IKKA_XENTR
ID IKKA_XENTR Reviewed; 743 AA.
AC Q28DZ1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=TEgg047h13.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CR848527; CAJ83676.1; -; mRNA.
DR RefSeq; NP_001016900.1; NM_001016900.2.
DR RefSeq; NP_001297046.1; NM_001310117.1.
DR AlphaFoldDB; Q28DZ1; -.
DR SMR; Q28DZ1; -.
DR STRING; 8364.ENSXETP00000038296; -.
DR PaxDb; Q28DZ1; -.
DR GeneID; 101732839; -.
DR GeneID; 549654; -.
DR KEGG; xtr:549654; -.
DR CTD; 1147; -.
DR Xenbase; XB-GENE-5910008; chuk.
DR eggNOG; KOG4250; Eukaryota.
DR HOGENOM; CLU_000288_101_2_1; -.
DR InParanoid; Q28DZ1; -.
DR OrthoDB; 1013139at2759; -.
DR Reactome; R-XTR-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-XTR-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-XTR-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-XTR-202424; Downstream TCR signaling.
DR Reactome; R-XTR-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-XTR-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-XTR-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-XTR-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-XTR-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-XTR-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-XTR-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-XTR-933542; TRAF6 mediated NF-kB activation.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000017643; Expressed in egg cell and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF18397; IKBKB_SDD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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..743
FT /note="Inhibitor of nuclear factor kappa-B kinase subunit
FT alpha"
FT /id="PRO_0000268829"
FT DOMAIN 15..300
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 453..474
FT /note="Leucine-zipper"
FT REGION 736..741
FT /note="NEMO-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 743 AA; 85088 MW; 2ED9B09747636CDE CRC64;
MEKPPVQHGA VCGPWDMKDR LGTGGFGNVC LYQNRETGEL KAIKSCRLEL SMKNKERWCQ
EIQIMKRLNH PNVVKACEVP PEMDFLVNDV PHLAMEYCAG GDLRKLLNKP ENCCGLKESQ
VLNLMSDIGS GIQYLHEKRI IHRDLKPENI VLQECNGKTV HKIIDLGYAK DLDQGSLCTS
FVGTLQYLAP ELFENKPYSV TVDYWSFGTM VFECIAGFRP FLHNMQPFTW HEKIKKKDHK
HIYAYEEMSG EIRFSSYLPQ PNNLCSIIVD KIETWLQLLL NWDPIQRGGG MDCGRPQCFV
LMDQILNLKI VHILNMTSAK IHSFHLQPEE SLHTLQSRIE TETGISTCNQ ELLLEMGVSL
DPRKPASQCV IDGVKGWDSY MVYLFDKSKT VYEGPFQSRS LSECLNYIVQ DSKVQLPIPQ
LRKVWAEAVH YVSGLKEDYS RLFQGQRAAM LSLLRFNTNL TKMKNTMVSA SQQLGAKLQF
FKRSIEIDLE RYSDQMAYGI SSEKMLRAWK EMEDKAVCFG KAGKIHFLDE TIMGLHTEIV
ELQKSPCARR QGDVMEHLEQ RAMELYKQLK PRSPDKAYSD STEMVKILVQ TVQGQDRVLK
ELFGHLSKLL GCKQKIIDLL PQIEMTVNNI KEADSSLMQM QAKRQREIWH LLKIACTQSS
ARSLGPASVE TPITPRTSAW PDQSSSQALF SMLTTKDKSR EILRHTIDKN SDYQKLLSSL
ILQTQTTMEQ NSLMSLDFSW LNK
