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 24-JAN-2024, entry version 186. 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}. 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; 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.ENSP00000358294; -. DR GlyCosmos; O95971; 2 sites, No reported glycans. 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; 9606-ENSP00000235933; -. DR PeptideAtlas; O95971; -. DR ProteomicsDB; 51154; -. DR Antibodypedia; 33967; 713 antibodies from 37 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 AGR; HGNC:17013; -. DR CTD; 11126; -. DR DisGeNET; 11126; -. DR GeneCards; CD160; -. DR HGNC; HGNC:17013; CD160. DR HPA; ENSG00000117281; Group enriched (bone marrow, brain, intestine, liver, lymphoid tissue). 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; 5258228at2759; -. 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 1152 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 112 other cell types or tissues. DR ExpressionAtlas; O95971; baseline and differential. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. 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:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:UniProtKB. DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:UniProtKB. 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:0032729; P:positive regulation of type II interferon production; IEA:Ensembl. DR GO; GO:0031295; P:T cell costimulation; IDA:UniProtKB. DR CDD; cd21392; IgC2_CD160; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR042385; CD160. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR15425; CD160 ANTIGEN; 1. DR PANTHER; PTHR15425:SF0; CD160 ANTIGEN; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR Genevisible; O95971; HS. 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 //