:453-461(1992).
RN [2]
RP INTERACTION WITH AANAT.
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).
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 the
CC 'Thr-369' phosphorylated form of DAPK2 (By similarity). Interacts with
CC PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with SLITRK1
CC (By similarity). Interacts with LRRK2; this interaction is dependent on
CC LRRK2 phosphorylation (By similarity). Interacts with MARK2 and MARK3
CC (By similarity). Interacts with MEFV (By similarity). Interacts with
CC ENDOG, TSC2 and PIK3C3; interaction with ENDOG weakens its interaction
CC with TSC2 and PIK3C3 (By similarity).Interacts with TH (phosphorylated
CC form); one YWHAG dimer bounds to one TH tetramer, this interaction may
CC influence the phosphorylation and dephosphorylation of TH (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P61981,
CC ECO:0000250|UniProtKB:P61982, ECO:0000269|PubMed:11427721}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: N-terminus residue is acetylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR PIR; S78574; S78574.
DR AlphaFoldDB; P68253; -.
DR SMR; P68253; -.
DR PRIDE; P68253; -.
DR Proteomes; UP000002356; 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: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; -; 2.
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; 2.
DR Pfam; PF00244; 14-3-3; 2.
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..>158
FT /note="14-3-3 protein gamma"
FT /id="PRO_0000058610"
FT SITE 34
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 60
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P61983"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61983"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT NON_CONS 48..49
FT /evidence="ECO:0000305"
FT NON_CONS 113..114
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 158
SQ SEQUENCE 158 AA; 18000 MW; 69EC73EBA23B7B6F CRC64;
AAAMKNVTEL NEPLSNEERN LLSVAYKNVV GARRSSWRVI SSIEQKTSFY LKMKGDYYRY
LAEVATGEKR ATVVESSEKA YSEAHEISKE HMQPTHPIRL GLALNYSVFY YEITAFDDAI
AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DQQDDDGG
