ID A0A1S3WKE2_ERIEU Unreviewed; 719 AA.
AC A0A1S3WKE2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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|RefSeq:XP_016046848.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016046848.1};
RN [1] {ECO:0000313|RefSeq:XP_016046848.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_016046848.1; XM_016191362.1.
DR AlphaFoldDB; A0A1S3WKE2; -.
DR GeneID; 103119930; -.
DR CTD; 1147; -.
DR OrthoDB; 3949542at2759; -.
DR Proteomes; UP000079721; Unplaced.
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-UniRule.
DR GO; GO:0008384; F:IkappaB kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:UniProt.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_016046848.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
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 719 AA; 82124 MW; 667983B88B8867E6 CRC64;
MERPPGLRPG AGGPWEMRER LGTGGFGNVC LYQHRELDLK IAIKSCRLEL STKNRERWCH
EIQIMKKLDH ANVVKACDVP EELNFLINDV PLLAMEYCSG GDLRKLLNKP ENCCGLKESQ
ILSLLNDIGS GIRYLHENKI IHRDLKPENI VLQDVGGKIM HKIIDLGYAK DVDQGSLCTS
FVGTLQYLAP ELFENKPYTA TVDYWSFGTM VFECIAGYRP FLHHLQPFTW HEKIKKKDPK
CIFACEEMTG EVRFSSHLPQ PNSLCSLIVE PMENWLQLML SWDPQQRGGP VDVTLKQPRC
FVLMDYILNL KIVHILNMTS AKIISFLLPS DESLHSLQSR IERETGINTG SQELLSETGI
SLDPRKPASQ CVLDGVRGCD SYMVYLFDKS KTVYEGPFAS RSLSECVNYI VQDSKIQLPI
IQLRKVWAEA VNYVSGLKED YSRLFQGQRA AMLSLLRYNA NLTKMKNTLI SASQQLKAKL
EFFHKSIQLD LERYSEQMTY GISSEKMLKA WKEMEEKAIH YAEVGVIGYL EDQIMSLHTE
IMELQKSPYG RRQGDLMESL EQRAIDLYKQ LKHRPPDHSY SDSTDMVKII VHTVQSQDRV
LKELFGHLSK LLGCKQKIID LLPKVEMALS NIKEADNTVM FMQGKRQKEI WHLLKIACTQ
SSARSLVGSS LEGAVTPQTS AWQPPTSAER EIPLSCVGNF DTNDRRKYEL SWSLRHNYS
//