ID   1433T_RABIT             Reviewed;         245 AA.
AC   Q6Q6X0;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=14-3-3 protein theta;
DE   AltName: Full=14-3-3 protein tau;
GN   Name=YWHAQ;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Qian Z., Barmack N.H.;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with CDK16 (By similarity). Interacts
CC       with RGS7 (phosphorylated form). Interacts with SSH1. Interacts with
CC       CDKN1B ('Thr-198' phosphorylated form); the interaction translocates
CC       CDKN1B to the cytoplasm. Interacts with GAB2. Interacts with the 'Ser-
CC       241' phosphorylated form of PDPK1. 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 RIPOR2 (By similarity). Interacts with
CC       INAVA; the interaction increases upon PRR (pattern recognition
CC       receptor) stimulation and is required for cellular signaling pathway
CC       activation and cytokine secretion (By similarity). Interacts with
CC       INAVA; the interaction increases upon PRR (pattern recognition
CC       receptor) stimulation and is required for cellular signaling pathway
CC       activation and cytokine secretion (By similarity). Interacts with
CC       MARK2, MARK3 and MARK4 (By similarity). Interacts with MEFV (By
CC       similarity). {ECO:0000250|UniProtKB:P27348,
CC       ECO:0000250|UniProtKB:P68254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR   EMBL; AY555574; AAS72303.1; -; mRNA.
DR   RefSeq; NP_001075637.1; NM_001082168.1.
DR   AlphaFoldDB; Q6Q6X0; -.
DR   SMR; Q6Q6X0; -.
DR   STRING; 9986.ENSOCUP00000009032; -.
DR   PRIDE; Q6Q6X0; -.
DR   GeneID; 100008930; -.
DR   KEGG; ocu:100008930; -.
DR   CTD; 10971; -.
DR   eggNOG; KOG0841; Eukaryota.
DR   InParanoid; Q6Q6X0; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   CDD; cd10023; 14-3-3_theta; 1.
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   InterPro; IPR042584; 14-3-3_theta.
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; Isopeptide bond; Nitration; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..245
FT                   /note="14-3-3 protein theta"
FT                   /id="PRO_0000058639"
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|UniProtKB:P27348"
FT   MOD_RES         3
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P27348"
FT   MOD_RES         49
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P27348"
FT   MOD_RES         68
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P27348"
FT   MOD_RES         82
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQV8"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P68254"
FT   MOD_RES         104
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQV8"
FT   MOD_RES         115
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P27348"
FT   MOD_RES         232
FT                   /note="Phosphoserine; by CK1"
FT                   /evidence="ECO:0000250|UniProtKB:P27348, ECO:0000305"
FT   CROSSLNK        49
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P27348"
SQ   SEQUENCE   245 AA;  27778 MW;  E30471260E8B366E CRC64;
     MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR
     VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK
     MKGDYFRYLA EVACGDDRKQ TIENSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE
     ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA
     EGAEN