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Database: UniProt
Entry: A0A0Q3TQK6_AMAAE
LinkDB: A0A0Q3TQK6_AMAAE
Original site: A0A0Q3TQK6_AMAAE 
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
//
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