NKG2D_MOUSE
ID NKG2D_MOUSE Reviewed; 232 AA.
AC O54709;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=NKG2-D type II integral membrane protein;
DE AltName: Full=Killer cell lectin-like receptor subfamily K member 1;
DE AltName: Full=NK cell receptor D;
DE AltName: Full=NKG2-D-activating NK receptor;
DE AltName: CD_antigen=CD314;
GN Name=Klrk1; Synonyms=Nkg2d;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=9600963; DOI=10.1073/pnas.95.11.6320;
RA Ho E.L., Heusel J.W., Brown M.G., Matsumoto K., Scalzo A.A., Yokoyama W.M.;
RT "Murine Nkg2d and Cd94 are clustered within the natural killer complex and
RT are expressed independently in natural killer cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6320-6325(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RA Butcher S., Cottage A., Cook G.P.;
RT "Mouse natural killer cell receptors homologous to human CD94 and NKG2-D.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=9464811; DOI=10.1002/eji.1830271222;
RA Vance R.E., Tanamachi D.M., Hanke T., Raulet D.H.;
RT "Cloning of a mouse homolog of CD94 extends the family of C-type lectins on
RT murine natural killer cells.";
RL Eur. J. Immunol. 27:3236-3241(1997).
RN [5]
RP FUNCTION IN CYTOTOXICITY ACTIVATION, AND FUNCTION AS A RECEPTOR FOR RAET1A;
RP RAET1B; RAET1C; RAET1D AND H60.
RX PubMed=10894171; DOI=10.1016/s1074-7613(00)80222-8;
RA Cerwenka A., Bakker A.B., McClanahan T., Wagner J., Wu J., Phillips J.H.,
RA Lanier L.L.;
RT "Retinoic acid early inducible genes define a ligand family for the
RT activating NKG2D receptor in mice.";
RL Immunity 12:721-727(2000).
RN [6]
RP FUNCTION IN CYTOTOXICITY ACTIVATION, FUNCTION AS A RECEPTOR FOR RAET1B AND
RP H60, AND TISSUE SPECIFICITY.
RX PubMed=11248803; DOI=10.1038/77793;
RA Diefenbach A., Jamieson A.M., Liu S.D., Shastri N., Raulet D.H.;
RT "Ligands for the murine NKG2D receptor: expression by tumor cells and
RT activation of NK cells and macrophages.";
RL Nat. Immunol. 1:119-126(2000).
RN [7]
RP FUNCTION IN CYTOTOXICITY ACTIVATION, AND FUNCTION AS A RECEPTOR FOR RAET1B
RP AND H60.
RX PubMed=11557981; DOI=10.1038/35093109;
RA Diefenbach A., Jensen E.R., Jamieson A.M., Raulet D.H.;
RT "Rae1 and H60 ligands of the NKG2D receptor stimulate tumour immunity.";
RL Nature 413:165-171(2001).
RN [8]
RP FUNCTION IN CYTOTOXICITY ACTIVATION, FUNCTION AS A RECEPTOR FOR RAET1E, AND
RP TISSUE SPECIFICITY.
RX PubMed=11567106; DOI=10.1126/science.1063916;
RA Girardi M., Oppenheim D.E., Steele C.R., Lewis J.M., Glusac E., Filler R.,
RA Hobby P., Sutton B., Tigelaar R.E., Hayday A.C.;
RT "Regulation of cutaneous malignancy by gammadelta T cells.";
RL Science 294:605-609(2001).
RN [9]
RP FUNCTION IN CYTOTOXICITY ACTIVATION, INDUCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12150888; DOI=10.1016/s1074-7613(02)00333-3;
RA Jamieson A.M., Diefenbach A., McMahon C.W., Xiong N., Carlyle J.R.,
RA Raulet D.H.;
RT "The role of the NKG2D immunoreceptor in immune cell activation and natural
RT killing.";
RL Immunity 17:19-29(2002).
RN [10]
RP FUNCTION AS A RECEPTOR FOR MULT1.
RX PubMed=12370332; DOI=10.4049/jimmunol.169.8.4079;
RA Carayannopoulos L.N., Naidenko O.V., Fremont D.H., Yokoyama W.M.;
RT "Murine UL16-binding protein-like transcript 1: a newly described
RT transcript encoding a high-affinity ligand for murine NKG2D.";
RL J. Immunol. 169:4079-4083(2002).
RN [11]
RP REVIEW, AND ALTERNATIVE SPLICING.
RX PubMed=11973127; DOI=10.1016/s0952-7915(02)00337-0;
RA Vivier E., Tomasello E., Paul P.;
RT "Lymphocyte activation via NKG2D: towards a new paradigm in immune
RT recognition?";
RL Curr. Opin. Immunol. 14:306-311(2002).
RN [12]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP AND INTERACTION WITH HCST AND TYROBP.
RX PubMed=12426565; DOI=10.1038/ni858;
RA Diefenbach A., Tomasello E., Lucas M., Jamieson A.M., Hsia J.K., Vivier E.,
RA Raulet D.H.;
RT "Selective associations with signaling proteins determine stimulatory
RT versus costimulatory activity of NKG2D.";
RL Nat. Immunol. 3:1142-1149(2002).
RN [13]
RP FUNCTION IN CYTOTOXICITY ACTIVATION, AND INTERACTION WITH TYROBP.
RX PubMed=12426564; DOI=10.1038/ni857;
RA Gilfillan S., Ho E.L., Cella M., Yokoyama W.M., Colonna M.;
RT "NKG2D recruits two distinct adapters to trigger NK cell activation and
RT costimulation.";
RL Nat. Immunol. 3:1150-1155(2002).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=15048723; DOI=10.1002/eji.200324793;
RA Alli R., Savithri B., Das S., Varalakshmi C., Rangaraj N., Khar A.;
RT "Involvement of NKR-P2/NKG2D in DC-mediated killing of tumor targets:
RT indicative of a common, innate, target-recognition paradigm?";
RL Eur. J. Immunol. 34:1119-1126(2004).
RN [15]
RP FUNCTION, INVOLVEMENT IN AUTOIMMUNE DIABETES, AND INDUCTION.
RX PubMed=15189740; DOI=10.1016/j.immuni.2004.05.008;
RA Ogasawara K., Hamerman J.A., Ehrlich L.R., Bour-Jordan H., Santamaria P.,
RA Bluestone J.A., Lanier L.L.;
RT "NKG2D blockade prevents autoimmune diabetes in NOD mice.";
RL Immunity 20:757-767(2004).
RN [16]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH HCST AND TYROBP,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15294961; DOI=10.4049/jimmunol.173.4.2470;
RA Rosen D.B., Araki M., Hamerman J.A., Chen T., Yamamura T., Lanier L.L.;
RT "A Structural basis for the association of DAP12 with mouse, but not human,
RT NKG2D.";
RL J. Immunol. 173:2470-2478(2004).
RN [17]
RP FUNCTION IN IMMUNITY AND ALLOGRAFT REJECTION, AND FUNCTION AS A RECEPTOR
RP FOR RAET1E.
RX PubMed=16086018; DOI=10.1038/ni1236;
RA Ogasawara K., Benjamin J., Takaki R., Phillips J.H., Lanier L.L.;
RT "Function of NKG2D in natural killer cell-mediated rejection of mouse bone
RT marrow grafts.";
RL Nat. Immunol. 6:938-945(2005).
RN [18]
RP FUNCTION IN TUMOR SURVEILLANCE, AND DISRUPTION PHENOTYPE.
RX PubMed=18394936; DOI=10.1016/j.immuni.2008.02.016;
RA Guerra N., Tan Y.X., Joncker N.T., Choy A., Gallardo F., Xiong N.,
RA Knoblaugh S., Cado D., Greenberg N.M., Greenberg N.R., Raulet D.H.;
RT "NKG2D-deficient mice are defective in tumor surveillance in models of
RT spontaneous malignancy.";
RL Immunity 28:571-580(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [20]
RP FUNCTION IN NK CELL DIFFERENTIATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19631564; DOI=10.1016/j.immuni.2009.06.017;
RA Zafirova B., Mandaric S., Antulov R., Krmpotic A., Jonsson H.,
RA Yokoyama W.M., Jonjic S., Polic B.;
RT "Altered NK cell development and enhanced NK cell-mediated resistance to
RT mouse cytomegalovirus in NKG2D-deficient mice.";
RL Immunity 31:270-282(2009).
RN [21]
RP REVIEW, AND FUNCTION.
RX PubMed=21898152; DOI=10.1007/s00018-011-0797-0;
RA Zafirova B., Wensveen F.M., Gulin M., Polic B.;
RT "Regulation of immune cell function and differentiation by the NKG2D
RT receptor.";
RL Cell. Mol. Life Sci. 68:3519-3529(2011).
RN [22]
RP REVIEW, AND FUNCTION AS A RECEPTOR FOR MHC CLASS I-RELATED GLYCOPROTEINS.
RX PubMed=23298206; DOI=10.1146/annurev-immunol-032712-095951;
RA Raulet D.H., Gasser S., Gowen B.G., Deng W., Jung H.;
RT "Regulation of ligands for the NKG2D activating receptor.";
RL Annu. Rev. Immunol. 31:413-441(2013).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 110-232.
RX PubMed=11224525; DOI=10.1038/85311;
RA Wolan D.W., Teyton L., Rudolph M.G., Villmow B., Bauer S., Busch D.H.,
RA Wilson I.A.;
RT "Crystal structure of the murine NK cell-activating receptor NKG2D at 1.95
RT A.";
RL Nat. Immunol. 2:248-254(2001).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 110-232 IN COMPLEX WITH RAET1B.
RX PubMed=11825567; DOI=10.1016/s1074-7613(02)00258-3;
RA Li P., McDermott G., Strong R.K.;
RT "Crystal structures of RAE-1beta and its complex with the activating
RT immunoreceptor NKG2D.";
RL Immunity 16:77-86(2002).
CC -!- FUNCTION: Functions as an activating and costimulatory receptor
CC involved in immunosurveillance upon binding to various cellular stress-
CC inducible ligands displayed at the surface of autologous tumor cells
CC and virus-infected cells. Provides both stimulatory and costimulatory
CC innate immune responses on activated killer (NK) cells, leading to
CC cytotoxic activity. Acts as a costimulatory receptor for T-cell
CC receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by
CC amplifying T-cell activation. Stimulates perforin-mediated elimination
CC of ligand-expressing tumor cells. Signaling involves calcium influx,
CC culminating in the expression of TNF-alpha. Participates in NK cell-
CC mediated bone marrow graft rejection. May play a regulatory role in
CC differentiation and survival of NK cells. Binds to ligands belonging to
CC various subfamilies of MHC class I-related glycoproteins including
CC RAET1A, RAET1B, RAET1C, RAET1D, RAET1E, H60 and MULT1.
CC {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:11248803,
CC ECO:0000269|PubMed:11557981, ECO:0000269|PubMed:11567106,
CC ECO:0000269|PubMed:12150888, ECO:0000269|PubMed:12370332,
CC ECO:0000269|PubMed:12426564, ECO:0000269|PubMed:12426565,
CC ECO:0000269|PubMed:15189740, ECO:0000269|PubMed:16086018,
CC ECO:0000269|PubMed:18394936, ECO:0000269|PubMed:19631564,
CC ECO:0000269|PubMed:21898152, ECO:0000269|PubMed:23298206}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Heterohexamer composed of two
CC subunits of KLRK1 and four subunits of HCST/DAP10 (By similarity).
CC Isoform 1 (via transmembrane domain) interacts with HCST/DAP10; the
CC interaction is required for KLRK1 cell surface expression on activated
CC CD8(+) T-cells, but is dispensable on activated TYROBP-expressing NK
CC cells. Isoform 2 (via transmembrane domain) interacts with HCST/DAP10
CC (via transmembrane domain); the interaction is required for KLRK1 NK
CC cell surface expression and induces NK cell-mediated cytotoxicity.
CC Isoform 2 (via transmembrane domain) interacts with TYROBP (via
CC transmembrane domain); the interaction is required for KLRK1 NK cell
CC surface expression and induce NK cell-mediated cytotoxicity and
CC cytokine secretion. Isoform 1 does not interact with TYROBP. Interacts
CC with CEACAM1; recruits PTPN6 that dephosphorylates VAV1 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P26718,
CC ECO:0000269|PubMed:11825567, ECO:0000269|PubMed:12426564,
CC ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15294961}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12426565,
CC ECO:0000269|PubMed:15294961}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15294961}.
CC Note=Colocalized with HCST and TYROBP on the cell surface.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced.;
CC Name=1; Synonyms=NKG2D long, NKG2D-L;
CC IsoId=O54709-1; Sequence=Displayed;
CC Name=2; Synonyms=NKG2D short, NKG2D-S;
CC IsoId=O54709-2; Sequence=VSP_053945;
CC -!- TISSUE SPECIFICITY: Expressed in natural killer (NK) cells, activated
CC CD8(+) alpha-beta and gamma-delta T-cells and natural killer T (NKT)
CC cells (at protein level). May be expressed on dendritic cell (DC).
CC Isoform 1 is strongly expressed in natural killer (NK) cells. Isoform 2
CC is weakly expressed in natural killer (NK) cells. Isoform 1 and isoform
CC 2 are expressed in stimulated, but not in unstimulated, CD8(+) T-cells
CC and macrophages. {ECO:0000269|PubMed:11248803,
CC ECO:0000269|PubMed:11567106, ECO:0000269|PubMed:12150888,
CC ECO:0000269|PubMed:15048723}.
CC -!- DEVELOPMENTAL STAGE: Expressed in NK cells from the thymus at 15 dpc
CC (at protein level). {ECO:0000269|PubMed:12150888}.
CC -!- INDUCTION: Up-regulated in activated CD8(+) T-cells. Up-regulated upon
CC lipopolysaccharide (LPS) and interferon treatments in macrophages. Up-
CC regulated in CD8(+) T-cell infiltring pancreatic islets of prediabetic
CC nonobese diabetic (NOD) mice (at protein level). Isoform 1 and isoform
CC 2 are up-regulated upon T-cell receptor (TCR) stimulation in CD8(+) T-
CC cells. Isoform 1 is modestly up-regulated upon lipopolysaccharide (LPS)
CC in macrophages. Isoform 2 is up-regulated upon lipopolysaccharide (LPS)
CC in macrophages. Isoform 2 is up-regulated upon poly(I:C) and
CC interleukin IL2 in natural killer (NK) cells.
CC {ECO:0000269|PubMed:12150888, ECO:0000269|PubMed:15189740}.
CC -!- DISEASE: Note=Involved in autoreactive CD8(+) T-cell-mediated
CC development of autoimmune diabetes. {ECO:0000269|PubMed:15189740}.
CC -!- DISRUPTION PHENOTYPE: Mice display no visible phenotype. According to
CC PubMed:18394936, show normal development of NK cells, B and T cells but
CC display enhanced formation of aggressive tumors. According to
CC PubMed:19631564, exhibit developmental perturbation in size of NK cell
CC subpopulations, increased proliferation, faster maturation and
CC increased sensitivity to apoptosis of immature NK cells, and lower
CC cytolytic response to KLRK1-sensitive tumor targets.
CC {ECO:0000269|PubMed:18394936, ECO:0000269|PubMed:19631564}.
CC -!- MISCELLANEOUS: Is not capable of signal transduction by itself; isoform
CC 1 operates either through the signaling adapter protein HCST and
CC isoform 2 through both HCST and TYROBP signaling adapter proteins
CC (PubMed:12426564). Some families of ligands for mouse and human KLRK1
CC receptors have been characterized being very similar in structure and
CC highly likely to be orthologs. In humans, an additional distinct
CC subfamily of ligands (MICA and MICB) differs structurally, having an
CC extra MHC alpha 3-like domain (PubMed:23298206).
CC {ECO:0000305|PubMed:12426564, ECO:0000305|PubMed:23298206}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=NKG2 D;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_286";
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DR EMBL; AF054819; AAC24356.1; -; mRNA.
DR EMBL; AF039026; AAD02117.1; -; mRNA.
DR EMBL; BC057147; AAH57147.1; -; mRNA.
DR EMBL; AF030313; AAC28245.1; -; mRNA.
DR CCDS; CCDS39660.1; -. [O54709-1]
DR CCDS; CCDS39661.1; -. [O54709-2]
DR RefSeq; NP_001076791.1; NM_001083322.2. [O54709-2]
DR RefSeq; NP_149069.1; NM_033078.4. [O54709-1]
DR PDB; 1HQ8; X-ray; 1.95 A; A=110-232.
DR PDB; 4PP8; X-ray; 1.95 A; A/B=109-232.
DR PDBsum; 1HQ8; -.
DR PDBsum; 4PP8; -.
DR AlphaFoldDB; O54709; -.
DR SMR; O54709; -.
DR BioGRID; 205095; 3.
DR IntAct; O54709; 1.
DR STRING; 10090.ENSMUSP00000032252; -.
DR GlyGen; O54709; 3 sites.
DR iPTMnet; O54709; -.
DR PhosphoSitePlus; O54709; -.
DR EPD; O54709; -.
DR PaxDb; O54709; -.
DR PRIDE; O54709; -.
DR ProteomicsDB; 293667; -. [O54709-1]
DR ProteomicsDB; 293668; -. [O54709-2]
DR ABCD; O54709; 2 sequenced antibodies.
DR Antibodypedia; 23295; 687 antibodies from 36 providers.
DR DNASU; 27007; -.
DR Ensembl; ENSMUST00000032252; ENSMUSP00000032252; ENSMUSG00000030149. [O54709-1]
DR Ensembl; ENSMUST00000095412; ENSMUSP00000093061; ENSMUSG00000030149. [O54709-2]
DR GeneID; 27007; -.
DR KEGG; mmu:27007; -.
DR UCSC; uc009egf.2; mouse. [O54709-1]
DR CTD; 22914; -.
DR MGI; MGI:1196250; Klrk1.
DR VEuPathDB; HostDB:ENSMUSG00000030149; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154558; -.
DR HOGENOM; CLU_049894_9_1_1; -.
DR InParanoid; O54709; -.
DR OMA; PLFFCCF; -.
DR PhylomeDB; O54709; -.
DR TreeFam; TF336674; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-2424491; DAP12 signaling.
DR BioGRID-ORCS; 27007; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Klrk1; mouse.
DR EvolutionaryTrace; O54709; -.
DR PRO; PR:O54709; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O54709; protein.
DR Bgee; ENSMUSG00000030149; Expressed in skin of snout and 76 other tissues.
DR ExpressionAtlas; O54709; baseline and differential.
DR Genevisible; O54709; MM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0042288; F:MHC class I protein binding; IPI:MGI.
DR GO; GO:0032394; F:MHC class Ib receptor activity; IMP:MGI.
DR GO; GO:0038023; F:signaling receptor activity; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:MGI.
DR GO; GO:0030101; P:natural killer cell activation; IMP:MGI.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:2000502; P:negative regulation of natural killer cell chemotaxis; IEA:Ensembl.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:MGI.
DR GO; GO:0030887; P:positive regulation of myeloid dendritic cell activation; ISO:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
DR GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:MGI.
DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; IMP:MGI.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR042169; NKG2D.
DR InterPro; IPR033992; NKR-like_CTLD.
DR PANTHER; PTHR47494; PTHR47494; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Differentiation; Disulfide bond; Glycoprotein; Immunity; Innate immunity;
KW Lectin; Membrane; Receptor; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..232
FT /note="NKG2-D type II integral membrane protein"
FT /id="PRO_0000046668"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..89
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 122..228
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 112..121
FT DISULFID 115..126
FT DISULFID 143..227
FT DISULFID 205..219
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9464811"
FT /id="VSP_053945"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4PP8"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1HQ8"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:1HQ8"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:1HQ8"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1HQ8"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:1HQ8"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:1HQ8"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1HQ8"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1HQ8"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1HQ8"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1HQ8"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1HQ8"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1HQ8"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:1HQ8"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:1HQ8"
SQ SEQUENCE 232 AA; 26710 MW; 050536EF8C23088A CRC64;
MALIRDRKSH HSEMSKCHNY DLKPAKWDTS QEQQKQRLAL TTSQPGENGI IRGRYPIEKL
KISPMFVVRV LAIALAIRFT LNTLMWLAIF KETFQPVLCN KEVPVSSREG YCGPCPNNWI
CHRNNCYQFF NEEKTWNQSQ ASCLSQNSSL LKIYSKEEQD FLKLVKSYHW MGLVQIPANG
SWQWEDGSSL SYNQLTLVEI PKGSCAVYGS SFKAYTEDCA NLNTYICMKR AV
