TIGIT_MOUSE
ID TIGIT_MOUSE Reviewed; 249 AA.
AC P86176;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=T-cell immunoreceptor with Ig and ITIM domains;
DE AltName: Full=V-set and transmembrane domain-containing protein 3 {ECO:0000312|MGI:MGI:3642260};
DE Flags: Precursor;
GN Name=Tigit {ECO:0000312|MGI:MGI:3642260};
GN Synonyms=Vstm3 {ECO:0000312|MGI:MGI:3642260};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Binds with high affinity to the poliovirus receptor (PVR)
CC which causes increased secretion of IL10 and decreased secretion of
CC IL12B and suppresses T-cell activation by promoting the generation of
CC mature immunoregulatory dendritic cells. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer in cis; binds with high affinity to PVR, forming a
CC heterotetrameric assembly of two TIGIT and two PVR molecules. Binds
CC with lower affinity to NECTIN2 and NECTIN3 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q495A1};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q495A1}.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC {ECO:0000250|UniProtKB:Q495A1, ECO:0000305}.
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DR EMBL; AC120871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P86176; -.
DR SMR; P86176; -.
DR STRING; 10090.ENSMUSP00000093770; -.
DR GlyGen; P86176; 1 site.
DR iPTMnet; P86176; -.
DR PhosphoSitePlus; P86176; -.
DR EPD; P86176; -.
DR MaxQB; P86176; -.
DR PaxDb; P86176; -.
DR PRIDE; P86176; -.
DR ProteomicsDB; 259449; -.
DR UCSC; uc012afs.1; mouse.
DR MGI; MGI:3642260; Tigit.
DR eggNOG; ENOG502SQW2; Eukaryota.
DR InParanoid; P86176; -.
DR PhylomeDB; P86176; -.
DR PRO; PR:P86176; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P86176; protein.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:MGI.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; ISS:UniProtKB.
DR GO; GO:0050868; P:negative regulation of T cell activation; IMP:MGI.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR042948; TIGIT.
DR PANTHER; PTHR47734; PTHR47734; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..249
FT /note="T-cell immunoreceptor with Ig and ITIM domains"
FT /id="PRO_0000365029"
FT TOPO_DOM 29..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..127
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255"
FT REGION 35..45
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 182..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 234..239
FT /note="ITIM motif"
FT /evidence="ECO:0000250|UniProtKB:Q495A1"
FT COMPBIAS 193..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 249 AA; 26959 MW; 3945C69C3133BCC0 CRC64;
MHGWLLLVWV QGLIQAAFLA TAIGATAGTI DTKRNISAEE GGSVILQCHF SSDTAEVTQV
DWKQQDQLLA IYSVDLGWHV ASVFSDRVVP GPSLGLTFQS LTMNDTGEYF CTYHTYPGGI
YKGRIFLKVQ ESSDDRNGLA QFQTAPLGGT MAAVLGLICL MVTGVTVLAR KDKSIRMHSI
ESGLGRTEAE PQEWNLRSLS SPGSPVQTQT APAGPCGEQA EDDYADPQEY FNVLSYRSLE
SFIAVSKTG
