BY55_HUMAN
ID BY55_HUMAN Reviewed; 181 AA.
AC O95971; A0A0B4J2A1; B8PRF2; Q5T2V6;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=CD160 antigen;
DE AltName: Full=Natural killer cell receptor BY55;
DE AltName: CD_antigen=CD160 {ECO:0000303|PubMed:16809620};
DE Contains:
DE RecName: Full=CD160 antigen, soluble form {ECO:0000303|PubMed:17237375};
DE Flags: Precursor;
GN Name=CD160 {ECO:0000303|PubMed:16809620, ECO:0000312|HGNC:HGNC:17013};
GN Synonyms=BY55 {ECO:0000303|PubMed:9743336};
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 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=9743336;
RA Anumanthan A., Bensussan A., Boumsell L., Christ A.D., Blumberg R.S.,
RA Voss S.D., Patel A.T., Robertson M.J., Nadler L.M., Freeman G.J.;
RT "Cloning of BY55, a novel Ig superfamily member expressed on NK cells, CTL,
RT and intestinal intraepithelial lymphocytes.";
RL J. Immunol. 161:2780-2790(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND FUNCTION.
RX PubMed=19109136; DOI=10.4049/jimmunol.182.1.63;
RA Giustiniani J., Bensussan A., Marie-Cardine A.;
RT "Identification and characterization of a transmembrane isoform of CD160
RT (CD160-TM), a unique activating receptor selectively expressed upon human
RT NK cell activation.";
RL J. Immunol. 182:63-71(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH HLA-A2-B2M.
RX PubMed=9973372;
RA Agrawal S., Marquet J., Freeman G.J., Tawab A., Bouteiller P.L., Roth P.,
RA Bolton W., Ogg G., Boumsell L., Bensussan A.;
RT "MHC class I triggering by a novel cell surface ligand costimulates
RT proliferation of activated human T cells.";
RL J. Immunol. 162:1223-1226(1999).
RN [6]
RP FUNCTION, SUBUNIT, INTERACTION WITH LCK, INTERACTION WITH CD247, AND TISSUE
RP SPECIFICITY.
RX PubMed=11978774; DOI=10.1093/intimm/14.5.445;
RA Nikolova M., Marie-Cardine A., Boumsell L., Bensussan A.;
RT "BY55/CD160 acts as a co-receptor in TCR signal transduction of a human
RT circulating cytotoxic effector T lymphocyte subset lacking CD28
RT expression.";
RL Int. Immunol. 14:445-451(2002).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12486241; DOI=10.1073/pnas.012681099;
RA Le Bouteiller P., Barakonyi A., Giustiniani J., Lenfant F.,
RA Marie-Cardine A., Aguerre-Girr M., Rabot M., Hilgert I., Mami-Chouaib F.,
RA Tabiasco J., Boumsell L., Bensussan A.;
RT "Engagement of CD160 receptor by HLA-C is a triggering mechanism used by
RT circulating natural killer (NK) cells to mediate cytotoxicity.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16963-16968(2002).
RN [8]
RP FUNCTION, SUBUNIT, INTERACTION WITH HLA-G, AND TISSUE SPECIFICITY.
RX PubMed=16809620; DOI=10.1182/blood-2005-12-019919;
RA Fons P., Chabot S., Cartwright J.E., Lenfant F., L'Faqihi F.,
RA Giustiniani J., Herault J.P., Gueguen G., Bono F., Savi P.,
RA Aguerre-Girr M., Fournel S., Malecaze F., Bensussan A., Plouet J.,
RA Le Bouteiller P.;
RT "Soluble HLA-G1 inhibits angiogenesis through an apoptotic pathway and by
RT direct binding to CD160 receptor expressed by endothelial cells.";
RL Blood 108:2608-2615(2006).
RN [9]
RP FUNCTION.
RX PubMed=17307798; DOI=10.1093/intimm/dxm005;
RA Rabot M., El Costa H., Polgar B., Marie-Cardine A., Aguerre-Girr M.,
RA Barakonyi A., Valitutti S., Bensussan A., Le Bouteiller P.;
RT "CD160-activating NK cell effector functions depend on the
RT phosphatidylinositol 3-kinase recruitment.";
RL Int. Immunol. 19:401-409(2007).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY IL15.
RX PubMed=17237375; DOI=10.4049/jimmunol.178.3.1293;
RA Giustiniani J., Marie-Cardine A., Bensussan A.;
RT "A soluble form of the MHC class I-specific CD160 receptor is released from
RT human activated NK lymphocytes and inhibits cell-mediated cytotoxicity.";
RL J. Immunol. 178:1293-1300(2007).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP INTERACTION WITH TNFRSF14.
RX PubMed=18193050; DOI=10.1038/ni1554;
RA Cai G., Anumanthan A., Brown J.A., Greenfield E.A., Zhu B., Freeman G.J.;
RT "CD160 inhibits activation of human CD4+ T cells through interaction with
RT herpesvirus entry mediator.";
RL Nat. Immunol. 9:176-185(2008).
RN [12]
RP TISSUE SPECIFICITY, SUBUNIT, INTERACTION WITH TNFRSF14, AND SUBCELLULAR
RP LOCATION.
RX PubMed=23761635; DOI=10.4049/jimmunol.1300894;
RA Sedy J.R., Bjordahl R.L., Bekiaris V., Macauley M.G., Ware B.C.,
RA Norris P.S., Lurain N.S., Benedict C.A., Ware C.F.;
RT "CD160 activation by herpesvirus entry mediator augments inflammatory
RT cytokine production and cytolytic function by NK cells.";
RL J. Immunol. 191:828-836(2013).
RN [13]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25255144; DOI=10.1371/journal.ppat.1004380;
RA Vigano S., Banga R., Bellanger F., Pellaton C., Farina A., Comte D.,
RA Harari A., Perreau M.;
RT "CD160-associated CD8 T-cell functional impairment is independent of PD-1
RT expression.";
RL PLoS Pathog. 10:E1004380-E1004380(2014).
CC -!- FUNCTION: [CD160 antigen]: Receptor on immune cells capable to deliver
CC stimulatory or inhibitory signals that regulate cell activation and
CC differentiation. Exists as a GPI-anchored and as a transmembrane form,
CC each likely initiating distinct signaling pathways via phosphoinositol
CC 3-kinase in activated NK cells and via LCK and CD247/CD3 zeta chain in
CC activated T cells (PubMed:19109136, PubMed:11978774, PubMed:17307798).
CC Receptor for both classical and non-classical MHC class I molecules
CC (PubMed:9973372, PubMed:12486241). In the context of acute viral
CC infection, recognizes HLA-C and triggers NK cell cytotoxic activity,
CC likely playing a role in anti-viral innate immune response
CC (PubMed:12486241). On CD8+ T cells, binds HLA-A2-B2M in complex with a
CC viral peptide and provides a costimulatory signal to activated/memory T
CC cells (PubMed:9973372). Upon persistent antigen stimulation, such as
CC occurs during chronic viral infection, may progressively inhibit TCR
CC signaling in memory CD8+ T cells, contributing to T cell exhaustion
CC (PubMed:25255144). On endothelial cells, recognizes HLA-G and controls
CC angiogenesis in immune privileged sites (PubMed:16809620). Receptor or
CC ligand for TNF superfamily member TNFRSF14, participating in
CC bidirectional cell-cell contact signaling between antigen presenting
CC cells and lymphocytes. Upon ligation of TNFRSF14, provides stimulatory
CC signal to NK cells enhancing IFNG production and anti-tumor immune
CC response (By similarity). On activated CD4+ T cells, interacts with
CC TNFRSF14 and down-regulates CD28 costimulatory signaling, restricting
CC memory and alloantigen-specific immune response (PubMed:18193050). In
CC the context of bacterial infection, acts as a ligand for TNFRSF14 on
CC epithelial cells, triggering the production of antimicrobial proteins
CC and pro-inflammatory cytokines (By similarity).
CC {ECO:0000250|UniProtKB:O88875, ECO:0000269|PubMed:11978774,
CC ECO:0000269|PubMed:12486241, ECO:0000269|PubMed:16809620,
CC ECO:0000269|PubMed:17307798, ECO:0000269|PubMed:18193050,
CC ECO:0000269|PubMed:19109136, ECO:0000269|PubMed:25255144,
CC ECO:0000269|PubMed:9973372}.
CC -!- FUNCTION: [CD160 antigen, soluble form]: The soluble GPI-cleaved form,
CC usually released by activated lymphocytes, might play an immune
CC regulatory role by limiting lymphocyte effector functions.
CC {ECO:0000269|PubMed:17237375}.
CC -!- SUBUNIT: Homomultimer; disulfide-linked (Probable). Interacts with HLA-
CC G (PubMed:16809620). Interacts with HLA-A2-B2M in complex with an HIV-
CC derived peptide (PubMed:9973372). Interacts with TNFRSF14 (via
CC cysteine-rich domain 1); this interaction is direct (PubMed:18193050).
CC Interacts with LCK and CD247/CD3 zeta chain (PubMed:11978774).
CC {ECO:0000269|PubMed:11978774, ECO:0000269|PubMed:16809620,
CC ECO:0000269|PubMed:18193050, ECO:0000269|PubMed:9973372,
CC ECO:0000305|PubMed:9743336}.
CC -!- INTERACTION:
CC O95971; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-4314390, EBI-741181;
CC O95971; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-4314390, EBI-11522780;
CC O95971; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-4314390, EBI-1054315;
CC O95971; Q969L2: MAL2; NbExp=3; IntAct=EBI-4314390, EBI-944295;
CC O95971; O15151: MDM4; NbExp=6; IntAct=EBI-4314390, EBI-398437;
CC O95971; P08247: SYP; NbExp=3; IntAct=EBI-4314390, EBI-9071725;
CC O95971; P10827: THRA; NbExp=3; IntAct=EBI-4314390, EBI-286285;
CC -!- SUBCELLULAR LOCATION: [CD160 antigen]: Cell membrane
CC {ECO:0000269|PubMed:12486241, ECO:0000269|PubMed:18193050,
CC ECO:0000269|PubMed:9973372}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:23761635, ECO:0000269|PubMed:9743336}.
CC -!- SUBCELLULAR LOCATION: [CD160 antigen, soluble form]: Secreted.
CC Note=Released from the cell membrane by GPI cleavage.
CC {ECO:0000269|PubMed:17237375, ECO:0000269|PubMed:23761635,
CC ECO:0000269|PubMed:9743336}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=CD160 {ECO:0000303|PubMed:19109136};
CC IsoId=O95971-1; Sequence=Displayed;
CC Name=2; Synonyms=CD160deltaIg {ECO:0000303|PubMed:19109136};
CC IsoId=O95971-2; Sequence=VSP_060018;
CC Name=3; Synonyms=CD160-TM {ECO:0000303|PubMed:19109136};
CC IsoId=O95971-3; Sequence=VSP_060019;
CC Name=4; Synonyms=CD160deltaIg-TM {ECO:0000303|PubMed:19109136};
CC IsoId=O95971-4; Sequence=VSP_060017;
CC -!- TISSUE SPECIFICITY: Expression is restricted to functional NK and
CC cytotoxic T lymphocytes. Expressed in viral-specific effector memory
CC and terminally differentiated effector memory CD8+ T cells. Expressed
CC in memory and activated CD4+ T cell subsets (at protein level)
CC (PubMed:9743336, PubMed:18193050, PubMed:11978774, PubMed:25255144).
CC Expressed at high levels in intraepithelial lymphocytes (at protein
CC level) (PubMed:9743336). Expressed in both alpha-beta and gamma-delta
CC CD8+ T cell subsets (at protein level) (PubMed:9743336,
CC PubMed:18193050, PubMed:11978774). Expressed in umbilical vein
CC endothelial cells (at protein level) (PubMed:16809620). Expressed in
CC monocytes and at lower levels in B cells (PubMed:23761635). Isoform 3:
CC Expressed exclusively in activated NK cells (at protein level)
CC (PubMed:19109136). {ECO:0000269|PubMed:11978774,
CC ECO:0000269|PubMed:16809620, ECO:0000269|PubMed:18193050,
CC ECO:0000269|PubMed:19109136, ECO:0000269|PubMed:23761635,
CC ECO:0000269|PubMed:25255144, ECO:0000269|PubMed:9743336}.
CC -!- INDUCTION: Up-regulated on CD4+ T cells upon stimulation via T cell
CC receptor plus costimulation via CD28 (PubMed:18193050). Up-regulated by
CC IL15 on immunoregulatory NCAM1/CD56-bright NK cells (PubMed:17237375).
CC {ECO:0000269|PubMed:17237375, ECO:0000269|PubMed:18193050}.
CC -!- MISCELLANEOUS: [Isoform 3]: Mutagenesis of TYR-225 to Phe abolishes
CC intracellular signaling. {ECO:0000269|PubMed:19109136}.
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DR EMBL; AF060981; AAC72302.1; -; mRNA.
DR EMBL; EU016100; ABV89736.1; -; mRNA.
DR EMBL; EU016101; ABV89737.1; -; mRNA.
DR EMBL; AL390725; CAI13714.1; -; Genomic_DNA.
DR EMBL; AC242845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014465; AAH14465.1; -; mRNA.
DR CCDS; CCDS72861.1; -. [O95971-1]
DR RefSeq; NP_008984.1; NM_007053.3. [O95971-1]
DR RefSeq; XP_005272986.1; XM_005272929.3. [O95971-3]
DR RefSeq; XP_011507406.1; XM_011509104.2. [O95971-3]
DR PDB; 6NG3; X-ray; 2.88 A; A=27-144.
DR PDB; 6NG9; X-ray; 1.95 A; A/B=27-144.
DR PDB; 6NGG; X-ray; 1.95 A; A/B=27-144.
DR PDB; 7MSG; X-ray; 3.50 A; D/E/F=27-144.
DR PDBsum; 6NG3; -.
DR PDBsum; 6NG9; -.
DR PDBsum; 6NGG; -.
DR PDBsum; 7MSG; -.
DR AlphaFoldDB; O95971; -.
DR SMR; O95971; -.
DR BioGRID; 116299; 48.
DR IntAct; O95971; 9.
DR MINT; O95971; -.
DR STRING; 9606.ENSP00000235933; -.
DR GlyGen; O95971; 2 sites.
DR iPTMnet; O95971; -.
DR PhosphoSitePlus; O95971; -.
DR BioMuta; CD160; -.
DR EPD; O95971; -.
DR jPOST; O95971; -.
DR MassIVE; O95971; -.
DR PaxDb; O95971; -.
DR PeptideAtlas; O95971; -.
DR PRIDE; O95971; -.
DR ProteomicsDB; 51154; -.
DR Antibodypedia; 33967; 643 antibodies from 36 providers.
DR DNASU; 11126; -.
DR Ensembl; ENST00000235933.10; ENSP00000235933.6; ENSG00000117281.16. [O95971-1]
DR Ensembl; ENST00000369288.7; ENSP00000358294.1; ENSG00000117281.16. [O95971-1]
DR Ensembl; ENST00000401557.7; ENSP00000385199.4; ENSG00000117281.16. [O95971-3]
DR Ensembl; ENST00000584442.2; ENSP00000462594.2; ENSG00000117281.16. [O95971-2]
DR Ensembl; ENST00000616463.1; ENSP00000483935.1; ENSG00000117281.16. [O95971-4]
DR GeneID; 11126; -.
DR KEGG; hsa:11126; -.
DR MANE-Select; ENST00000369288.7; ENSP00000358294.1; NM_007053.4; NP_008984.1.
DR UCSC; uc010oyz.3; human.
DR UCSC; uc031ute.2; human.
DR CTD; 11126; -.
DR DisGeNET; 11126; -.
DR GeneCards; CD160; -.
DR HGNC; HGNC:17013; CD160.
DR HPA; ENSG00000117281; Tissue enhanced (lymphoid).
DR MIM; 604463; gene.
DR neXtProt; NX_O95971; -.
DR OpenTargets; ENSG00000117281; -.
DR PharmGKB; PA134943137; -.
DR VEuPathDB; HostDB:ENSG00000117281; -.
DR eggNOG; ENOG502RR8D; Eukaryota.
DR GeneTree; ENSGT00390000007258; -.
DR HOGENOM; CLU_103393_0_0_1; -.
DR InParanoid; O95971; -.
DR OMA; HLQGHFF; -.
DR OrthoDB; 1278184at2759; -.
DR PhylomeDB; O95971; -.
DR TreeFam; TF338321; -.
DR PathwayCommons; O95971; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; O95971; -.
DR BioGRID-ORCS; 11126; 8 hits in 1072 CRISPR screens.
DR GeneWiki; CD160; -.
DR GenomeRNAi; 11126; -.
DR Pharos; O95971; Tbio.
DR PRO; PR:O95971; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O95971; protein.
DR Bgee; ENSG00000117281; Expressed in granulocyte and 111 other tissues.
DR ExpressionAtlas; O95971; baseline and differential.
DR Genevisible; O95971; HS.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:HGNC-UCL.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032397; F:activating MHC class I receptor activity; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0023024; F:MHC class I protein complex binding; IEA:Ensembl.
DR GO; GO:0032393; F:MHC class I receptor activity; IDA:HGNC-UCL.
DR GO; GO:0032394; F:MHC class Ib receptor activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IDA:HGNC-UCL.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002385; P:mucosal immune response; IEA:Ensembl.
DR GO; GO:1905675; P:negative regulation of adaptive immune memory response; IDA:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:1900280; P:negative regulation of CD4-positive, alpha-beta T cell costimulation; IDA:UniProtKB.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0002729; P:positive regulation of natural killer cell cytokine production; IDA:UniProtKB.
DR GO; GO:0043323; P:positive regulation of natural killer cell degranulation; IDA:UniProtKB.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
DR GO; GO:0002857; P:positive regulation of natural killer cell mediated immune response to tumor cell; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR042385; CD160.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR15425; PTHR15425; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Angiogenesis;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Immunity;
KW Immunoglobulin domain; Innate immunity; Lipoprotein; Membrane; Receptor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..159
FT /note="CD160 antigen"
FT /id="PRO_0000014543"
FT CHAIN 25..159
FT /note="CD160 antigen, soluble form"
FT /evidence="ECO:0000305|PubMed:17237375,
FT ECO:0000305|PubMed:23761635, ECO:0000305|PubMed:9743336"
FT /id="PRO_0000446049"
FT PROPEP 160..181
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014544"
FT DOMAIN 25..133
FT /note="Ig-like V-type"
FT /evidence="ECO:0000305|PubMed:19109136"
FT LIPID 159
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..112
FT /evidence="ECO:0000255"
FT DISULFID 61..68
FT /evidence="ECO:0000255"
FT VAR_SEQ 25..181
FT /note="GCINITSSASQEGTRLNLICTVWHKKEEAEGFVVFLCKDRSGDCSPETSLKQ
FT LRLKRDPGIDGVGEISSQLMFTISQVTPLHSGTYQCCARSQKSGIRLQGHFFSILFTET
FT GNYTVTGLKQRQHLEFSHNEGTLSSGFLQEKVWVMLVTSLVALQAL -> ETGNYTVTG
FT LKQRQHLEFSHNEGTLSSGFLQEKVWVMLVTSLVALQGMSKRAVSTPSNEGAIIFLPPW
FT LFSRRRRLERMSRGREKCYSSPGYPQESSNQFH (in isoform 4)"
FT /id="VSP_060017"
FT VAR_SEQ 25..133
FT /note="Missing (in isoform 2)"
FT /id="VSP_060018"
FT VAR_SEQ 180..181
FT /note="AL -> GMSKRAVSTPSNEGAIIFLPPWLFSRRRRLERMSRGREKCYSSPGY
FT PQESSNQFH (in isoform 3)"
FT /evidence="ECO:0000305|PubMed:19109136"
FT /id="VSP_060019"
FT VARIANT 91
FT /note="I -> V (in dbSNP:rs2231373)"
FT /id="VAR_027747"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:6NGG"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:6NGG"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6NG3"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:6NGG"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:6NGG"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:6NGG"
FT STRAND 88..101
FT /evidence="ECO:0007829|PDB:6NGG"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6NGG"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:6NGG"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:6NGG"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6NGG"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:6NGG"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:6NGG"
SQ SEQUENCE 181 AA; 19810 MW; EF0B981ACC7478BD CRC64;
MLLEPGRGCC ALAILLAIVD IQSGGCINIT SSASQEGTRL NLICTVWHKK EEAEGFVVFL
CKDRSGDCSP ETSLKQLRLK RDPGIDGVGE ISSQLMFTIS QVTPLHSGTY QCCARSQKSG
IRLQGHFFSI LFTETGNYTV TGLKQRQHLE FSHNEGTLSS GFLQEKVWVM LVTSLVALQA
L
