TBK1_XENLA
ID TBK1_XENLA Reviewed; 725 AA.
AC Q6DFJ6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Serine/threonine-protein kinase TBK1;
DE EC=2.7.11.1;
GN Name=tbk1;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine/threonine kinase that plays an essential role in
CC regulating inflammatory responses to foreign agents. Following
CC activation of toll-like receptors by viral or bacterial components,
CC associates with traf3 and tank and phosphorylates interferon regulatory
CC factors (IRFs) irf3 and irf7 as well as ddx3x. This activity allows
CC subsequent homodimerization and nuclear translocation of the IRFs
CC leading to transcriptional activation of pro-inflammatory and antiviral
CC genes including ifna and ifnb. In order to establish such an antiviral
CC state, TBK1 form several different complexes whose composition depends
CC on the type of cell and cellular stimuli.
CC {ECO:0000250|UniProtKB:Q9UHD2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q9UHD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9UHD2};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9UHD2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UHD2}.
CC -!- DOMAIN: Comprises A N-terminal kinase domain, a ubiquitin-like domain
CC and a C-terminal coiled-coil region mediating homodimerization.
CC {ECO:0000250|UniProtKB:Q9UHD2}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. I-kappa-B kinase subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; BC076740; AAH76740.1; -; mRNA.
DR RefSeq; NP_001086516.1; NM_001093047.1.
DR AlphaFoldDB; Q6DFJ6; -.
DR SMR; Q6DFJ6; -.
DR BioGRID; 103211; 1.
DR IntAct; Q6DFJ6; 1.
DR PRIDE; Q6DFJ6; -.
DR DNASU; 446351; -.
DR GeneID; 446351; -.
DR KEGG; xla:446351; -.
DR CTD; 446351; -.
DR Xenbase; XB-GENE-955455; tbk1.L.
DR OMA; DWSADMP; -.
DR OrthoDB; 563981at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 446351; Expressed in spleen and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:0032479; P:regulation of type I interferon production; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR041309; TBK1_CCD1.
DR InterPro; IPR041087; TBK1_ULD.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18394; TBK1_CCD1; 1.
DR Pfam; PF18396; TBK1_ULD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Immunity; Innate immunity; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..725
FT /note="Serine/threonine-protein kinase TBK1"
FT /id="PRO_0000086745"
FT DOMAIN 9..306
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 309..385
FT /note="Ubiquitin-like"
FT COILED 635..709
FT /evidence="ECO:0000255"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 725 AA; 83271 MW; 0264EC5A270D12EB CRC64;
MQSTANYLWM LSDILGQGAT ANVYRGRNKK TGDLYAVKVF NSLSFQRPAD VQMREFEVLK
KLNHKNIVKL FAIEEEMSSR HKVLVMEFCP CASLYSVLEE PTNSYGLPES EFLIVSRDVV
AGMNHLRENG IIHRDIKPGN IMREIGEDGK SVYKLTDFGA ARELEDDEQF VSLYGTEEYL
HPDMYERAVL RKEHQKKYSA TVDLWSIGVT FYHAATGSLP FRPFEGPRRN KEVMYKIIAG
KPSGAISGVQ RAENGPIEWS GELPATCNLS MGLQTLFTPV LANILEADQE KCWGFEQFFA
VTNDIFNRIV VHVFSLQQMT PHKIYINTYD KVPDFHDLVY KQTKIPGQNQ ELLFEGRRLV
LEQGRLAQHF PITTDENPIF VLTREMVSVI GLRFDEIVIP KPISHYDLDV DANMAKAVTG
VACYYCRIAA SLLLVLDLMR KGIRWLSELM KEEYNENVHR NTEVSLKLNF CNRTTEKDLK
IYEQLMQTSV ESEVYAIHAK LLNLSSTQEG LKSSLQEVKN KLTPGGTLMD SWINTEGIHA
ADRNVEKLQV LLSLITEIYC QFKKDKAQRR LSYNEEQIHK FDKQKLCLHA AKAYSLFKDE
CVGKYEVFRS KTLEWMRKMI HVRKQLFSIK SKCFDIEEEA SKCQHYINQY QEKMSPKMFA
APSGMKSAVN PIYSSPNTLV EMTLGMRKLK EDMEGVVKEL EENNHILERF GALTIDGDFR
NVDCI
