ID A0A6I8PEK0_ORNAN Unreviewed; 745 AA.
AC A0A6I8PEK0;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=Inhibitor of nuclear factor kappa-B kinase subunit alpha {ECO:0000256|ARBA:ARBA00021841};
DE EC=2.7.11.10 {ECO:0000256|ARBA:ARBA00012442};
DE AltName: Full=I-kappa-B kinase 1 {ECO:0000256|ARBA:ARBA00076062};
DE AltName: Full=Nuclear factor NF-kappa-B inhibitor kinase alpha {ECO:0000256|ARBA:ARBA00032095};
GN Name=CHUK {ECO:0000313|Ensembl:ENSOANP00000053135.1};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000053135.1, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000053135.1}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000053135.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSOANP00000053135.1}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000053135.1};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[I-kappa-B protein] + ATP = O-phospho-L-seryl-[I-
CC kappa-B protein] + ADP + H(+); 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 Evidence={ECO:0000256|ARBA:ARBA00048789};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_028936882.1; XM_029081049.2.
DR RefSeq; XP_028936883.1; XM_029081050.2.
DR RefSeq; XP_028936884.1; XM_029081051.2.
DR RefSeq; XP_028936885.1; XM_029081052.2.
DR RefSeq; XP_028936886.1; XM_029081053.2.
DR RefSeq; XP_028936887.1; XM_029081054.2.
DR AlphaFoldDB; A0A6I8PEK0; -.
DR FunCoup; A0A6I8PEK0; 2239.
DR Ensembl; ENSOANT00000068284.1; ENSOANP00000053135.1; ENSOANG00000002485.3.
DR GeneID; 100082351; -.
DR KEGG; oaa:100082351; -.
DR CTD; 1147; -.
DR GeneTree; ENSGT00950000182937; -.
DR InParanoid; A0A6I8PEK0; -.
DR OMA; FILMDHI; -.
DR OrthoDB; 267381at2759; -.
DR Proteomes; UP000002279; Unplaced.
DR Bgee; ENSOANG00000002485; Expressed in endometrium and 8 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008385; C:IkappaB kinase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008384; F:IkappaB kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:1990459; F:transferrin receptor binding; IEA:Ensembl.
DR GO; GO:0006914; P:autophagy; IEA:Ensembl.
DR GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IBA:GO_Central.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IBA:GO_Central.
DR CDD; cd14039; STKc_IKK_alpha; 1.
DR CDD; cd17046; Ubl_IKKA_like; 1.
DR FunFam; 1.20.1270.250:FF:000001; Inhibitor of nuclear factor kappa-B kinase subunit alpha; 1.
DR FunFam; 3.10.20.90:FF:000061; Inhibitor of nuclear factor kappa-B kinase subunit alpha; 1.
DR FunFam; 1.10.510.10:FF:000147; Inhibitor of nuclear factor kappa-B kinase subunit beta; 1.
DR Gene3D; 1.20.1270.250; -; 1.
DR Gene3D; 6.10.250.2110; -; 1.
DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041185; IKBKB_SDD.
DR InterPro; IPR046375; IKBKB_SDD_sf.
DR InterPro; IPR051180; IKK.
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 PANTHER; PTHR22969; IKB KINASE; 1.
DR PANTHER; PTHR22969:SF13; INHIBITOR OF NUCLEAR FACTOR KAPPA-B KINASE SUBUNIT ALPHA; 1.
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; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..302
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 745 AA; 84758 MW; FD021DFF11742230 CRC64;
MERPPGLRPP VSGPWEMRER LGTGGFGNVS LYQHRDLGDK IAIKACRQEL SAKNKDRWCH
EIQIMKKLNH PNVVTACDVP EEMNFLVNDV PLLAMEYCSG GDLRKLLNKT ENCCGLKESQ
ILSLLSDIGS GIQYLHENRI IHRDLKPENI VLQNVDGKVI HKIIDLGYAK DLDQGSLCTS
FVGTLQYLAP ELFENKPYTA TVDYWSFGTM VFEGIVGYRP FLHHLQPFMW HEKIKKKDPK
HIFASEEMSG EVRFSSHLPQ PNSLCRLIVE PMENWLQLML NWDPQQRGGG IDSSTKQPRC
FLLMDQILHL KIVHILNMTS AKIISFLLLP DESLHSLQSR IEQETGISTG TQELLLEMGI
SLDPRKPASQ CVIDGVRGWD SYMVYLFDKS KIVYEGPFAS RSLSDCVNYI VQDSKIQLPI
TQLRKVWAEA VHYVSGLKED YSRLFQGQRA AMLSLLRYNA NLTKMKNTMI SASQQLKAKL
QFFHQSIQLD LDKYSDQMAY GISSEKMLKA WKEMEEKAIH CAQAGDIGYL DEQIMTLHTE
IVELQRSPYA RRQGDVMETL EQKAIDLYKQ LKHRSPDHSY SDSTEMVKII VQTVQSQDRV
LKELFGHLSK LLGCKQKIID LLPKVEVALN NIKEADNTVM LMQGKRQREI WHLLKIACTQ
SSARSLVGSS LEGAVPPPTP AWLPASATGT VPHPFSSLVT PKDGENFTQM IEENLNYLGC
FSTIIREAKE EQGNSMMSLD WSWLK
//