TACT_MOUSE
ID TACT_MOUSE Reviewed; 602 AA.
AC Q3U0X8; Q7TMW0; Q8C9U6; Q99M67;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
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 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 [MRNA].
RC STRAIN=BALB/cJ;
RA Saito H.;
RT "Mouse homolog of CD96/Tactile.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6NCr;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY029156; AAK31788.1; -; mRNA.
DR EMBL; AK040539; BAC30620.1; -; mRNA.
DR EMBL; AK156470; BAE33723.1; -; mRNA.
DR EMBL; BC052865; AAH52865.1; -; mRNA.
DR CCDS; CCDS37348.1; -.
DR RefSeq; NP_115854.2; NM_032465.2.
DR PDB; 7S11; X-ray; 2.58 A; C/D/E/F=24-138.
DR PDB; 7S13; X-ray; 2.12 A; C/D=21-138.
DR PDBsum; 7S11; -.
DR PDBsum; 7S13; -.
DR AlphaFoldDB; Q3U0X8; -.
DR SMR; Q3U0X8; -.
DR STRING; 10090.ENSMUSP00000023336; -.
DR GlyGen; Q3U0X8; 16 sites.
DR iPTMnet; Q3U0X8; -.
DR PhosphoSitePlus; Q3U0X8; -.
DR EPD; Q3U0X8; -.
DR PaxDb; Q3U0X8; -.
DR PRIDE; Q3U0X8; -.
DR ProteomicsDB; 259341; -.
DR Antibodypedia; 32434; 330 antibodies from 33 providers.
DR DNASU; 84544; -.
DR Ensembl; ENSMUST00000023336; ENSMUSP00000023336; ENSMUSG00000022657.
DR GeneID; 84544; -.
DR KEGG; mmu:84544; -.
DR UCSC; uc007zjf.2; mouse.
DR CTD; 10225; -.
DR MGI; MGI:1934368; Cd96.
DR VEuPathDB; HostDB:ENSMUSG00000022657; -.
DR eggNOG; ENOG502QWNP; Eukaryota.
DR GeneTree; ENSGT00390000003446; -.
DR HOGENOM; CLU_033543_1_0_1; -.
DR InParanoid; Q3U0X8; -.
DR OMA; QHGFYCA; -.
DR OrthoDB; 1115066at2759; -.
DR PhylomeDB; Q3U0X8; -.
DR TreeFam; TF336934; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 84544; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Cd96; mouse.
DR PRO; PR:Q3U0X8; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3U0X8; protein.
DR Bgee; ENSMUSG00000022657; Expressed in thymus and 46 other tissues.
DR Genevisible; Q3U0X8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0002728; P:negative regulation of natural killer cell cytokine production; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
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 InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR15317; PTHR15317; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..602
FT /note="T-cell surface protein tactile"
FT /id="PRO_0000313891"
FT TOPO_DOM 22..536
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..134
FT /note="Ig-like V-type 1"
FT DOMAIN 138..244
FT /note="Ig-like V-type 2"
FT DOMAIN 250..355
FT /note="Ig-like C2-type"
FT REGION 402..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..474
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 100
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 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 160..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 271..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 33
FT /note="V -> A (in Ref. 2; BAC30620)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="N -> D (in Ref. 2; BAC30620)"
FT /evidence="ECO:0000305"
FT CONFLICT 374..375
FT /note="ST -> Y (in Ref. 1; AAK31788)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="G -> A (in Ref. 3; AAH52865)"
FT /evidence="ECO:0000305"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:7S13"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:7S13"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:7S13"
FT STRAND 52..72
FT /evidence="ECO:0007829|PDB:7S13"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:7S13"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:7S13"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:7S13"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:7S13"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:7S13"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:7S13"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:7S13"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:7S13"
FT STRAND 126..136
FT /evidence="ECO:0007829|PDB:7S13"
SQ SEQUENCE 602 AA; 67133 MW; 62B26F60EC17B33D CRC64;
MGRKWTYCVV YTIIQIQFFR GVWEELFNVG DDVYALPGSD INLTCQTKEK NFLVQMQWSK
VTDKNDMIAL YHPQYGLYCG QEHACESQVA ATETEKGVTN WTLYLRNISS ALGGKYECIF
TLYPEGIKTT VYNLIVEPYT QDEHNYTIEI ETNRTLEIPC FQNTSSEIPP RFTFSWLVEK
DGVEEVLFTH HHHVNNSTSF KGRIRLGGDY RLHLSPVQIQ DDGRTFSCHL TVNPLKAWKM
STTVKVFAKP EILMTVENST MDVLGERVFT CLLKNVFPKA NITWFIDGRF LQGNEEGIYI
TNEEKNCSSG FWELKSVLTR MHSGPSQSNN MTAWCMALSP GPRNKMWNTS SQPITVSFDS
VIAPTKHLPT VTGSTLGTQP FSDAGVSPTG YLATPSVTIV DENGLTPDAT PQTSNSSMTT
KDGNYLEASS GTDAKNSSRA AASSKSGSWP FPFTSPPEWH SLPGTSTGPQ EPDSPVSWIP
SEVHTSAPLD ASLAPHDTII STTTEFPNVL TTANGTTKID HGPITSIIVN QPSDGMSWPV
LVAALLFFCT LLFGLGVRKW YRYQNEIMER PPPFKPPPPP IKYTYIQEPI GCDLCCHEME
VL
