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 16-APR-2014, entry version 91. 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. 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). CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane CC protein (By similarity). Note=Colocalized with HCST on the cell CC surface (By similarity). 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 -!- MISCELLANEOUS: Is not capable of signal transduction by itself, CC but operates through the adapter protein HCST (By similarity). CC -!- SIMILARITY: Contains 1 C-type lectin domain. 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_006237077.1. DR UniGene; Rn.14544; -. DR ProteinModelPortal; O70215; -. DR SMR; O70215; 93-215. DR STRING; 10116.ENSRNOP00000012886; -. DR PRIDE; O70215; -. DR Ensembl; ENSRNOT00000012886; ENSRNOP00000012886; ENSRNOG00000009638. 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 KO; K06728; -. DR OMA; NDWICHR; -. DR OrthoDB; EOG7NW6B5; -. DR PhylomeDB; O70215; -. DR TreeFam; TF336674; -. DR NextBio; 604911; -. DR PRO; PR:O70215; -. DR Genevestigator; O70215; -. DR GO; GO:0009986; C:cell surface; ISS:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0032394; F:MHC class Ib receptor activity; IEA:Ensembl. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl. DR GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISS:UniProtKB. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl. DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; IEA:Ensembl. 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 (Potential). FT TRANSMEM 52 74 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 75 215 Extracellular (Potential). FT DOMAIN 105 211 C-type lectin. FT CARBOHYD 120 120 N-linked (GlcNAc...) (Potential). FT CARBOHYD 130 130 N-linked (GlcNAc...) (Potential). FT CARBOHYD 162 162 N-linked (GlcNAc...) (Potential). FT DISULFID 95 104 By similarity. FT DISULFID 98 109 By similarity. FT DISULFID 126 210 By similarity. FT DISULFID 188 202 By similarity. 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 //