BY55_MOUSE
ID BY55_MOUSE Reviewed; 185 AA.
AC O88875; Q8C9H4;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=CD160 antigen;
DE AltName: Full=Natural killer cell receptor BY55;
DE AltName: CD_antigen=CD160 {ECO:0000303|PubMed:18193050};
DE Contains:
DE RecName: Full=CD160 antigen, soluble form {ECO:0000303|PubMed:16177084};
DE Flags: Precursor;
GN Name=Cd160 {ECO:0000303|PubMed:18193050, ECO:0000312|MGI:MGI:1860383};
GN Synonyms=By55 {ECO:0000303|PubMed:18193050};
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].
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=16177084; DOI=10.4049/jimmunol.175.7.4426;
RA Maeda M., Carpenito C., Russell R.C., Dasanjh J., Veinotte L.L., Ohta H.,
RA Yamamura T., Tan R., Takei F.;
RT "Murine CD160, Ig-like receptor on NK cells and NKT cells, recognizes
RT classical and nonclassical MHC class I and regulates NK cell activation.";
RL J. Immunol. 175:4426-4432(2005).
RN [5]
RP SUBUNIT, AND 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 [6]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=22801499; DOI=10.1038/nature11242;
RA Shui J.W., Larange A., Kim G., Vela J.L., Zahner S., Cheroutre H.,
RA Kronenberg M.;
RT "HVEM signalling at mucosal barriers provides host defence against
RT pathogenic bacteria.";
RL Nature 488:222-225(2012).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25711213; DOI=10.1084/jem.20131601;
RA Tu T.C., Brown N.K., Kim T.J., Wroblewska J., Yang X., Guo X., Lee S.H.,
RA Kumar V., Lee K.M., Fu Y.X.;
RT "CD160 is essential for NK-mediated IFN-gamma production.";
RL J. Exp. Med. 212:415-429(2015).
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 (By similarity). Receptor for both classical and non-
CC classical MHC class I molecules (PubMed:16177084). Receptor or ligand
CC for TNF superfamily member TNFRSF14, participating in bidirectional
CC cell-cell contact signaling between antigen presenting cells and
CC lymphocytes. Upon ligation of TNFRSF14, provides stimulatory signal to
CC NK cells enhancing IFNG production and anti-tumor immune response
CC (PubMed:25711213). On activated CD4+ T cells, interacts with TNFRSF14
CC and down-regulates CD28 costimulatory signaling, restricting memory and
CC alloantigen-specific immune response (By similarity). In the context of
CC bacterial infection, acts as a ligand for TNFRSF14 on epithelial cells,
CC triggering the production of antimicrobial proteins and pro-
CC inflammatory cytokines (PubMed:22801499).
CC {ECO:0000250|UniProtKB:O95971, ECO:0000269|PubMed:16177084,
CC ECO:0000269|PubMed:22801499, ECO:0000269|PubMed:25711213}.
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:0000250|UniProtKB:O95971}.
CC -!- SUBUNIT: Homomultimer; disulfide-linked (By similarity). Interacts with
CC classical and non-classical MHC class I molecules (PubMed:16177084).
CC Interacts with TNFRSF14 (via cysteine-rich domain 1); this interaction
CC is direct (PubMed:18193050). Interacts with LCK and CD247/CD3 zeta
CC chain (By similarity). {ECO:0000250|UniProtKB:O95971,
CC ECO:0000269|PubMed:16177084, ECO:0000269|PubMed:18193050}.
CC -!- SUBCELLULAR LOCATION: [CD160 antigen]: Cell membrane
CC {ECO:0000269|PubMed:22801499, ECO:0000269|PubMed:25711213}; Lipid-
CC anchor, GPI-anchor {ECO:0000250|UniProtKB:O95971}.
CC -!- SUBCELLULAR LOCATION: [CD160 antigen, soluble form]: Secreted
CC {ECO:0000250|UniProtKB:O95971, ECO:0000305|PubMed:16177084}.
CC Note=Released from the cell membrane by GPI cleavage.
CC {ECO:0000250|UniProtKB:O95971, ECO:0000305|PubMed:16177084}.
CC -!- TISSUE SPECIFICITY: Expressed in resting and activated NK cell subsets
CC (at protein level) (PubMed:25711213, PubMed:16177084). Expressed in
CC resting NKT cells (at protein level) (PubMed:16177084). Expressed in
CC activated CD8+ T cells (at protein level). Highly expressed in
CC intraepithelial lymphocyte (IEL) subsets, particularly in innate-like
CC CD8A-positive IELs (at protein level) (PubMed:22801499).
CC {ECO:0000269|PubMed:16177084, ECO:0000269|PubMed:22801499,
CC ECO:0000269|PubMed:25711213}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:25711213}.
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DR EMBL; AF060982; AAC62227.1; -; mRNA.
DR EMBL; AK042093; BAC31162.1; -; mRNA.
DR EMBL; AK145332; BAE26372.1; -; mRNA.
DR EMBL; AC127297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS17648.1; -.
DR RefSeq; NP_001156968.1; NM_001163496.1.
DR RefSeq; NP_061237.3; NM_018767.3.
DR AlphaFoldDB; O88875; -.
DR SMR; O88875; -.
DR STRING; 10090.ENSMUSP00000102689; -.
DR GlyGen; O88875; 2 sites.
DR PhosphoSitePlus; O88875; -.
DR PaxDb; O88875; -.
DR PRIDE; O88875; -.
DR ProteomicsDB; 273780; -.
DR Antibodypedia; 33967; 643 antibodies from 36 providers.
DR DNASU; 54215; -.
DR Ensembl; ENSMUST00000047702; ENSMUSP00000037466; ENSMUSG00000038304.
DR Ensembl; ENSMUST00000107074; ENSMUSP00000102689; ENSMUSG00000038304.
DR GeneID; 54215; -.
DR KEGG; mmu:54215; -.
DR UCSC; uc008qof.2; mouse.
DR CTD; 11126; -.
DR MGI; MGI:1860383; Cd160.
DR VEuPathDB; HostDB:ENSMUSG00000038304; -.
DR eggNOG; ENOG502RR8D; Eukaryota.
DR GeneTree; ENSGT00390000007258; -.
DR InParanoid; O88875; -.
DR OMA; HLQGHFF; -.
DR OrthoDB; 1278184at2759; -.
DR TreeFam; TF338321; -.
DR BioGRID-ORCS; 54215; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cd160; mouse.
DR PRO; PR:O88875; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O88875; protein.
DR Bgee; ENSMUSG00000038304; Expressed in secondary oocyte and 44 other tissues.
DR ExpressionAtlas; O88875; baseline and differential.
DR Genevisible; O88875; MM.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0023024; F:MHC class I protein complex binding; IDA:UniProtKB.
DR GO; GO:0032393; F:MHC class I receptor activity; ISO:MGI.
DR GO; GO:0032394; F:MHC class Ib receptor activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002385; P:mucosal immune response; IDA:UniProtKB.
DR GO; GO:1905675; P:negative regulation of adaptive immune memory response; ISO:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:1900280; P:negative regulation of CD4-positive, alpha-beta T cell costimulation; ISO:MGI.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
DR GO; GO:0002729; P:positive regulation of natural killer cell cytokine production; ISS:UniProtKB.
DR GO; GO:0043323; P:positive regulation of natural killer cell degranulation; ISO:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0002857; P:positive regulation of natural killer cell mediated immune response to tumor cell; IMP:UniProtKB.
DR GO; GO:0031295; P:T cell costimulation; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR042385; CD160.
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; IPR013106; Ig_V-set.
DR PANTHER; PTHR15425; PTHR15425; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunity; Immunoglobulin domain; Innate immunity; Lipoprotein; Membrane;
KW Receptor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..160
FT /note="CD160 antigen"
FT /id="PRO_0000014545"
FT CHAIN 28..160
FT /note="CD160 antigen, soluble form"
FT /evidence="ECO:0000305|PubMed:16177084"
FT /id="PRO_0000446050"
FT PROPEP 161..185
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014546"
FT DOMAIN 28..136
FT /note="Ig-like V-type"
FT /evidence="ECO:0000250|UniProtKB:O95971"
FT LIPID 160
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 64..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 45
FT /note="L -> P (in Ref. 1; AAC62227)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 20570 MW; 37071CB339E032E2 CRC64;
MQRILMAPGQ SCCALAILLA IVNFQHGGCI HVTSSASQKG GRLDLTCTLW HKKDEAEGLI
LFWCKDNPWN CSPETNLEQL RVKRDPETDG ITEKSSQLVF TIEQATPSDS GTYQCCARSQ
KPEIYIHGHF LSVLVTGNHT EIRQRQRSHP DFSHINGTLS SGFLQVKAWG MLVTSLVALQ
ALYTL
