IRAK2_RAT
ID IRAK2_RAT Reviewed; 624 AA.
AC Q4QQS0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Interleukin-1 receptor-associated kinase-like 2;
DE Short=IRAK-2;
GN Name=Irak2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Binds to the IL-1 type I receptor following IL-1 engagement,
CC triggering intracellular signaling cascades leading to transcriptional
CC up-regulation and mRNA stabilization. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MYD88. IL-1 stimulation leads to the formation
CC of a signaling complex which dissociates from the IL-1 receptor
CC following the binding of PELI1 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. Pelle subfamily. {ECO:0000305}.
CC -!- CAUTION: Asn-335 is present instead of the conserved Asp which is
CC expected to be an active site residue. {ECO:0000305}.
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DR EMBL; BC098060; AAH98060.1; -; mRNA.
DR RefSeq; NP_001020593.1; NM_001025422.1.
DR AlphaFoldDB; Q4QQS0; -.
DR SMR; Q4QQS0; -.
DR STRING; 10116.ENSRNOP00000034508; -.
DR iPTMnet; Q4QQS0; -.
DR PhosphoSitePlus; Q4QQS0; -.
DR PaxDb; Q4QQS0; -.
DR PRIDE; Q4QQS0; -.
DR Ensembl; ENSRNOT00000029819; ENSRNOP00000034508; ENSRNOG00000021817.
DR GeneID; 362418; -.
DR KEGG; rno:362418; -.
DR UCSC; RGD:1309584; rat.
DR CTD; 3656; -.
DR RGD; 1309584; Irak2.
DR eggNOG; KOG1187; Eukaryota.
DR GeneTree; ENSGT00940000159835; -.
DR HOGENOM; CLU_000288_173_0_1; -.
DR InParanoid; Q4QQS0; -.
DR OMA; ALSEWDW; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q4QQS0; -.
DR TreeFam; TF328924; -.
DR Reactome; R-RNO-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-RNO-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-RNO-9020702; Interleukin-1 signaling.
DR Reactome; R-RNO-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-RNO-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-RNO-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR PRO; PR:Q4QQS0; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000021817; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q4QQS0; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:RGD.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0001959; P:regulation of cytokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0070555; P:response to interleukin-1; ISO:RGD.
DR CDD; cd08795; Death_IRAK2; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR042151; Death_IRAK2.
DR InterPro; IPR033611; IRAK2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR24419:SF2; PTHR24419:SF2; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..624
FT /note="Interleukin-1 receptor-associated kinase-like 2"
FT /id="PRO_0000277562"
FT DOMAIN 13..94
FT /note="Death"
FT DOMAIN 210..475
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 508..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 337..340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 624 AA; 69237 MW; EF8995F30AB4FDD5 CRC64;
MACYIYQLPS WVLDDLCRNI DTLSEWDWMQ FASYVITDLT QLRKIKSMER VQGVSITREL
LWWWSMRQAT VQQLVDLLCH LELYRAAQIV LSWKPAPDSL SPLSAFPEAV KPGPVATSGR
NLKDDQKKGQ PVKPCSFLSS GTTMAGAQQQ ASCQRPCEED APCSLKTDVP DSLQSKYCST
SIPKQEKLLN LPGDRLFWSE ADIVQATEDF DQSHRISEGT FADIYRGQRN GVAFAFKRLR
EVTGSSPGSM DRFLQAEMQL CLRCCHPNIL PLLGFCTGRQ FHSLIYPYMA NGSLQDRLWA
QGDSDMLSWP QRASICSGLL LAVEHLHSLD IIHSNVKSAN VLLDQHLNPK LAHPVAHPCP
TNKKTKYTVM KTHLFQASAA YLPENFIRVG QLTKQVDIFS CGIVLAEVLT GIPAMDKDRS
PVYLKDLLLS EIPSNTSSVH SRKTSMGKVV VKEICQKHLE RKAGLLPEAC AETWATAVSV
CLRRREASLE EARVSMAGVE EQLRGQLSLP WSRVSEDTGS SSNTPEETDD VDNSSLSVPS
SVMVVSCARV SSPPPSMGNG TAQPSTSGRQ EADSSSEACA GPQPPQEATE TSWKIEINEA
KRRLMENILL YKEEKLDSVE LFGP
