ID F1S8V5_PIG Unreviewed; 594 AA.
AC F1S8V5; F1S8V4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 4.
DT 27-MAR-2024, entry version 75.
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=Nuclear factor NF-kappa-B inhibitor kinase alpha {ECO:0000256|ARBA:ARBA00032095};
GN Name=CHUK {ECO:0000313|Ensembl:ENSSSCP00000011239.5,
GN ECO:0000313|VGNC:VGNC:86688};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000011239.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000011239.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000011239.5,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000011239.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00023939};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; F1S8V5; -.
DR STRING; 9823.ENSSSCP00000011239; -.
DR PaxDb; 9823-ENSSSCP00000029824; -.
DR Ensembl; ENSSSCT00000011540.5; ENSSSCP00000011239.5; ENSSSCG00000010548.6.
DR VGNC; VGNC:86688; CHUK.
DR eggNOG; KOG4250; Eukaryota.
DR GeneTree; ENSGT00950000182937; -.
DR HOGENOM; CLU_000288_101_2_1; -.
DR InParanoid; F1S8V5; -.
DR OMA; DINAACK; -.
DR Reactome; R-SSC-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-SSC-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-SSC-202424; Downstream TCR signaling.
DR Reactome; R-SSC-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-SSC-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-SSC-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-SSC-5357956; TNFR1-induced NF-kappa-B signaling pathway.
DR Reactome; R-SSC-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-SSC-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-SSC-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-SSC-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR Reactome; R-SSC-9020702; Interleukin-1 signaling.
DR Reactome; R-SSC-933542; TRAF6 mediated NF-kB activation.
DR Reactome; R-SSC-937039; IRAK1 recruits IKK complex.
DR Reactome; R-SSC-937041; IKK complex recruitment mediated by RIP1.
DR Reactome; R-SSC-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR Reactome; R-SSC-9758274; Regulation of NF-kappa B signaling.
DR Reactome; R-SSC-9833482; PKR-mediated signaling.
DR ChiTaRS; CHUK; pig.
DR Proteomes; UP000008227; Chromosome 14.
DR Bgee; ENSSSCG00000010548; Expressed in metanephros cortex and 43 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:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
DR GO; GO:0098586; P:cellular response to virus; 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; IEA:Ensembl.
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 Gene3D; 1.20.1270.250; -; 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; 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; 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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
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 594 AA; 68098 MW; 7293D5FD26B5B2DF CRC64;
MERPPGLRPG AGGPWEMRER LGTGGFGNVC LYQHRELDLK IAIKSCRLEL STKNRERWCH
EIQIMKKLNH DNVVKACDVP EELNFLINDV PLLAMEYCSG GDLRKLLNKP ENCCGLKESQ
ILSLLSDIGS GIRYLHENKI IHRDLKPENI VLQDVGGKIL HKIIDLGYAK DVDQGSLCTS
FVGTLQYLAP ELFENKPYTA TVDYWSFGTM VFECIAGYRP FLHHLQPFTW HEKIKKKDPK
CIFACEEMTG EVRFSSHLPQ PNSLCSLIVE PMENWLQLML NWDPQQRGGP IDLTLKQPKC
FILMDHILNL KIVHILNMTS AKIISFLLPP DESLHSLQSR IERETGINTG SQELLSEMGI
SLDPRKPASQ CVLDGVRGCD SYMVYLFDKS KTVYEGPFAS RSLSDCVNYI VQDSKIQLPI
IQLRKVWAEA VHYVSGLKED YSRLFQGQRA AMLSLLRYNA NLTKMKNTLI SASQQLKAKL
EFFHKSIQLD LERYSEQMTY GISSEKMLKA WKEMEEKAIH YAEVGVIGYL EDQIMSLHTE
IMELQKSPYG RRQGDLMESL EQRAIDLYKQ LKHRPAGKTV FHSTQRHFRK PSLT
//
