ID   IRAK2_PONAB             Reviewed;         625 AA.
AC   Q5R810;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Interleukin-1 receptor-associated kinase-like 2;
DE            Short=IRAK-2;
GN   Name=IRAK2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR859945; CAH92100.1; -; mRNA.
DR   AlphaFoldDB; Q5R810; -.
DR   SMR; Q5R810; -.
DR   STRING; 9601.ENSPPYP00000015274; -.
DR   eggNOG; KOG1187; Eukaryota.
DR   InParanoid; Q5R810; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; IEA:InterPro.
DR   GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0044093; P:positive regulation of molecular function; IEA:UniProt.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0001959; P:regulation of cytokine-mediated signaling pathway; IEA:InterPro.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   GO; GO:0010556; P:regulation of macromolecule biosynthetic process; IEA:UniProt.
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; Phosphoprotein; Reference proteome.
FT   CHAIN           1..625
FT                   /note="Interleukin-1 receptor-associated kinase-like 2"
FT                   /id="PRO_0000277561"
FT   DOMAIN          13..94
FT                   /note="Death"
FT   DOMAIN          210..503
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          111..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..539
FT                   /note="Polar residues"
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"
FT   MOD_RES         144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43187"
SQ   SEQUENCE   625 AA;  69578 MW;  6D25A1C184FEF41B CRC64;
     MACYIYQLPS WVLDDPCRNM DALSEWDWME FASYVITDLT QLRKIKSMER VQGVSITREL
     LWWWGMRQAT VRQLVDLLCR LELYRAAQII LNWKPAPEIR CPIPAFPDSV KPEKPLAASV
     KKAENEQEEG QPVRMATFPG PGSSPARAHQ PAFLQPPEED APHSLRTDLP TSSDSKDFST
     SIPKQEKLLS LAGDSLFWSE ADVVQATDDF NQNHKISQGT FADVYRGYRH GTPFVFKKLR
     ETACSSPGSI ERFFQAELQI CLRCCHPNVL PVLGFCAARQ FHSFIYPYMA NGSLQDRLQG
     QGGSDPLPWP QRVSICSGLL CAVEYLHGLE IIHSNVKSSN VLLDQNLTPK LAHPMAHLCP
     VNKRSKYTMM KTHLFRTSAA YLPEDFIRVG QLTKRVDIFS CGIVLAEVLT GIPAMDNNRS
     PVYLKDLLLS EIPSSTASPC SRKTGVENVM AKEICQKYLE KGAGRLPEDC AEALATAACL
     CLRKRNTSLQ EVRGSVAAVE EWLRGREMLL PWSGLSEGTG SSSNTPEETD DVDNSSLDAS
     SSVSVAPWAG AATPLLPTEN GEGRLRVIVR READSSSEAC VGPEPPQDVT ETSWQIDINE
     AKRKLMENIL LYKEEKLDSI ELFGP