TACT_HUMAN
ID TACT_HUMAN Reviewed; 585 AA.
AC P40200; Q5JPB3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 183.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1313846;
RA Wang P.L., O'Farrell S., Clayberger C., Krensky A.M.;
RT "Identification and molecular cloning of tactile. A novel human T cell
RT activation antigen that is a member of the Ig gene superfamily.";
RL J. Immunol. 148:2600-2608(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH PVR.
RX PubMed=15034010; DOI=10.4049/jimmunol.172.7.3994;
RA Fuchs A., Cella M., Giurisato E., Shaw A.S., Colonna M.;
RT "CD96 (tactile) promotes NK cell-target cell adhesion by interacting with
RT the poliovirus receptor (CD155).";
RL J. Immunol. 172:3994-3998(2004).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-277 AND ASN-278.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP VARIANT CSYN MET-280.
RX PubMed=17847009; DOI=10.1086/522014;
RA Kaname T., Yanagi K., Chinen Y., Makita Y., Okamoto N., Maehara H.,
RA Owan I., Kanaya F., Kubota Y., Oike Y., Yamamoto T., Kurosawa K.,
RA Fukushima Y., Bohring A., Opitz J.M., Yoshiura K., Niikawa N., Naritomi K.;
RT "Mutations in CD96, a member of the immunoglobulin superfamily, cause a
RT form of the C (Opitz trigonocephaly) syndrome.";
RL Am. J. Hum. Genet. 81:835-841(2007).
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.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PVR.
CC {ECO:0000269|PubMed:15034010}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P40200-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P40200-2; Sequence=VSP_029908;
CC -!- TISSUE SPECIFICITY: Expressed on normal T-cell lines and clones, and
CC some transformed T-cells, but no other cultured cell lines tested. It
CC is expressed at very low levels on activated B-cells.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels on peripheral T-cells and
CC is strongly up-regulated after activation, peaking 6 to 9 days after
CC the activating stimulus.
CC -!- DISEASE: C syndrome (CSYN) [MIM:211750]: A syndrome characterized by
CC trigonocephaly, severe intellectual disability, hypotonia, variable
CC cardiac defects, redundant skin, and dysmorphic facial features,
CC including upslanted palpebral fissures, epicanthal folds, depressed
CC nasal bridge, and low-set, posteriorly rotated ears.
CC {ECO:0000269|PubMed:17847009}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. A chromosomal aberration
CC involving CD96 has been found in a patient with C syndrome.
CC Translocation t(3;18)(q13.13;q12.1). CD96 gene was located at the
CC 3q13.13 breakpoint. Precise structural analysis around the breakpoint
CC showed that the gene was disrupted by the translocation in exon 5,
CC probably leading to premature termination or loss of expression of CD96
CC protein. No gene was detected at the chromosome 18 breakpoint.
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DR EMBL; M88282; AAA36662.1; -; mRNA.
DR EMBL; AL833681; CAI46155.1; -; mRNA.
DR EMBL; CH471052; EAW79698.1; -; Genomic_DNA.
DR CCDS; CCDS2958.1; -. [P40200-2]
DR CCDS; CCDS2959.1; -. [P40200-1]
DR PIR; A46462; A46462.
DR RefSeq; NP_005807.1; NM_005816.4. [P40200-2]
DR RefSeq; NP_937839.1; NM_198196.2. [P40200-1]
DR PDB; 6ARQ; X-ray; 2.88 A; A=21-139.
DR PDBsum; 6ARQ; -.
DR AlphaFoldDB; P40200; -.
DR SMR; P40200; -.
DR BioGRID; 115519; 16.
DR IntAct; P40200; 1.
DR STRING; 9606.ENSP00000283285; -.
DR GlyGen; P40200; 15 sites.
DR iPTMnet; P40200; -.
DR PhosphoSitePlus; P40200; -.
DR SwissPalm; P40200; -.
DR BioMuta; CD96; -.
DR DMDM; 161784352; -.
DR MassIVE; P40200; -.
DR PaxDb; P40200; -.
DR PeptideAtlas; P40200; -.
DR PRIDE; P40200; -.
DR ProteomicsDB; 55346; -. [P40200-1]
DR ProteomicsDB; 55347; -. [P40200-2]
DR ABCD; P40200; 19 sequenced antibodies.
DR Antibodypedia; 32434; 330 antibodies from 33 providers.
DR DNASU; 10225; -.
DR Ensembl; ENST00000283285.10; ENSP00000283285.5; ENSG00000153283.13. [P40200-1]
DR Ensembl; ENST00000352690.9; ENSP00000342040.3; ENSG00000153283.13. [P40200-2]
DR GeneID; 10225; -.
DR KEGG; hsa:10225; -.
DR MANE-Select; ENST00000352690.9; ENSP00000342040.3; NM_005816.5; NP_005807.1. [P40200-2]
DR UCSC; uc003dxw.4; human. [P40200-1]
DR CTD; 10225; -.
DR DisGeNET; 10225; -.
DR GeneCards; CD96; -.
DR HGNC; HGNC:16892; CD96.
DR HPA; ENSG00000153283; Tissue enhanced (lymphoid).
DR MalaCards; CD96; -.
DR MIM; 211750; phenotype.
DR MIM; 606037; gene.
DR neXtProt; NX_P40200; -.
DR OpenTargets; ENSG00000153283; -.
DR Orphanet; 1308; C syndrome.
DR PharmGKB; PA437; -.
DR VEuPathDB; HostDB:ENSG00000153283; -.
DR eggNOG; ENOG502QWNP; Eukaryota.
DR GeneTree; ENSGT00390000003446; -.
DR HOGENOM; CLU_033543_1_0_1; -.
DR InParanoid; P40200; -.
DR OMA; QHGFYCA; -.
DR OrthoDB; 1115066at2759; -.
DR PhylomeDB; P40200; -.
DR TreeFam; TF336934; -.
DR PathwayCommons; P40200; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; P40200; -.
DR BioGRID-ORCS; 10225; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; CD96; human.
DR GenomeRNAi; 10225; -.
DR Pharos; P40200; Tbio.
DR PRO; PR:P40200; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P40200; protein.
DR Bgee; ENSG00000153283; Expressed in granulocyte and 110 other tissues.
DR ExpressionAtlas; P40200; baseline and differential.
DR Genevisible; P40200; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0002728; P:negative regulation of natural killer cell cytokine production; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
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; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion;
KW Chromosomal rearrangement; Craniosynostosis; Disease variant;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..585
FT /note="T-cell surface protein tactile"
FT /id="PRO_0000014970"
FT TOPO_DOM 22..519
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..125
FT /note="Ig-like V-type 1"
FT DOMAIN 156..238
FT /note="Ig-like V-type 2"
FT DOMAIN 269..375
FT /note="Ig-like C2-type"
FT REGION 385..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
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 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..118
FT /evidence="ECO:0000305"
FT DISULFID 163..247
FT /evidence="ECO:0000305"
FT DISULFID 290..355
FT /evidence="ECO:0000305"
FT VAR_SEQ 182..197
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1313846"
FT /id="VSP_029908"
FT VARIANT 142
FT /note="A -> P (in dbSNP:rs2276872)"
FT /id="VAR_021928"
FT VARIANT 280
FT /note="T -> M (in CSYN; dbSNP:rs119477056)"
FT /evidence="ECO:0000269|PubMed:17847009"
FT /id="VAR_037578"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:6ARQ"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:6ARQ"
FT STRAND 50..72
FT /evidence="ECO:0007829|PDB:6ARQ"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:6ARQ"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:6ARQ"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6ARQ"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:6ARQ"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:6ARQ"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6ARQ"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:6ARQ"
FT STRAND 126..136
FT /evidence="ECO:0007829|PDB:6ARQ"
SQ SEQUENCE 585 AA; 65634 MW; 2C00C2971CAB13EE CRC64;
MEKKWKYCAV YYIIQIHFVK GVWEKTVNTE ENVYATLGSD VNLTCQTQTV GFFVQMQWSK
VTNKIDLIAV YHPQYGFYCA YGRPCESLVT FTETPENGSK WTLHLRNMSC SVSGRYECML
VLYPEGIQTK IYNLLIQTHV TADEWNSNHT IEIEINQTLE IPCFQNSSSK ISSEFTYAWS
VENSSTDSWV LLSKGIKEDN GTQETLISQN HLISNSTLLK DRVKLGTDYR LHLSPVQIFD
DGRKFSCHIR VGPNKILRSS TTVKVFAKPE IPVIVENNST DVLVERRFTC LLKNVFPKAN
ITWFIDGSFL HDEKEGIYIT NEERKGKDGF LELKSVLTRV HSNKPAQSDN LTIWCMALSP
VPGNKVWNIS SEKITFLLGS EISSTDPPLS VTESTLDTQP SPASSVSPAR YPATSSVTLV
DVSALRPNTT PQPSNSSMTT RGFNYPWTSS GTDTKKSVSR IPSETYSSSP SGAGSTLHDN
VFTSTARAFS EVPTTANGST KTNHVHITGI VVNKPKDGMS WPVIVAALLF CCMILFGLGV
RKWCQYQKEI MERPPPFKPP PPPIKYTCIQ EPNESDLPYH EMETL
