ID   Q7Z6A8_HUMAN            Unreviewed;       292 AA.
AC   Q7Z6A8;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Interleukin-1 receptor-associated kinase 4 {ECO:0000256|PIRNR:PIRNR038189};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038189};
GN   Name=IRAK4 {ECO:0000313|EMBL:AAP57089.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAP57089.1};
RN   [1] {ECO:0000313|EMBL:AAP57089.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12925671; DOI=10.1084/jem.20030701;
RA   Medvedev A.E., Lentschat A., Kuhns D.B., Blanco J.C.G., Salkowski C.,
RA   Zhang S., Arditi M., Gallin J.I., Vogel S.N.;
RT   "Distinct mutations in IRAK-4 confer hyporesponsiveness to
RT   lipopolysaccharide and interleukin-1 in a patient with recurrent bacterial
RT   infections.";
RL   J. Exp. Med. 198:521-531(2003).
CC   -!- FUNCTION: Serine/threonine-protein kinase that plays a critical role in
CC       initiating innate immune response against foreign pathogens.
CC       {ECO:0000256|PIRNR:PIRNR038189}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038189};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|PIRNR:PIRNR038189};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038189};
CC   -!- SUBUNIT: Associates with MYD88 and IRAK2 to form a ternary complex
CC       called the Myddosome. {ECO:0000256|PIRNR:PIRNR038189}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR038189}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. Pelle subfamily.
CC       {ECO:0000256|PIRNR:PIRNR038189}.
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DR   EMBL; AY283670; AAP57089.1; -; mRNA.
DR   AlphaFoldDB; Q7Z6A8; -.
DR   PeptideAtlas; Q7Z6A8; -.
DR   ChiTaRS; IRAK4; human.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071310; P:cellular response to organic substance; IEA:UniProt.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:UniProt.
DR   GO; GO:0031349; P:positive regulation of defense response; IEA:UniProt.
DR   GO; GO:0032103; P:positive regulation of response to external stimulus; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd08793; Death_IRAK4; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR017428; IRAK4.
DR   InterPro; IPR037970; IRAK4_Death.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR45647; OS02G0152300 PROTEIN; 1.
DR   PANTHER; PTHR45647:SF100; U-BOX DOMAIN-CONTAINING PROTEIN 33; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF038189; IRAK4; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR038189, ECO:0000256|PIRSR:PIRSR038189-
KW   2}; Cytoplasm {ECO:0000256|PIRNR:PIRNR038189};
KW   Immunity {ECO:0000256|PIRNR:PIRNR038189};
KW   Innate immunity {ECO:0000256|PIRNR:PIRNR038189};
KW   Kinase {ECO:0000256|PIRNR:PIRNR038189, ECO:0000313|EMBL:AAP57089.1};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR038189};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR038189,
KW   ECO:0000256|PIRSR:PIRSR038189-2}; Receptor {ECO:0000313|EMBL:AAP57089.1};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038189};
KW   Transferase {ECO:0000256|PIRNR:PIRNR038189}.
FT   DOMAIN          186..292
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038189-2"
SQ   SEQUENCE   292 AA;  32704 MW;  58F1708A63BD3BE5 CRC64;
     MNKPITPSTY VRCLNVGLIR KLSDFIDPQE GWKKLAVAIK KPSGDDRYNQ FHIRRFEALL
     QTGKSPTSEL LFDWGTTNCT AGDLVDLLIQ NEFFAPASLL LPDAVPKTAN TLPSKEAITV
     QQKQMPFCDK DRTLMTPVQN LEQSYMPPDS SSPENKSLEV SDTRFHSFSF YELKNVTNNF
     DERPISVGGN KMGEGGFGVV YKGYVNNTTV AVKKLAAMVD ITTEELKQQF DQEIKVMAKC
     QHENLVELLG FSSDGDDLCL VYVYMPNGSL LDRLSCLDGT PPLSWHMRCK IA
//