TACT_BOVIN
ID TACT_BOVIN Reviewed; 570 AA.
AC Q3MHP9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=T-cell surface protein tactile;
DE AltName: Full=Cell surface antigen CD96;
DE AltName: Full=T cell-activated increased late expression protein;
DE AltName: CD_antigen=CD96;
DE Flags: Precursor;
GN Name=CD96;
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 [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in adhesive interactions of activated T and
CC NK cells during the late phase of the immune response. Promotes NK
CC cell-target adhesion by interacting with PVR present on target cells.
CC May function at a time after T and NK cells have penetrated the
CC endothelium using integrins and selectins, when they are actively
CC engaging diseased cells and moving within areas of inflammation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PVR (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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DR EMBL; BC105154; AAI05155.1; -; mRNA.
DR RefSeq; NP_001030244.1; NM_001035072.2.
DR AlphaFoldDB; Q3MHP9; -.
DR STRING; 9913.ENSBTAP00000019209; -.
DR PaxDb; Q3MHP9; -.
DR GeneID; 509578; -.
DR KEGG; bta:509578; -.
DR CTD; 10225; -.
DR eggNOG; ENOG502QWNP; Eukaryota.
DR InParanoid; Q3MHP9; -.
DR OrthoDB; 1115066at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR042381; CD96.
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 PANTHER; PTHR15317; PTHR15317; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..570
FT /note="T-cell surface protein tactile"
FT /id="PRO_0000313890"
FT TOPO_DOM 22..504
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..125
FT /note="Ig-like V-type 1"
FT DOMAIN 156..222
FT /note="Ig-like V-type 2"
FT DOMAIN 253..359
FT /note="Ig-like C2-type"
FT REGION 373..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 163..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 274..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 570 AA; 63395 MW; D2D7C17638A2F5DB CRC64;
MEKKWTYCAV YSIIQMHLVR GIVEETFGAE EHIYALPGSD VNLTCQTQKK GILVQMQWSK
VTDKVDLLAV YHPQHGFYCD SKSACRSLVA FREPPGNVFE WTLYLRNVSS STTGKYECSF
TLYPEGIQTK IYSLKIQTNV AQEEWKNNHT IEIEINGTLE IPCFQNTSLE ISSVLTFAWL
VEDNGTQKTL TAGGHPISNS ALFKDRVRIG TDYRLYLSPV QIHDDGWKFS CHVVVRPGRV
LRSSTTVKVF AKPEIPMIVE NNSMDVIGER IFTCSLRNVF PTANLTWFIQ RSFPQGEREE
MYTTSEKRKN KDGFWELKSV LTSAYDNKPA HSNNLTIWCM ALSPAPGHKV WNSSSEKITF
FLGSLNPPID SPLNATESTL GTRPSLANSI SPTGYRTPSS TAHVDVSTST SNVILPSVQT
SNSDVPTRGF NYSWTSSGKD AKHSAPWMPS ETNSSPSSGA GSTLPGDIFT STTRASSEVP
TTANVSTKNN HITGTVISKP KDGMSWPVIV AALLLSCFVL FGLGVRKWCQ YQKEIMQRPP
PFKPPPPPIK YTCIQESIGS DLPCHELETL
