1433T_BOVIN
ID 1433T_BOVIN Reviewed; 245 AA.
AC Q3SZI4; A7E3X8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=14-3-3 protein theta;
GN Name=YWHAQ;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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 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; BT030749; ABS45065.1; -; mRNA.
DR EMBL; BC102840; AAI02841.1; -; mRNA.
DR RefSeq; NP_001071595.1; NM_001078127.2.
DR PDB; 6BCY; X-ray; 2.30 A; A/B/E/F=1-245.
DR PDB; 6BD1; X-ray; 2.35 A; A/B/E/F=1-245.
DR PDBsum; 6BCY; -.
DR PDBsum; 6BD1; -.
DR AlphaFoldDB; Q3SZI4; -.
DR SMR; Q3SZI4; -.
DR STRING; 9913.ENSBTAP00000032779; -.
DR PaxDb; Q3SZI4; -.
DR PeptideAtlas; Q3SZI4; -.
DR PRIDE; Q3SZI4; -.
DR Ensembl; ENSBTAT00000032851; ENSBTAP00000032779; ENSBTAG00000002108.
DR GeneID; 768311; -.
DR KEGG; bta:768311; -.
DR CTD; 10971; -.
DR VEuPathDB; HostDB:ENSBTAG00000002108; -.
DR VGNC; VGNC:37047; YWHAQ.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; Q3SZI4; -.
DR OMA; FEMATTI; -.
DR OrthoDB; 1176818at2759; -.
DR TreeFam; TF102002; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000002108; Expressed in adenohypophysis and 102 other tissues.
DR ExpressionAtlas; Q3SZI4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Nitration;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..245
FT /note="14-3-3 protein theta"
FT /id="PRO_0000058635"
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"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:6BCY"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:6BCY"
FT HELIX 38..67
FT /evidence="ECO:0007829|PDB:6BCY"
FT HELIX 76..103
FT /evidence="ECO:0007829|PDB:6BCY"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:6BCY"
FT HELIX 112..132
FT /evidence="ECO:0007829|PDB:6BCY"
FT HELIX 135..159
FT /evidence="ECO:0007829|PDB:6BCY"
FT HELIX 165..180
FT /evidence="ECO:0007829|PDB:6BCY"
FT HELIX 185..201
FT /evidence="ECO:0007829|PDB:6BCY"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:6BCY"
FT HELIX 208..228
FT /evidence="ECO:0007829|PDB:6BCY"
SQ SEQUENCE 245 AA; 27764 MW; 175534325E9E37C4 CRC64;
MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR
VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK
MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE
ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA
EGAEN
