ID Q540G0_MOUSE Unreviewed; 710 AA.
AC Q540G0;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=Irak1 {ECO:0000313|MGI:MGI:107420};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAO63012.1};
RN [1] {ECO:0000313|EMBL:AAO63012.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/c {ECO:0000313|EMBL:AAO63012.1};
RA Reichwald K., Petz U., Rosenthal A., Platzer M.;
RT "Transcript analysis of human and mouse orthologs.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. Pelle subfamily.
CC {ECO:0000256|ARBA:ARBA00008718}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY184362; AAO63012.1; -; mRNA.
DR RefSeq; NP_001171445.1; NM_001177974.1.
DR RefSeq; NP_032389.2; NM_008363.2.
DR AlphaFoldDB; Q540G0; -.
DR SMR; Q540G0; -.
DR Antibodypedia; 3845; 1274 antibodies from 47 providers.
DR DNASU; 16179; -.
DR GeneID; 16179; -.
DR KEGG; mmu:16179; -.
DR AGR; MGI:107420; -.
DR CTD; 3654; -.
DR MGI; MGI:107420; Irak1.
DR VEuPathDB; HostDB:ENSMUSG00000031392; -.
DR OMA; PIAIQIY; -.
DR OrthoDB; 2999496at2759; -.
DR BioGRID-ORCS; 16179; 1 hit in 80 CRISPR screens.
DR ChiTaRS; Irak1; mouse.
DR ExpressionAtlas; Q540G0; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR GO; GO:0045087; P:innate immune response; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR GO; GO:0010033; P:response to organic substance; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08794; Death_IRAK1; 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; IPR000488; Death_domain.
DR InterPro; IPR035533; Death_IRAK1.
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; PTHR47989; OS01G0750732 PROTEIN; 1.
DR PANTHER; PTHR47989:SF47; SERINE_THREONINE-PROTEIN KINASE PBL28-RELATED; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47986; DEATH domain; 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AAO63012.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000313|EMBL:AAO63012.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:AAO63012.1}.
FT DOMAIN 212..521
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 107..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 710 AA; 77269 MW; 8A501F002CD3EBD2 CRC64;
MAGGPGPGEP VVPGAQHFLY EVPPWVMCRF YKVMDALEPA DWCQFAALIV RDQTELRLCE
RSEQRTASVL WPWINRNARV ADLVHILTHL QLLRARDIIT AWHPPAPVVP PSTAAPRPSS
ISAGSEAGDW SPRKLQSSAS TFLSPAFPGS QTHSESELLQ VPLPVSLGPP LPSSAPSSTK
SSPESPVSGL QRAHPSPFCW PFCEISQGTC NFSEELRIGE GGFGCVYRAV MRNTTYAVKR
LKEEADLEWT MVKQSFLTEV EQLSRFRHPN IVDFAGYCAE SGLYCLVYGF LPNGSLEDQL
HLQTQACSPL SWPQRLDILL GTARAIQFLH QDSPSLIHGD IKSSNVLLDE RLMPKLGDFG
LARFSRFAGA KASQSSTVAR TSTVRGTLAY LPEEYIKTGR LAVDTDTFSF GVVILETLAG
QRAVRTQGAK TKYLKDLIED EAEEAGVTLK STQPTLWVGV ATDAWAAPIA AQIYKKHLDS
RPGPCPPQLG LALAQLACCC MHRRAKKRPP MTQVYKRLEG LQAGPPWELE VAGHGSPSPQ
ENSYMSTTGS AQSGDEPWQP LVVTTRAPAQ AAQQLQRSPN QPVESDESVP GLSATLHSWH
LTPGSHPSPA SFREASCTQG GTTRESSVRS SPGFQPTTME GSPTGSSSLL SSEPPQIIIN
PARQKMVQKL ALYEEGVLDS LQLLSSGFFP GLDLEPEKSQ GPEESDEFQS
//
