ID A0A0Q3TQK6_AMAAE Unreviewed; 697 AA.
AC A0A0Q3TQK6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE RecName: Full=TIR domain-containing adapter molecule 1 {ECO:0000256|PIRNR:PIRNR037744};
DE Short=TICAM-1 {ECO:0000256|PIRNR:PIRNR037744};
GN ORFNames=AAES_66587 {ECO:0000313|EMBL:KQK82830.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK82830.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK82830.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK82830.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in innate immunity against invading pathogens.
CC Adapter used by TLR3, TLR4 (through TICAM2) and TLR5 to mediate NF-
CC kappa-B and interferon-regulatory factor (IRF) activation, and to
CC induce apoptosis. Ligand binding to these receptors results in TRIF
CC recruitment through its TIR domain. Distinct protein-interaction motifs
CC allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which
CC in turn, lead to the activation of transcription factors IRF3 and IRF7,
CC NF-kappa-B and FADD respectively. Phosphorylation by TBK1 on the pLxIS
CC motif leads to recruitment and subsequent activation of the
CC transcription factor IRF3 to induce expression of type I interferon and
CC exert a potent immunity against invading pathogens. Component of a
CC multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of
CC viral double-stranded RNA (dsRNA) and plays a role in the activation of
CC a cascade of antiviral responses including the induction of pro-
CC inflammatory cytokines. {ECO:0000256|PIRNR:PIRNR037744}.
CC -!- SUBUNIT: Homodimer. Found in a multi-helicase-TICAM1 complex at least
CC composed of DHX36, DDX1, DDX21 and TICAM1.
CC {ECO:0000256|PIRNR:PIRNR037744}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC {ECO:0000256|PIRNR:PIRNR037744}. Cytoplasm, cytosol
CC {ECO:0000256|PIRNR:PIRNR037744}. Mitochondrion
CC {ECO:0000256|PIRNR:PIRNR037744}.
CC -!- DOMAIN: The N-terminal region is essential for activation of the IFNB
CC promoter activity. {ECO:0000256|PIRNR:PIRNR037744}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK82830.1}.
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DR EMBL; LMAW01001703; KQK82830.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3TQK6; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-UniRule.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-UniRule.
DR GO; GO:0043330; P:response to exogenous dsRNA; IEA:UniProtKB-UniRule.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; IEA:InterPro.
DR Gene3D; 1.25.40.780; -; 1.
DR Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 1.
DR InterPro; IPR025735; RHIM_dom.
DR InterPro; IPR046946; TCAM1/2.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR InterPro; IPR040886; TRIF_N.
DR PANTHER; PTHR47230; TIR DOMAIN-CONTAINING ADAPTER MOLECULE 1; 1.
DR PANTHER; PTHR47230:SF1; TIR DOMAIN-CONTAINING ADAPTER MOLECULE 1; 1.
DR Pfam; PF12721; RHIM; 1.
DR Pfam; PF17798; TRIF-NTD; 1.
DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR PROSITE; PS50104; TIR; 1.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|PIRNR:PIRNR037744};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR037744};
KW Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR037744};
KW Immunity {ECO:0000256|PIRNR:PIRNR037744};
KW Inflammatory response {ECO:0000256|PIRNR:PIRNR037744};
KW Innate immunity {ECO:0000256|PIRNR:PIRNR037744};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR037744};
KW Receptor {ECO:0000313|EMBL:KQK82830.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836}.
FT DOMAIN 433..600
FT /note="TIR"
FT /evidence="ECO:0000259|PROSITE:PS50104"
FT REGION 136..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 74885 MW; 67A811CFA2B056DF CRC64;
MAQSTPLQPS FEDVLHILSQ VPQEKLLNLK HKLKHLVFGP SSKXLQAMVL LALGQETKAR
ICLDALRDNR AAQYVHQTKL GAAGAQKDGE DLQPPXLDAG AMELLAQIYK VLVKEKLCXP
EAMEKACQAA SEACXGSKET APGPVNSIPP REQGEHGSAA SMGSGDNQQM LRSDAAGFLL
PATPNYVVRS SPVQIGIHSD LSRLSSPRSL RSXESSLENL SLPSHLEISA SPTAALRSQA
SRPERAQQPD GDRQSHGLQE TSCTSPSSQP TQVLRAENAP QASSCHPMVP VPDTQLPTMG
AVNQPGESSD VSSTVAANPQ AQKENTDKKQ GEKQSSTGLP ASRAAVDTGP APVSMEEPHM
PGDIPPNSAS ASISARSFPP PPTYSFXSTL PPPQGPRSSL PYPLRSHSSP SLAWPPPLQT
AXPAPTSEPE SGKFFTFVVL HASEDEIVAH RVKDLLENMG VPNGATLCED FAIAGRSHMT
CFQDAMENSA FIILLLTKNF PCDLCMFQTN TVLMESIMNP SKSDSVIPFI PQENPLEWSQ
IPAVLGGLTP LDEKSPGFSR TVQNTFTTSR INEKKDSWDL LQRKKLQLRE ERYRTLQNMA
ALNLGSIPPP AXQPXLLEQP PRPWWSLAGG GPRPARMGPP PVQPPSGHYN VLPGPGEIPP
LIIQNARMVQ IGNHNVMQVE TLTPGPEGTG EGSRQCV
//