ID   1433E_CHICK             Reviewed;         255 AA.
AC   Q5ZMT0; P84171;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=14-3-3 protein epsilon;
DE            Short=14-3-3E;
GN   Name=YWHAE {ECO:0000250|UniProtKB:P62262}; ORFNames=RCJMB04_1e8;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAG30963.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB {ECO:0000312|EMBL:CAG30963.1};
RC   TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG30963.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION, AND MASS SPECTROMETRY.
RC   TISSUE=Embryo {ECO:0000269|PubMed:16287166};
RX   PubMed=16287166; DOI=10.1002/pmic.200402056;
RA   Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J.,
RA   Schneider J., Palomar M.A., Linares R.;
RT   "Proteomic analysis of the Gallus gallus embryo at stage-29 of
RT   development.";
RL   Proteomics 5:4946-4957(2005).
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:0000250|UniProtKB:P62261}.
CC   -!- SUBUNIT: Homodimer, and heterodimer with other family members.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62258}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P62258}.
CC   -!- MASS SPECTROMETRY: Mass=29440; Mass_error=2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16287166};
CC   -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000255}.
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DR   EMBL; AJ719304; CAG30963.1; -; mRNA.
DR   RefSeq; NP_001006219.1; NM_001006219.1.
DR   AlphaFoldDB; Q5ZMT0; -.
DR   SMR; Q5ZMT0; -.
DR   BioGRID; 678887; 3.
DR   IntAct; Q5ZMT0; 1.
DR   STRING; 9031.ENSGALP00000039133; -.
DR   PaxDb; Q5ZMT0; -.
DR   PRIDE; Q5ZMT0; -.
DR   Ensembl; ENSGALT00000039926; ENSGALP00000039133; ENSGALG00000002661.
DR   GeneID; 417554; -.
DR   KEGG; gga:417554; -.
DR   CTD; 7531; -.
DR   VEuPathDB; HostDB:geneid_417554; -.
DR   eggNOG; KOG0841; Eukaryota.
DR   GeneTree; ENSGT01050000244964; -.
DR   HOGENOM; CLU_058290_0_2_1; -.
DR   InParanoid; Q5ZMT0; -.
DR   OMA; IPCATTG; -.
DR   OrthoDB; 1176818at2759; -.
DR   PhylomeDB; Q5ZMT0; -.
DR   PRO; PR:Q5ZMT0; -.
DR   Proteomes; UP000000539; Chromosome 19.
DR   Bgee; ENSGALG00000002661; Expressed in brain and 13 other tissues.
DR   ExpressionAtlas; Q5ZMT0; baseline.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0050815; F:phosphoserine residue binding; IBA:GO_Central.
DR   GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR   GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
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; Nucleus; Reference proteome.
FT   CHAIN           1..255
FT                   /note="14-3-3 protein epsilon"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000223506"
FT   REGION          234..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            57
FT                   /note="Interaction with phosphoserine on interacting
FT                   protein"
FT                   /evidence="ECO:0000250"
FT   SITE            130
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:P62262"
SQ   SEQUENCE   255 AA;  29174 MW;  07817CCBD1F75B26 CRC64;
     MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW
     RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF
     YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF
     YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE
     EQNKEALQDV EDENQ