NKG2D_PIG
ID NKG2D_PIG Reviewed; 214 AA.
AC Q9GLF5; Q9GL58;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 89.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=11398969; DOI=10.1007/s002510100321;
RA Yim D., Jie H.-B., Sotiriadis J., Kim Y.-S., Kim K.-S., Rothschild M.F.,
RA Lanier L.L., Kim Y.B.;
RT "Molecular cloning and characterization of pig immunoreceptor DAP10 and
RT NKG2D.";
RL Immunogenetics 53:243-249(2001).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GLF5-1; Sequence=Displayed;
CC Name=2; Synonyms=Truncated;
CC IsoId=Q9GLF5-2; Sequence=VSP_022793, VSP_022794;
CC -!- TISSUE SPECIFICITY: Detected in peripheral blood leukocytes,
CC macrophages, monocytes and natural killer cells.
CC {ECO:0000269|PubMed:11398969}.
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; AF285448; AAG29426.1; -; mRNA.
DR EMBL; AF313487; AAG33631.1; -; mRNA.
DR RefSeq; NP_998978.2; NM_213813.2. [Q9GLF5-1]
DR AlphaFoldDB; Q9GLF5; -.
DR SMR; Q9GLF5; -.
DR STRING; 9823.ENSSSCP00000000676; -.
DR PaxDb; Q9GLF5; -.
DR PRIDE; Q9GLF5; -.
DR GeneID; 396737; -.
DR KEGG; ssc:396737; -.
DR CTD; 22914; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q9GLF5; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; Alternative splicing; Cell membrane; Differentiation;
KW Disulfide bond; Glycoprotein; Immunity; Innate immunity; Lectin; Membrane;
KW Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..214
FT /note="NKG2-D type II integral membrane protein"
FT /id="PRO_0000274559"
FT TOPO_DOM 1..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 98..210
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 97..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 125..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 187..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 79..80
FT /note="LL -> CK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11398969"
FT /id="VSP_022793"
FT VAR_SEQ 81..214
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11398969"
FT /id="VSP_022794"
FT CONFLICT 6
FT /note="D -> G (in Ref. 1; AAG33631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 24773 MW; 22C0857BBE136362 CRC64;
MGWIRDRRSP SSMEIRELHN RDVINRGAFK SRQKRTQTLI TSKCGENPSP FFLARSIAIA
MGIRFIVMVM IYSGMIINLL FNQEAPSPLK ESYCGPCPKN WICYRNSCYQ FSNESKTWLQ
SQASCRSQNS SLLKIYSRED QDFFKLVKSY HWMGLVQIPT NRSWQWEDGS ILSPNQITMV
EMQNGSCAVY GSSFKGYTEN CLTLNTYICM KRTV
