ID A0A383Z0H2_BALAS Unreviewed; 460 AA.
AC A0A383Z0H2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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|RefSeq:XP_007168399.1,
GN ECO:0000313|RefSeq:XP_007168400.1, ECO:0000313|RefSeq:XP_007168401.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007168399.1};
RN [1] {ECO:0000313|RefSeq:XP_007168399.1, ECO:0000313|RefSeq:XP_007168400.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007168399.1,
RC ECO:0000313|RefSeq:XP_007168400.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
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|ARBA:ARBA00001433,
CC 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|ARBA:ARBA00000775,
CC 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. {ECO:0000256|ARBA:ARBA00008718,
CC ECO:0000256|PIRNR:PIRNR038189}.
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DR RefSeq; XP_007168399.1; XM_007168337.1.
DR RefSeq; XP_007168400.1; XM_007168338.1.
DR RefSeq; XP_007168401.1; XM_007168339.1.
DR AlphaFoldDB; A0A383Z0H2; -.
DR STRING; 310752.A0A383Z0H2; -.
DR GeneID; 103013107; -.
DR KEGG; bacu:103013107; -.
DR CTD; 51135; -.
DR InParanoid; A0A383Z0H2; -.
DR OrthoDB; 2999496at2759; -.
DR Proteomes; UP000261681; Unplaced.
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:0045087; P:innate immune response; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08793; Death_IRAK4; 1.
DR CDD; cd14158; STKc_IRAK4; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR47989; OS01G0750732 PROTEIN; 1.
DR PANTHER; PTHR47989:SF62; OS05G0423500 PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038189; IRAK4; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR038189};
KW 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|RefSeq:XP_007168399.1};
KW Magnesium {ECO:0000256|PIRNR:PIRNR038189};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038189};
KW Receptor {ECO:0000313|RefSeq:XP_007168399.1,
KW ECO:0000313|RefSeq:XP_007168400.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR038189};
KW Transferase {ECO:0000256|PIRNR:PIRNR038189}.
FT DOMAIN 186..454
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 137..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 311
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038189-1"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038189-2"
FT BINDING 313..315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038189-2"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038189-2"
SQ SEQUENCE 460 AA; 51666 MW; B408DDD1DEDB2347 CRC64;
MNKPITASTY VRCLNLGLIR KLSDFIDPQE GWKKLAVAIK KPSGDDRYNQ FHIRRFEALL
QTGKSPTCEL LFDWGTTNCT VGDLVDLLVQ NEFFAPASLL LPDAVPKTVN TLPSKVPVTV
QQKHMPLYGK DRTSVISDEN TEQNYMPPDS SRPENRSLEV SDTRFHSFSF YELKDVTNNF
DERPISVGGN KMGEGGFGVV YKGYVNNRTV AVKKLAAMVD ISTEELKQQF DQEIKVMAKC
QHENLVELLG FSSDGDDLCL VYVYMPNGSL LDRLSCLDDT LPLSWCIRCK IAQGAANGLS
YLHENHHIHR DIKSANILLD EDFTAKISDF GLARASEKFA QTVLTSRIVG TTAYMAPEAL
RGEITAKSDI YSFGVVLLEI ITGLPAVDEH REPQLLLDIK EEIEDEEKTI EDYSDTKMND
IDSTSIETMY SVASQCLHEK KNKRPDIKKV QQLLQEMTAS
//
