ID TAOK3_CHICK Reviewed; 898 AA.
AC Q9I9E0; Q5F3C7;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 24-JAN-2024, entry version 121.
DE RecName: Full=Serine/threonine-protein kinase TAO3;
DE EC=2.7.11.1;
DE AltName: Full=Kinase from chicken;
DE AltName: Full=Thousand and one amino acid protein 3;
GN Name=TAOK3; Synonyms=KFC; ORFNames=RCJMB04_21d18;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Fibroblast;
RX PubMed=10698516; DOI=10.1038/sj.onc.1203342;
RA Yustein J.T., Li D., Robinson D., Kung H.-J.;
RT "KFC, a Ste20-like kinase with mitogenic potential and capability to
RT activate the SAPK/JNK pathway.";
RL Oncogene 19:710-718(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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, ECO:0000269|PubMed:10698516}.
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; AF263314; AAF73045.1; -; mRNA.
DR EMBL; AJ851723; CAH65357.1; -; mRNA.
DR RefSeq; NP_001012541.1; NM_001012523.1.
DR AlphaFoldDB; Q9I9E0; -.
DR SMR; Q9I9E0; -.
DR STRING; 9031.ENSGALP00000069369; -.
DR PaxDb; 9031-ENSGALP00000011954; -.
DR GeneID; 395499; -.
DR KEGG; gga:395499; -.
DR CTD; 51347; -.
DR VEuPathDB; HostDB:geneid_395499; -.
DR eggNOG; KOG0577; Eukaryota.
DR InParanoid; Q9I9E0; -.
DR PhylomeDB; Q9I9E0; -.
DR PRO; PR:Q9I9E0; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:AgBase.
DR GO; GO:0016740; F:transferase activity; ISS:AgBase.
DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; ISS:AgBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISS:AgBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:AgBase.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:AgBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:AgBase.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR CDD; cd06633; STKc_TAO3; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR47167; SERINE/THREONINE-PROTEIN KINASE TAO1-LIKE PROTEIN; 1.
DR PANTHER; PTHR47167:SF7; TAO KINASE 3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; DNA damage; DNA repair; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..898
FT /note="Serine/threonine-protein kinase TAO3"
FT /id="PRO_0000086741"
FT DOMAIN 24..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 316..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 452..502
FT /evidence="ECO:0000255"
FT COILED 548..649
FT /evidence="ECO:0000255"
FT COILED 754..875
FT /evidence="ECO:0000255"
FT COMPBIAS 338..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..594
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 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"
FT CONFLICT 111
FT /note="M -> L (in Ref. 1; AAF73045)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..218
FT /note="ERK -> QRP (in Ref. 1; AAF73045)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="T -> A (in Ref. 1; AAF73045)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="M -> L (in Ref. 1; AAF73045)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="L -> V (in Ref. 1; AAF73045)"
FT /evidence="ECO:0000305"
FT CONFLICT 787
FT /note="R -> L (in Ref. 1; AAF73045)"
FT /evidence="ECO:0000305"
FT CONFLICT 811
FT /note="A -> G (in Ref. 1; AAF73045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 898 AA; 105459 MW; 62DD657B83DACFFB CRC64;
MRKGVPKDPE IADLFYKDDP EEIFVGLHEI GHGSFGAVYF ATNSHTNEVV AVKKMSYSGK
QTNEKWQDII KEVKFLQQLK HPNTIEYKGC YLKEHTAWLV MEYCLGSASD MLEVHKKPLQ
EVEIAAITHG ALQGLAYLHS HCKIHRDIKA GNILLTEPGQ VKLADFGSAS IVSPANSFVG
TPYWMAPEVI LAMDEGQYDG KVDVWSLGIT CIELAERKPP LFNMNAMSAL YHIAQNDSPT
LQSNEWSDSF RGFVDYCLQK IPQERPSSAD LLRHDFVRRD RPPRVLIDLI QRTKDAVREL
DNLQYRKMKK ILFQETRNGP LTESQEEEED SEHGSNLSRK MDSLGSNHSI PSMSVSTGSQ
SSSVSSMQEV LDESSPELVM MHSDESTVNS TSSVVQKKDH VFIRDEVGHR DRRPEVRPTQ
SVQNQALHYR NRERFATIKS ASLVTRQIHE HEQENELREQ MSGYKRMRRQ HQKQLIALEN
KLKAEMDEHR LKLQKEVETH ANNSSIELEK LAKKQVAVME KEAKTAAADE KKFQQQILAQ
QKKDMATFLE SQKKQYKLCK EKIKEEMNED HSTPKKEKQE RISKHKENLQ HTQAEEEAHL
LSQQRLYYDK NCRFFKRKTM IKRHELEQQN IREELNKKRT QKEMEHAMLI RHDESTRELE
YRQLHTLQKL RMDLIRLQHQ TELENQLEYN KRRERELHRK HFMELRQQPK NLKAMEMQIK
KQFQDTCKVQ TKQYKALKNH QLEVTPKSEH KTILKSLKDE QTRKLAILAE QYEQSINEMM
ASQALRRDEA QEAECQALRL QLQQEMELLN AYQSKIKMQT EAQHERELQK LEQRVSLRRA
HLEQKIEEEL AALQKERSER IKFLLERQER EIETFDMESL RMGFGNLVTL DYPKEDYR
//
