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MYD88_PIG
ID   MYD88_PIG               Reviewed;         293 AA.
AC   A2TF48; A7UL70; A8I488; B1B361; C6ZCT2;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Myeloid differentiation primary response protein MyD88;
GN   Name=MYD88;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Peyer patch;
RX   PubMed=17976317;
RA   Tohno M., Shimazu T., Aso H., Kawai Y., Saito T., Kitazawa H.;
RT   "Molecular cloning and functional characterization of porcine MyD88
RT   essential for TLR signaling.";
RL   Cell. Mol. Immunol. 4:369-376(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li Q., Li X., Zhu L., Chen L., Li M., Wu X.;
RT   "Molecular cloning and tissue-specific expression of porcine myeloid
RT   differentiation primary response gene 88 (MYD88).";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Li K., Li X., Liu H., Yang S., Tang Z., Ma Y., Chu M.;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   He Y., Wang D., Jiang Y., Fang L., Chen H., Xiao S.;
RT   "Molecular cloning and sequence analysis of porcine myeloid differentiation
RT   primary response gene 88 (MYD88).";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 58-214.
RX   PubMed=17330086; DOI=10.1038/sj.gt.3302930;
RA   Alves M.P., Neuhaus V., Guzylack-Piriou L., Ruggli N., McCullough K.C.,
RA   Summerfield A.;
RT   "Toll-like receptor 7 and MyD88 knockdown by lentivirus-mediated RNA
RT   interference to porcine dendritic cell subsets.";
RL   Gene Ther. 14:836-844(2007).
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 (By
CC       similarity). {ECO:0000250|UniProtKB:P22366,
CC       ECO:0000250|UniProtKB:Q99836}.
CC   -!- SUBUNIT: Homodimer. Also forms heterodimers with TIRAP. Binds to TLR2,
CC       TLR4, IRAK1, IRAK2 and IRAK4 via their respective TIR domains.
CC       Interacts with IL18R1. Interacts with BMX, IL1RL1, IKBKE and IRF7.
CC       Interacts with LRRFIP1 and LRRFIP2; this interaction positively
CC       regulates Toll-like receptor (TLR) signaling in response to agonist.
CC       Interacts with FLII. LRRFIP1 and LRRFIP2 compete with FLII for MYD88-
CC       binding. Interacts with IRF1. Upon IL1B treatment, forms a complex with
CC       PELI1, IRAK1, IRAK4 and TRAF6; this complex recruits MAP3K7/TAK1, TAB1
CC       and TAB2 to mediate NF-kappa-B activation. Direct binding of SMAD6 to
CC       PELI1 prevents the complex formation and hence negatively regulates
CC       IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression.
CC       May interact with PIK3AP1. Interacts (via TIR domain) with DHX9 (via
CC       H2A and OB-fold regions); this interaction is direct. Interacts with
CC       OTUD4 deubiquitinase; the interaction is direct.
CC       {ECO:0000250|UniProtKB:Q99836}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99836}. Nucleus
CC       {ECO:0000250|UniProtKB:Q99836}.
CC   -!- TISSUE SPECIFICITY: Expressed in esophagus, duodenum, jejenum, ileum,
CC       ileal Peyer patches, mesenteric lymph node, colon and spleen.
CC       {ECO:0000269|PubMed:17976317}.
CC   -!- DOMAIN: The intermediate domain (ID) is required for the
CC       phosphorylation and activation of IRAK. {ECO:0000250|UniProtKB:P22366}.
CC   -!- PTM: Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination. OTUD4
CC       specifically hydrolyzes 'Lys-63'-linked polyubiquitinated MYD88.
CC       {ECO:0000250|UniProtKB:Q99836}.
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DR   EMBL; AB292176; BAG12314.1; -; mRNA.
DR   EMBL; EF198416; ABM90642.1; -; mRNA.
DR   EMBL; EU056736; ABW74617.1; -; mRNA.
DR   EMBL; EU056737; ABW74618.1; -; Genomic_DNA.
DR   EMBL; EU077229; ABU54860.1; -; mRNA.
DR   EMBL; EU155133; ABV91305.1; -; mRNA.
DR   RefSeq; NP_001093393.1; NM_001099923.1.
DR   AlphaFoldDB; A2TF48; -.
DR   SMR; A2TF48; -.
DR   STRING; 9823.ENSSSCP00000011996; -.
DR   PaxDb; A2TF48; -.
DR   PRIDE; A2TF48; -.
DR   GeneID; 396646; -.
DR   KEGG; ssc:396646; -.
DR   CTD; 4615; -.
DR   eggNOG; ENOG502QWKI; Eukaryota.
DR   HOGENOM; CLU_045884_0_0_1; -.
DR   InParanoid; A2TF48; -.
DR   OrthoDB; 890418at2759; -.
DR   TreeFam; TF326264; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; A2TF48; SS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0070976; F:TIR domain binding; IEA:InterPro.
DR   GO; GO:0035325; F:Toll-like receptor binding; IBA:GO_Central.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:InterPro.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR   GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB.
DR   GO; GO:0008063; P:Toll signaling pathway; IBA:GO_Central.
DR   GO; GO:0034158; P:toll-like receptor 8 signaling pathway; ISS:UniProtKB.
DR   CDD; cd08312; Death_MyD88; 1.
DR   Gene3D; 1.10.533.10; -; 1.
DR   Gene3D; 3.40.50.10140; -; 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; PTHR15079; 1.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF01582; TIR; 1.
DR   PIRSF; PIRSF037756; MyD88; 1.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00255; TIR; 1.
DR   SUPFAM; SSF47986; SSF47986; 1.
DR   SUPFAM; SSF52200; SSF52200; 1.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS50104; TIR; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Immunity; Inflammatory response; Innate immunity; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..293
FT                   /note="Myeloid differentiation primary response protein
FT                   MyD88"
FT                   /id="PRO_0000393136"
FT   DOMAIN          32..109
FT                   /note="Death"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT   DOMAIN          156..290
FT                   /note="TIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   REGION          110..152
FT                   /note="Intermediate domain"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99836"
FT   CONFLICT        3
FT                   /note="A -> E (in Ref. 1; BAG12314 and 3; ABW74617/
FT                   ABW74618)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="I -> T (in Ref. 2; ABM90642)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="V -> A (in Ref. 1; BAG12314)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   293 AA;  33254 MW;  3B893B610B7E9E76 CRC64;
     MAAGGSGAES APPTPSMSSL PLAALNVRVR HRLSLFLNVR TQVAADWTGL AEEMNFEYLE
     IRRLETHPDP TRSLLDDWQG RPGASVGRLL ELLAKLGRDD VLVELGPSIE EDCRKYILKQ
     QQEAAEKPLQ VDSVDSSIPW MSGITIRDDP LGQMPEHFDA FICYCPSDIQ FVQEMIRQLE
     QTNYRLKLCV SDRDVLPGTC VWSIASELIE KRCRRMVVVV SDDYLQSKEC DFQTKFALSL
     SPGAHQKRLI PVKYKSMKKE FPSILRFITV CDYTNPCTKS WFWTRLARAL SLP
 
 
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