ID K7D5W8_PANTR Unreviewed; 309 AA.
AC K7D5W8; A0A2J8NQC5; A0A8I3B333;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Myeloid differentiation primary response protein MyD88 {ECO:0000256|ARBA:ARBA00021472, ECO:0000256|PIRNR:PIRNR037756};
GN Name=MYD88 {ECO:0000313|EMBL:JAA07954.1};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA07954.1};
RN [1] {ECO:0000313|EMBL:JAA07954.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA07954.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA41358.1}, Skin {ECO:0000313|EMBL:JAA24115.1}, and
RC Smooth vascular {ECO:0000313|EMBL:JAA17307.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adapter protein involved in the Toll-like receptor and IL-1
CC receptor signaling pathway in the innate immune response. Acts via
CC IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation,
CC cytokine secretion and the inflammatory response. Increases IL-8
CC transcription. Involved in IL-18-mediated signaling pathway. Activates
CC IRF1 resulting in its rapid migration into the nucleus to mediate an
CC efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. Upon TLR8
CC activation by GU-rich single-stranded RNA (GU-rich RNA) derived from
CC viruses, induces IL1B release through NLRP3 inflammasome activation (By
CC similarity). MyD88-mediated signaling in intestinal epithelial cells is
CC crucial for maintenance of gut homeostasis and controls the expression
CC of the antimicrobial lectin REG3G in the small intestine.
CC {ECO:0000256|ARBA:ARBA00037083}.
CC -!- SUBUNIT: Homodimer. Also forms heterodimers with TIRAP. Binds to TLR2,
CC TLR4, IRAK1, IRAK2 and IRAK4 via their respective TIR domains.
CC {ECO:0000256|PIRNR:PIRNR037756}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR037756}.
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DR EMBL; GABC01003384; JAA07954.1; -; mRNA.
DR EMBL; GABF01004838; JAA17307.1; -; mRNA.
DR EMBL; GABD01008985; JAA24115.1; -; mRNA.
DR EMBL; GABE01003381; JAA41358.1; -; mRNA.
DR AlphaFoldDB; K7D5W8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070976; F:TIR domain binding; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:InterPro.
DR CDD; cd08312; Death_MyD88; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR034249; MyD88_Death.
DR InterPro; IPR017281; Myelin_different_resp_MyD88.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR15079; MYD88; 1.
DR PANTHER; PTHR15079:SF3; MYELOID DIFFERENTIATION PRIMARY RESPONSE PROTEIN MYD88; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF13676; TIR_2; 1.
DR PIRSF; PIRSF037756; MyD88; 1.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS50104; TIR; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR037756};
KW Immunity {ECO:0000256|PIRNR:PIRNR037756};
KW Inflammatory response {ECO:0000256|PIRNR:PIRNR037756};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 45..122
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
FT DOMAIN 172..306
FT /note="TIR"
FT /evidence="ECO:0000259|PROSITE:PS50104"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR037756-1"
SQ SEQUENCE 309 AA; 34617 MW; D3A37ECF624F77E2 CRC64;
MRPDRAEAPG PPAMAAGGPA AGSAAPISST SSLPLAALNM RVRRRLSLFL NVRTQVAADW
TALAEEMDFE YLEIRQLETH ADPTGRLLDA WQGRPGASVG RLLELLTKLG RDDVLLELGP
SIEEDCQKYI LKQQQEEAEK PLQVAAVDSS VPRTAELAGI TTLDDPLGHM PERFDAFICY
CPSDIQFVQE MIRQLEQTNY RLKLCVSDRD VLPGTCVWSI ASELIEKRCR RMVVVVSDDY
LQSKECDFQT KFALSLSPGA HQKRLIPIKY KAMKKEFPSI LRFITVCDYT NPCTKSWFWT
RLAKALSLP
//