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 02-SEP-2026, entry version 97. DE RecName: Full=14-3-3 protein gamma {ECO:0000250|UniProtKB:P61981}; DE AltName: Full=Protein kinase C inhibitor protein 1; DE Short=KCIP-1; DE Flags: Fragments; GN Name=YWHAG {ECO:0000250|UniProtKB:P61981}; 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, AND SUBCELLULAR LOCATION. 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. Promotes inactivation of WDR24 CC component of the GATOR2 complex by binding to phosphorylated WDR24. CC Participates in the positive regulation of NMDA glutamate receptor CC activity by promoting the L-glutamate secretion through interaction CC with BEST1. Reduces keratinocyte intercellular adhesion, via CC interacting with PKP1 and sequestering it in the cytoplasm, thereby CC reducing its incorporation into desmosomes. Plays a role in CC mitochondrial protein catabolic process (also named MALM) that promotes CC the degradation of damaged proteins inside mitochondria (By CC similarity). {ECO:0000250|UniProtKB:P61981}. CC -!- SUBUNIT: Homodimer (By similarity). Forms heterodimers with SFN, YWHAB CC or YWHAQ (By similarity). Part of a complex that contains DSG3, PKP1, CC YAP1 and YWHAG; the complex is required for localization of DSG3 and CC YAP1 to the cell membrane in keratinocytes (By similarity). Interacts CC with YAP1 (By similarity). Interacts with SAMSN1 (By similarity). CC Interacts with RAF1, SSH1 and CRTC2/TORC2 (By similarity). Interacts CC with ABL1 (phosphorylated form); the interaction retains it in the CC cytoplasm (By similarity). Interacts with GAB2 (By similarity). CC Interacts with MDM4 (phosphorylated); negatively regulates MDM4 CC activity toward TP53 (By similarity). Interacts with PKA-phosphorylated CC AANAT and SIRT2 (PubMed:11427721). Interacts with the 'Thr-369' CC phosphorylated form of DAPK2 (By similarity). Interacts with PI4KB, CC TBC1D22A and TBC1D22B (By similarity). Interacts with SLITRK1 (By CC 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 (phosphorylated) CC WDR24 (By similarity). Interacts with BEST1; this interaction promotes CC L-glutamate channel activity leading to the positive regulation of NMDA CC glutamate receptor activity through the L-glutamate secretion (By CC similarity). Interacts with PKP1 (when phosphorylated); the interaction CC results in translocation of PKP1 to the cytoplasm and loss of CC intercellular adhesion in keratinocytes (By similarity). Interacts with CC SPATA18/MIEAP; a protein that also plays a role in MALM (By CC similarity). {ECO:0000250|UniProtKB:P61981, CC ECO:0000250|UniProtKB:P61982, ECO:0000269|PubMed:11427721}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:1317796}. CC Mitochondrion matrix {ECO:0000250|UniProtKB:P61981}. Note=Translocates CC to the mitochondrial matrix following induction of MALM (mitochondrial CC protein catabolic process). {ECO:0000250|UniProtKB:P61981}. CC -!- PTM: Phosphorylated by various PKC isozymes. CC {ECO:0000250|UniProtKB:P61981}. 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 PIR; S78574; S78574. DR AlphaFoldDB; P68253; -. DR SMR; P68253; -. DR Proteomes; UP000809102; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB. DR GO; GO:0140031; F:phosphorylation-dependent protein binding; ISS:UniProtKB. DR GO; GO:0140311; F:protein sequestering activity; ISS:UniProtKB. DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISS:UniProtKB. DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB. DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB. DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB. DR FunFam; 1.20.190.20:FF:000004; 14-3-3 protein gamma; 1. DR Gene3D; 1.20.190.20; 14-3-3 domain; 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; 14-3-3 PROTEIN; 1. DR Pfam; PF00244; 14-3-3; 1. 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 Cytoplasm; Direct protein sequencing; Mitochondrion; Phosphoprotein; KW Reference proteome. FT CHAIN <1..>158 FT /note="14-3-3 protein gamma" FT /id="PRO_0000058610" FT REGION <1..>158 FT /note="Interaction with SPATA18/MIEAP" FT SITE 34 FT /note="Interaction with phosphoserine on interacting FT protein" FT /evidence="ECO:0000250|UniProtKB:P61981" FT SITE 59 FT /note="Interaction with phosphoserine on interacting FT protein" FT /evidence="ECO:0000250|UniProtKB:P61981" 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 //