TAOK3_XENLA
ID TAOK3_XENLA Reviewed; 896 AA.
AC Q6DD27;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Serine/threonine-protein kinase TAO3;
DE EC=2.7.11.1;
DE AltName: Full=Thousand and one amino acid protein 3;
GN Name=taok3;
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-protein kinase that acts as a regulator of
CC the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK
CC cascade. Acts as an activator of the p38/MAPK14 stress-activated MAPK
CC cascade. In response to DNA damage, involved in the G2/M transition DNA
CC damage checkpoint by activating the p38/MAPK14 stress-activated MAPK
CC cascade, probably by mediating phosphorylation of upstream MAP kinase
CC kinases. Inhibits basal activity of MAPK8/JNK cascade (By similarity).
CC {ECO:0000250}.
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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; BC077802; AAH77802.1; -; mRNA.
DR RefSeq; NP_001086943.1; NM_001093474.1.
DR AlphaFoldDB; Q6DD27; -.
DR SMR; Q6DD27; -.
DR IntAct; Q6DD27; 1.
DR PRIDE; Q6DD27; -.
DR GeneID; 446778; -.
DR KEGG; xla:446778; -.
DR CTD; 446778; -.
DR Xenbase; XB-GENE-978581; taok3.L.
DR OrthoDB; 617606at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 446778; Expressed in intestine 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; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; DNA damage; DNA repair; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..896
FT /note="Serine/threonine-protein kinase TAO3"
FT /id="PRO_0000086742"
FT DOMAIN 24..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 316..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..513
FT /evidence="ECO:0000255"
FT COILED 545..650
FT /evidence="ECO:0000255"
FT COILED 752..873
FT /evidence="ECO:0000255"
FT COMPBIAS 338..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 896 AA; 105366 MW; 5A05AA569974B458 CRC64;
MRRGLVKDPD NADLFCKEDP ERIFVDLHEI GHGSFGAVYF ATNSTTNEIV AVKKMSYSGK
QMNEKWQDII KEVKFLQQLK HPNTIEYKGC YLKDHTAWLV MEYCLGSASD LLEVHKKPLQ
EVEIAAITHG ALQGLAYLHS HNMIHRDIKA GNILLTEPGQ VKLADFGSAS KSSPANSFVG
TPYWMAPEVI LAMDEGQYDG KIDIWSLGIT CIELAERKPP LFNMNAMSAL YHIAQNESPT
LQSNEWTDSF KGFVDYCLQK LPQERPASLE LLRHDFVWRE RPARVLIDLI QRTKDAVREL
DNLQYRKMKK ILFQESRNGP LNESQEDDED SEHGTSLTRK MDSLGSNHSI PSTSVSTGSQ
SSSVNSIQEV MEDGSPDLIM SFSCSFDSTS SLVHKKDHAF IRDEADHRDP RPELRPTQSV
QSQALHYRTR ERFATIKSAS LVTRQIHEHE QENELREQMS GYKRMRRQHQ KQLIALENKL
KAEMDEHRLK LQKEVETHAN NASIELEKLS KRQFVGMDKE AKVAAADERR FQQQIIAQQK
KDLTSFLESQ KKQYKICKEK IKEELNEDHS TPKKEKQERI SKHKENLQHT QAEEEAQLLS
QQRLYYEKNC RLFKRKIMIK RHEVEQQHIR EELNKKRTQK EMEHAMLIRQ DESTRELEYR
QLQMLQKLRM DLIRLQHQTE LENQLEYNKR RERELHRKHV MELRQQPKNL KVMEMQIKKQ
FQDTCKVQTK QYKALKNHQL EVSPKCEHKT ILKSLKDEQT RKLAILAEQY EQSINEMMAS
QALRLDEAQE AECQALRQQL QQEMELLNAY QSKIKMQTEA QHERELQKLE QRVSLRRAHL
EQKIEEELVA LQKERSERIK HLFERQEREI ETFDMESLRM GFGNLVTLEY PKEDYR
