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   24-JAN-2024, entry version 190.
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   GlyCosmos; P40200; 15 sites, No reported glycans.
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; 9606-ENSP00000283285; -.
DR   PeptideAtlas; P40200; -.
DR   ProteomicsDB; 55346; -. [P40200-1]
DR   ProteomicsDB; 55347; -. [P40200-2]
DR   ABCD; P40200; 19 sequenced antibodies.
DR   Antibodypedia; 32434; 377 antibodies from 34 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   AGR; HGNC:16892; -.
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; 4272797at2759; -.
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 1155 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 111 other cell types or tissues.
DR   ExpressionAtlas; P40200; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
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:0002728; P:negative regulation of natural killer cell cytokine production; IEA:Ensembl.
DR   GO; GO:0032689; P:negative regulation of type II interferon production; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; T-CELL SURFACE PROTEIN TACTILE; 1.
DR   PANTHER; PTHR15317:SF1; T-CELL SURFACE PROTEIN TACTILE; 1.
DR   SMART; SM00409; IG; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   Genevisible; P40200; HS.
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
//