TCAM2_BOVIN
ID TCAM2_BOVIN Reviewed; 232 AA.
AC Q2LGB7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=TIR domain-containing adapter molecule 2;
DE Short=TICAM-2;
DE AltName: Full=TRIF-related adapter molecule;
GN Name=TICAM2; Synonyms=TRAM;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=16621030; DOI=10.1016/j.vetimm.2006.03.003;
RA Connor E.E., Cates E.A., Williams J.L., Bannerman D.D.;
RT "Cloning and radiation hybrid mapping of bovine toll-like receptor-4 (TLR-
RT 4) signaling molecules.";
RL Vet. Immunol. Immunopathol. 112:302-308(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as sorting adapter in different signaling pathways
CC to facilitate downstream signaling leading to type I interferon
CC induction. In TLR4 signaling, physically bridges TLR4 and TICAM1 and
CC functionally transmits signal to TICAM1 in early endosomes after
CC endocytosis of TLR4. In TLR2 signaling, physically bridges TLR2 and
CC MYD88 and is required for the TLR2-dependent movement of MYD88 to
CC endosomes following ligand engagement. Involved in IL-18 signaling and
CC is proposed to function as a sorting adapter for MYD88 in IL-18
CC signaling during adaptive immune response. Forms a complex with
CC RAB11FIP2 that is recruited to the phagosomes to promote the activation
CC of the actin-regulatory GTPases RAC1 and CDC42 and subsequent
CC phagocytosis of Gram-negative bacteria. {ECO:0000250|UniProtKB:Q86XR7}.
CC -!- SUBUNIT: Homodimer. Interacts with TLR4, TICAM1, IRF3 and IRF7 in
CC response to LPS. Interacts with IL1R1, IL1RAP, IRAK2, IRAK3 and TRAF6.
CC Interacts with protein kinase-inactive mutants of IRAK1 and IRAK4.
CC Isoform 1 interacts with isoform 2; the interaction occurs in late
CC endosomes and disrupts the interaction between isoform 1 and TICAM1.
CC Interacts with MYD88; the interaction decreases after IL-18 stimulation
CC in a time-dependent manner. Interacts with IL18R1 and IL18RAP.
CC Interacts with TLR2. Interacts with RAB11FIP2.
CC {ECO:0000250|UniProtKB:Q86XR7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}. Cell membrane {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250}. Early endosome {ECO:0000250}. Late endosome
CC {ECO:0000250}. Cell projection, phagocytic cup
CC {ECO:0000250|UniProtKB:Q86XR7}. Note=Localized to the plasma membrane
CC as a result of myristoylation. {ECO:0000250}.
CC -!- DOMAIN: The TIR domain mediates the interaction with TRAF6 and MYD88.
CC {ECO:0000250|UniProtKB:Q86XR7}.
CC -!- PTM: Myristoylated. Required for membrane association which is critical
CC for its ability to initiate efficient signaling.
CC {ECO:0000250|UniProtKB:Q86XR7}.
CC -!- PTM: Phosphorylated by PRKCE in response to LPS. Phosphorylation is
CC essential for its function. It is depleted from the membrane upon
CC phosphorylation. Tyrosine phosphorylation is inhibited by phosphatase
CC PTPN4. {ECO:0000250|UniProtKB:Q86XR7}.
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DR EMBL; DQ319071; ABC47874.1; -; mRNA.
DR EMBL; BC118338; AAI18339.1; -; mRNA.
DR RefSeq; NP_001039921.1; NM_001046456.1.
DR RefSeq; XP_005211269.1; XM_005211212.3.
DR RefSeq; XP_010807135.1; XM_010808833.2.
DR AlphaFoldDB; Q2LGB7; -.
DR SMR; Q2LGB7; -.
DR STRING; 9913.ENSBTAP00000003042; -.
DR PaxDb; Q2LGB7; -.
DR PRIDE; Q2LGB7; -.
DR Ensembl; ENSBTAT00000003042; ENSBTAP00000003042; ENSBTAG00000002357.
DR GeneID; 539350; -.
DR KEGG; bta:539350; -.
DR CTD; 353376; -.
DR VEuPathDB; HostDB:ENSBTAG00000002357; -.
DR VGNC; VGNC:55148; TICAM2.
DR eggNOG; KOG1693; Eukaryota.
DR GeneTree; ENSGT00940000164712; -.
DR HOGENOM; CLU_094608_0_0_1; -.
DR InParanoid; Q2LGB7; -.
DR OMA; SAWTIIL; -.
DR OrthoDB; 1351613at2759; -.
DR TreeFam; TF336953; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000002357; Expressed in prostate gland and 102 other tissues.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
DR GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; ISS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:2000494; P:positive regulation of interleukin-18-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; ISS:UniProtKB.
DR GO; GO:0070671; P:response to interleukin-12; IEA:Ensembl.
DR GO; GO:0035669; P:TRAM-dependent toll-like receptor 4 signaling pathway; ISS:UniProtKB.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR015720; Emp24-like.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR Pfam; PF13676; TIR_2; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50104; TIR; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cytoplasm; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Immunity; Inflammatory response; Innate immunity;
KW Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q86XR7"
FT CHAIN 2..232
FT /note="TIR domain-containing adapter molecule 2"
FT /id="PRO_0000317688"
FT DOMAIN 70..226
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 164
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q86XR7"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q86XR7"
SQ SEQUENCE 232 AA; 26511 MW; 01570A48D02C8186 CRC64;
MGIGKSKMDP CHLSVPWGKS QSVDTSQSHH MSDSKQSEEI SLHGDAVCSS TAEMPAEEQE
GVEERPEEDT EEEVFLKFVI LHAEEDTGEA LRVQSLLEND FGIKPGIIFA EMPCGRQHLQ
NLDDAVNGSA WTILLLTENF LRDTWCKFQF YSSLMNSVNR QHKYNSVIPM RPLNNPLPRE
RTPFALRTIN ALEEESRGFP TQVERIFQES VYRIQQAIWK ETRNTVQRQS VA
