NKG2D_PANTR
ID NKG2D_PANTR Reviewed; 216 AA.
AC Q9MZ37; Q05HF9;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11751968; DOI=10.4049/jimmunol.168.1.240;
RA Shum B.P., Flodin L.R., Muir D.G., Rajalingam R., Khakoo S.I., Cleland S.,
RA Guethlein L.A., Uhrberg M., Parham P.;
RT "Conservation and variation in human and common chimpanzee CD94 and NKG2
RT genes.";
RL J. Immunol. 168:240-252(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoid tissue;
RA Biassoni R., Radic L., Faravelli A., De Maria A.;
RT "Conserved NK receptors in primates.";
RL Submitted (OCT-2005) 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; AF259063; AAF86971.1; -; mRNA.
DR EMBL; AM113545; CAJ34533.1; -; mRNA.
DR RefSeq; NP_001009059.1; NM_001009059.1.
DR RefSeq; XP_009423046.1; XM_009424771.2.
DR RefSeq; XP_009423047.1; XM_009424772.2.
DR RefSeq; XP_009423048.1; XM_009424773.2.
DR AlphaFoldDB; Q9MZ37; -.
DR SMR; Q9MZ37; -.
DR STRING; 9598.ENSPTRP00000007992; -.
DR PaxDb; Q9MZ37; -.
DR Ensembl; ENSPTRT00000008649; ENSPTRP00000007992; ENSPTRG00000004672.
DR GeneID; 450153; -.
DR KEGG; ptr:450153; -.
DR CTD; 22914; -.
DR VGNC; VGNC:52050; KLRK1.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154558; -.
DR HOGENOM; CLU_049894_9_1_1; -.
DR InParanoid; Q9MZ37; -.
DR OMA; PLFFCCF; -.
DR OrthoDB; 1201127at2759; -.
DR TreeFam; TF336674; -.
DR Proteomes; UP000002277; Chromosome 12.
DR Bgee; ENSPTRG00000004672; Expressed in lymph node and 19 other tissues.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISS:UniProtKB.
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_0000046669"
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; 25303 MW; 30DD0FF401D99BE1 CRC64;
MGWIRGRRSR HSWEMSEFHN YNLDLKKSDF STRWQKQRCP VVKSKCRENA SPFFFCCFIA
VAMGIRFIIM VTIWSAVFLN SLFNQEVQIP LTESYCGPCP KNWICYKNNC YQFFNESKNW
YESQASCMSQ NASLLKVYSK EDQDLLKLVK SYHWMGLVHI PTNGSWQWED GSILSPNLLT
IIEMQKGDCA LYASSFKGYI ENCSTPNTYI CMQRTV
