IKKA_XENLA
ID IKKA_XENLA Reviewed; 743 AA.
AC Q6GM53;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 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;
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=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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; BC074232; AAH74232.1; -; mRNA.
DR RefSeq; NP_001086127.1; NM_001092658.1.
DR AlphaFoldDB; Q6GM53; -.
DR SMR; Q6GM53; -.
DR GeneID; 444556; -.
DR KEGG; xla:444556; -.
DR CTD; 444556; -.
DR Xenbase; XB-GENE-5910051; chuk.S.
DR OrthoDB; 1013139at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 444556; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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_0000268828"
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; 85152 MW; 7FB7B4FA325B1860 CRC64;
MERPPVQHGA VCGPWDMKDR LGTGGFGNVC LYQNRETGEL KAIKSCRLEL SVKNKERWCQ
EIQIMKRLNH PNVVKACDVP PEMDFLVNDV PHLAMEYCAG GDLRKLLNKP ENCCGLKESQ
VLNLISDIGS GIQYLHENRI IHRDLKPENI VLQECNGKTV HKIIDLGYAK DLDQGSLCTS
FVGTLQYLAP ELFENKPYSV TVDYWSFGTM AFECIAGFRP FLHNMQPFTW HEKIKKKDHK
HIYAYEEMSG EIRFSTSLPE PNNLCSIIVD KIETWLQLLL NWDPVQRGGG IDCGRPRCFM
LMDQIFSLKI VHILNMTSAK IHSFHLQPEE SLHTLQSRIE RETGISTCNQ ELLLEMGVSL
DPRKPASQCV IDGVKGWDSY MVYLFDKSKT VYEGPFQSRS LSECLNYIVQ DSKVQLPIPQ
LRKVWAEAVH YVSGLKEDYS RLFQGQRAAM LSLLRFNTNL TKMKNTMVSA SQQLDAKLQF
FKRSIEIDLE RYSDQMAYGI SSEKMLRAWK EMEDKAVCFG KAGEIHFLDE TIMGLHTEIV
ELQRSPCARR QGDVMEHLEQ RAMELYKQLK PRSPDKAYSD STEMVKILVQ TVQGQDRVLK
ELFGHLSKLL GCKQKIIDLL PQIEMTVNNI KEADSSLMQM QAKRQREIWH LLKIACTQSS
TRSLVTASGE TPITSRTSAW SDQSSPQALF SMLTSKDKGR EILRHTIDKN TDYQKLLSNL
ILQTQTTMEQ TSLMSMDFSW LNQ
