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Database: UniProt
Entry: A0A2K5Y827_MANLE
LinkDB: A0A2K5Y827_MANLE
Original site: A0A2K5Y827_MANLE 
ID   A0A2K5Y827_MANLE        Unreviewed;       248 AA.
AC   A0A2K5Y827;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=14-3-3 protein theta {ECO:0000256|ARBA:ARBA00014997};
GN   Name=YWHAQ {ECO:0000313|Ensembl:ENSMLEP00000011694.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000011694.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000011694.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025150}.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
CC       {ECO:0000256|ARBA:ARBA00006141, ECO:0000256|RuleBase:RU003466}.
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DR   AlphaFoldDB; A0A2K5Y827; -.
DR   STRING; 9568.ENSMLEP00000011694; -.
DR   Ensembl; ENSMLET00000035119.1; ENSMLEP00000011694.1; ENSMLEG00000030005.1.
DR   GeneTree; ENSGT01090000260040; -.
DR   OMA; NPKRACE; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR   CDD; cd10023; 14-3-3_theta; 1.
DR   Gene3D; 1.20.190.20; 14-3-3 domain; 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   InterPro; IPR042584; 14-3-3_theta.
DR   PANTHER; PTHR18860; 14-3-3 PROTEIN; 1.
DR   PANTHER; PTHR18860:SF3; 14-3-3 PROTEIN THETA; 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; 14-3-3 protein; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT   DOMAIN          6..245
FT                   /note="14-3-3"
FT                   /evidence="ECO:0000259|SMART:SM00101"
FT   SITE            59
FT                   /note="Interaction with phosphoserine on interacting
FT                   protein"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
FT   SITE            130
FT                   /note="Interaction with phosphoserine on interacting
FT                   protein"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
SQ   SEQUENCE   248 AA;  28004 MW;  4279A31EEE839D6F CRC64;
     APAMEKTELI QKAKLAEQAE RYDDMATCMK AVTEQGAELS NEERNLLSVA YKNVVGGRRS
     AWRVISSIEQ KTDTSDKKLQ LIKDYREKVE SELRSICTTV LELLDKYLIA NATNPESKVF
     YLKMKGDYFR YLAEVACGDD RKQTIDNSQG AYQEAFDISK KEMQPTHPIR LGLALNFSVF
     YYEILNNPEL ACTLAKTAFD EAIAELDTLN EDSYKDSTLI MQLLRDNLTL WTSDSAGEEC
     DAAEGAEN
//
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