IKKA_CHICK
ID IKKA_CHICK Reviewed; 759 AA.
AC Q5ZJB4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Inhibitor of nuclear factor kappa-B kinase subunit alpha;
DE Short=I kappa-B kinase alpha;
DE Short=IKK-A;
DE Short=IKK-alpha;
DE Short=IkBKA;
DE Short=IkappaB kinase;
DE EC=2.7.11.10;
DE AltName: Full=Conserved helix-loop-helix ubiquitous kinase;
DE AltName: Full=Nuclear factor NF-kappa-B inhibitor kinase alpha;
DE Short=NFKBIKA;
GN Name=CHUK; Synonyms=IKKA; ORFNames=RCJMB04_19h23;
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 [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: Phosphorylates inhibitors of NF-kappa-B thus leading to the
CC dissociation of the inhibitor/NF-kappa-B complex and ultimately the
CC degradation of the inhibitor. Phosphorylates 'Ser-10' of histone H3 at
CC NF-kappa-B-regulated promoters during inflammatory responses triggered
CC by cytokines. {ECO:0000250|UniProtKB:O15111}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-
CC seryl-[I-kappa-B protein]; Xref=Rhea:RHEA:19073, Rhea:RHEA-
CC COMP:13698, Rhea:RHEA-COMP:13699, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC ChEBI:CHEBI:456216; EC=2.7.11.10;
CC -!- ACTIVITY REGULATION: Activated when phosphorylated and inactivated when
CC dephosphorylated. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250}.
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; AJ720520; CAG32179.1; -; mRNA.
DR RefSeq; NP_001012922.1; NM_001012904.1.
DR AlphaFoldDB; Q5ZJB4; -.
DR SMR; Q5ZJB4; -.
DR STRING; 9031.ENSGALP00000005196; -.
DR PaxDb; Q5ZJB4; -.
DR PRIDE; Q5ZJB4; -.
DR GeneID; 423669; -.
DR KEGG; gga:423669; -.
DR CTD; 1147; -.
DR VEuPathDB; HostDB:geneid_423669; -.
DR eggNOG; KOG4250; Eukaryota.
DR InParanoid; Q5ZJB4; -.
DR OrthoDB; 1013139at2759; -.
DR PhylomeDB; Q5ZJB4; -.
DR Reactome; R-GGA-1227739; Caspase-8 and -10 mediated induction of NF-kB.
DR Reactome; R-GGA-1227892; TRAF6 mediated NF-kB activation.
DR Reactome; R-GGA-434001; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
DR Reactome; R-GGA-434131; NFkB activation mediated by RIP1 complexed with activated TLR3.
DR PRO; PR:Q5ZJB4; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008385; C:IkappaB kinase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008384; F:IkappaB kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:AgBase.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 1.20.1270.250; -; 1.
DR InterPro; IPR041185; IKBKB_SDD.
DR InterPro; IPR046375; IKBKB_SDD_sf.
DR InterPro; IPR022007; IKKbetaNEMObind.
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; PF18397; IKBKB_SDD; 1.
DR Pfam; PF12179; IKKbetaNEMObind; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM01239; IKKbetaNEMObind; 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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..759
FT /note="Inhibitor of nuclear factor kappa-B kinase subunit
FT alpha"
FT /id="PRO_0000268160"
FT DOMAIN 29..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..490
FT /note="Leucine-zipper"
FT REGION 691..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..758
FT /note="NEMO-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 691..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 35..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 759 AA; 86144 MW; 135FDF10396B7B96 CRC64;
MERGAERGPP PAPGGVALRG QPAGGCGPWE MRDRLGTGGF GNVCLYQHQD TGARVAIKSC
RLELSVKNKD RWCHEIDIMK KLNHPNVVRA CEVPEEMNFL VNDVPLLAME YCSGGDLRKL
LNKPENCCGL KESQILSLLS DIGSGIQYLH ENRIIHRDLK PENIVLQDEG GKIIHKIIDL
GYAKDLDQGS LCTSFVGTLQ YLAPELFENK SYSVTVDYWS FGTMVFECIA GFRPFLHNLQ
PFTWHEKIKK KDPKHIFASE EMNGEVRFST HLPQPHSICS LIVEPMESWL QLMLNWDPEQ
RGGGLDPETN SPKCFLLMDH ILNLKIVHIL NMTSAKIVSF LLHPEESLHF LQNRIESETG
ISTGNQELLL ETGICLDPRK PASQCVIDGV RGWDSYMVYL FDKSKTVYDG PFASRSLSEC
VNYIVQDSKI QLPIPQLRKV WAEAVHYVIG LKEDYSRLFQ GQRAAMLSLL RYNANLIKMK
NNMVSASQQL KAKLEFFHQS IRLDLERYSD QMAYGISSEK MLKAWKEMEE KASHCAQAED
IGYLDEQIMA LHTEIVELQK SPYARRQGEV MESLEQRAID LYKQLKTRPP DHAYSDSTDM
VKIIVQTVQS QDRVLKELFG HLSKLLGCKQ KIIDLLPKIE VALNNIKEAD NSEMQMQGKR
QREIWHLLKI ACTQSSSRSL VSSSLEGTAS TPAATWVPQS SSEYAPHPLS SMATPGDGEN
FVDVIEENLN YLDRFSSMLQ EAREEQNNSL TNFDWSWLK
