NKG2D_MACFA
ID NKG2D_MACFA Reviewed; 216 AA.
AC P61252;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Natural killer cell;
RA Biassoni R.;
RT "Macaca fascicularis NKG2D NK receptor.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Heterohexamer composed of two
CC subunits of KLRK1 and four subunits of HCST/DAP10. Interacts (via
CC transmembrane domain) with HCST/DAP10 (via transmembrane domain); the
CC interaction is required for KLRK1 NK cell surface and induces NK cell-
CC mediated cytotoxicity. Can form disulfide-bonded heterodimer with CD94
CC (By similarity). Interacts with CEACAM1; recruits PTPN6 that
CC dephosphorylates VAV1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P26718}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}. Note=Colocalized with HCST on the cell
CC surface. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Natural killer cells.
CC -!- MISCELLANEOUS: Is not capable of signal transduction by itself, but
CC operates through the adapter protein HCST. {ECO:0000250}.
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DR EMBL; AJ426429; CAD19993.1; -; mRNA.
DR RefSeq; NP_001270213.1; NM_001283284.1.
DR RefSeq; XP_015285653.1; XM_015430167.1.
DR AlphaFoldDB; P61252; -.
DR SMR; P61252; -.
DR STRING; 9541.XP_005570175.1; -.
DR ABCD; P61252; 36 sequenced antibodies.
DR Ensembl; ENSMFAT00000087397; ENSMFAP00000059183; ENSMFAG00000032496.
DR GeneID; 102120479; -.
DR KEGG; mcf:102120479; -.
DR VEuPathDB; HostDB:ENSMFAG00000032496; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154558; -.
DR OMA; PLFFCCF; -.
DR OrthoDB; 1201127at2759; -.
DR Proteomes; UP000233100; Chromosome 11.
DR Bgee; ENSMFAG00000032496; Expressed in lymph node and 7 other tissues.
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:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0042288; F:MHC class I protein binding; IEA:Ensembl.
DR GO; GO:0032394; F:MHC class Ib receptor activity; IEA:Ensembl.
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; 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: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; 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 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 2: Evidence at transcript level;
KW Adaptive immunity; Cell membrane; Differentiation; Disulfide bond;
KW Glycoprotein; Immunity; Innate immunity; Lectin; Membrane; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..216
FT /note="NKG2-D type II integral membrane protein"
FT /id="PRO_0000046666"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 98..213
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 99..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 127..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 189..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 216 AA; 25075 MW; A44883F31400DEAC CRC64;
MGWIRGRRPR HNLEMSEFHN YKLGLAKSDF STRCQKQRCP VIKSKCRENA SPLFFCCFIA
VAMGIRFIIM VTIWSAVFLN SLFNQEVQIP LTESYCGPCP KNWICYKNNC YQFFNESKNW
YESQASCMSQ NASLLKVYSK EDQDLLKLVK SYHWMGLVHI PTNGSWQWED GSILSPNLLT
IIEMQKGDCA LYASSFKGYI ENCSIPNTYI CMQRTV
