ID NKG2D_RAT Reviewed; 215 AA. AC O70215; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 14-OCT-2015, entry version 103. 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=NK lectin-like receptor; DE Short=NKLLR; DE AltName: Full=NKG2-D-activating NK receptor; DE AltName: Full=NKR-P2; DE AltName: CD_antigen=CD314; GN Name=Klrk1; Synonyms=Nkg2d, Nkrp2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=Fischer 344; TISSUE=Natural killer cell; RX PubMed=9620593; DOI=10.1093/intimm/10.4.379; RA Berg S.F., Dissen E., Westgaard I.H., Fossum S.; RT "Molecular characterization of rat NKR-P2, a lectin-like receptor RT expressed by NK cells and resting T cells."; RL Int. Immunol. 10:379-385(1998). RN [2] RP FUNCTION, AND 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). CC -!- FUNCTION: Function as an activating and costimulatory receptor CC involved in immunosurveillance upon binding to various cellular CC stress-inducible ligands displayed at the surface of autologous CC tumor cells and virus-infected cells. Provides both stimulatory CC and costimulatory innate immune responses on activated killer (NK) CC cells, leading to cytotoxic activity. Acts as a costimulatory CC receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated CC adaptive immune responses by amplifying T-cell activation. CC Stimulates perforin-mediated elimination of ligand-expressing CC tumor cells. Signaling involves calcium influx, culminating in the CC expression of TNF-alpha. Participates in NK cell-mediated bone CC marrow graft rejection. May play a regulatory role in CC differentiation and survival of NK cells. Binds to ligands CC belonging to various subfamilies of MHC class I-related CC glycoproteins. {ECO:0000269|PubMed:15048723}. CC -!- SUBUNIT: Homodimer; disulfide-linked. Heterohexamer composed of CC two subunits of KLRK1 and four subunits of HCST/DAP10. Interacts CC (via transmembrane domain) with HCST/DAP10 (via transmembrane CC domain); the interaction is required for KLRK1 NK cell surface and CC induces NK cell-mediated cytotoxicity. Can form disulfide-bonded CC heterodimer with CD94 (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass CC type II membrane protein {ECO:0000250}. Note=Colocalized with HCST CC on the cell surface. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed by natural killer cells and by CC resting thoracic duct CD4+ and CD8+ T-cells, but not by thymocytes CC or other hemopoietic cells. Expressed by DC cells. CC {ECO:0000269|PubMed:15048723, ECO:0000269|PubMed:9620593}. CC -!- MISCELLANEOUS: Is not capable of signal transduction by itself, CC but operates through the adapter protein HCST. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 C-type lectin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00040}. 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; AF009511; AAC40092.1; -; mRNA. DR RefSeq; NP_598196.1; NM_133512.2. DR RefSeq; XP_006237139.1; XM_006237077.2. DR UniGene; Rn.14544; -. DR ProteinModelPortal; O70215; -. DR SMR; O70215; 93-215. DR STRING; 10116.ENSRNOP00000012886; -. DR PRIDE; O70215; -. DR Ensembl; ENSRNOT00000088151; ENSRNOP00000074391; ENSRNOG00000061739. DR GeneID; 24934; -. DR KEGG; rno:24934; -. DR UCSC; RGD:3180; rat. DR CTD; 22914; -. DR RGD; 3180; Klrk1. DR eggNOG; NOG315914; -. DR GeneTree; ENSGT00730000110282; -. DR HOGENOM; HOG000220925; -. DR HOVERGEN; HBG052629; -. DR InParanoid; O70215; -. DR KO; K06728; -. DR OMA; NDWICHR; -. DR OrthoDB; EOG7NW6B5; -. DR PhylomeDB; O70215; -. DR TreeFam; TF336674; -. DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-RNO-2172127; DAP12 interactions. DR Reactome; R-RNO-2424491; DAP12 signaling. DR NextBio; 604911; -. DR PRO; PR:O70215; -. DR Proteomes; UP000002494; Chromosome 4. DR Genevisible; O70215; RN. DR GO; GO:0009986; C:cell surface; ISS:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD. DR GO; GO:0030887; P:positive regulation of myeloid dendritic cell activation; IDA:RGD. DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISS:UniProtKB. DR GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IMP:RGD. DR Gene3D; 3.10.100.10; -; 1. DR InterPro; IPR001304; C-type_lectin. DR InterPro; IPR016186; C-type_lectin-like. DR InterPro; IPR016187; C-type_lectin_fold. 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 2: Evidence at transcript level; KW Adaptive immunity; Cell membrane; Complete proteome; Differentiation; KW Disulfide bond; Glycoprotein; Immunity; Innate immunity; Lectin; KW Membrane; Receptor; Reference proteome; Signal-anchor; Transmembrane; KW Transmembrane helix. FT CHAIN 1 215 NKG2-D type II integral membrane protein. FT /FTId=PRO_0000046670. FT TOPO_DOM 1 51 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 52 74 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 75 215 Extracellular. {ECO:0000255}. FT DOMAIN 105 211 C-type lectin. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT CARBOHYD 120 120 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 130 130 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 162 162 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 95 104 {ECO:0000255|PROSITE-ProRule:PRU00040}. FT DISULFID 98 109 {ECO:0000255|PROSITE-ProRule:PRU00040}. FT DISULFID 126 210 {ECO:0000255|PROSITE-ProRule:PRU00040}. FT DISULFID 188 202 {ECO:0000255|PROSITE-ProRule:PRU00040}. SQ SEQUENCE 215 AA; 24438 MW; B49C0364613031AF CRC64; MSKCHNYDLK PAKWDTSQEH QKQRSALPTS RPGENGIIRR RSSIEELKIS PLFVVRVLVA AMTIRFTVIT LTWLAVFITL LCNKEVSVSS REGYCGPCPN DWICHRNNCY QFFNENKAWN QSQASCLSQN SSLLKIYSKE EQDFLKLVKS YHWMGLVQSP ANGSWQWEDG SSLSPNELTL VKTPSGTCAV YGSSFKAYTE DCSNPNTYIC MKRAV //