ID   1433Z_XENLA             Reviewed;         245 AA.
AC   Q91896; O57469;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=14-3-3 protein zeta;
GN   Name=ywhaz;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9197545; DOI=10.1016/s0378-1119(97)00013-9;
RA   Kousteni S., Tura F., Sweeney G.E., Ramji D.P.;
RT   "Sequence and expression analysis of a Xenopus laevis cDNA which encodes a
RT   homologue of mammalian 14-3-3 zeta protein.";
RL   Gene 190:279-285(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9450960; DOI=10.1091/mbc.9.2.345;
RA   Kumagai A., Yakowec P.S., Dunphy W.G.;
RT   "14-3-3 proteins act as negative regulators of the mitotic inducer Cdc25 in
RT   Xenopus egg extracts.";
RL   Mol. Biol. Cell 9:345-354(1998).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Present in all adult tissues examined with the
CC       highest levels in the brain.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR   EMBL; X95519; CAA64773.1; -; mRNA.
DR   EMBL; AF033312; AAC41252.1; -; mRNA.
DR   AlphaFoldDB; Q91896; -.
DR   SMR; Q91896; -.
DR   OMA; AEATMNS; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Reference proteome.
FT   CHAIN           1..245
FT                   /note="14-3-3 protein zeta"
FT                   /id="PRO_0000058633"
FT   SITE            56
FT                   /note="Interaction with phosphoserine on interacting
FT                   protein"
FT                   /evidence="ECO:0000250"
FT   SITE            127
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"
FT   CONFLICT        173..185
FT                   /note="NFSVFYYEILNCP -> KLLCVLTNEESSTVQ (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   245 AA;  27729 MW;  8ACF62C58E68C630 CRC64;
     MDKNELVQKA KLAEQAERYD DMAACMKRVT EEGGELSNEE RNLLSVAYKN VVGARRSSWR
     VVSSIEQKTE GAEKKQEMSR EYREKIEAEL REICNDVLNL LDKFLIANAT QPESKVFYLK
     MKGDYYRYLA EVAAGNAKTE IVGQSQKAYQ DAFDISKTEM QPTHPIRLGL ALNFSVFYYE
     ILNCPDKACA LAKAAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEQG
     EGGEN