ID   NKG2E_PANTR             Reviewed;         240 AA.
AC   Q95MI4; Q95MI3;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=NKG2-E type II integral membrane protein;
DE   AltName: Full=NK cell receptor E;
DE   AltName: Full=NKG2-E-activating NK receptor;
GN   Name=KLRC3; Synonyms=NKG2E;
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], AND VARIANT ARG-213.
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).
CC   -!- FUNCTION: Plays a role as a receptor for the recognition of MHC class I
CC       HLA-E molecules by NK cells and some cytotoxic T-cells.
CC   -!- SUBUNIT: Can form disulfide-bonded heterodimer with CD94.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC   -!- TISSUE SPECIFICITY: Natural killer cells.
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DR   EMBL; AF350006; AAK83793.1; -; mRNA.
DR   EMBL; AF350007; AAK83794.1; -; mRNA.
DR   RefSeq; NP_001009017.1; NM_001009017.1.
DR   AlphaFoldDB; Q95MI4; -.
DR   SMR; Q95MI4; -.
DR   STRING; 9598.ENSPTRP00000007991; -.
DR   PaxDb; Q95MI4; -.
DR   GeneID; 449624; -.
DR   KEGG; ptr:449624; -.
DR   CTD; 3823; -.
DR   eggNOG; ENOG502S6IE; Eukaryota.
DR   InParanoid; Q95MI4; -.
DR   OrthoDB; 1161111at2759; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IBA:GO_Central.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; IBA:GO_Central.
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; IPR033992; NKR-like_CTLD.
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   Disulfide bond; Glycoprotein; Lectin; Membrane; Receptor;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..240
FT                   /note="NKG2-E type II integral membrane protein"
FT                   /id="PRO_0000046672"
FT   TOPO_DOM        1..70
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..93
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..240
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          116..230
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        117..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        207..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   VARIANT         213
FT                   /note="C -> R (in allele NKG2-E*02)"
FT                   /evidence="ECO:0000269|PubMed:11751968"
FT                   /id="VAR_018702"
SQ   SEQUENCE   240 AA;  26996 MW;  BC28FB3CEA93A5E0 CRC64;
     MNKQRGTFSE VSLAQDPKRQ QRKPKGNKSS ISATEQEIFQ VELNLQNASL NHQGIDKIYD
     CQGLLPPPEK LTAKMLGIIC IVLMSAVLKT IVLIPFLEQN NSSPNTRTQK ARPCGHCPEE
     WITYSNSCYY IGKERRTWEE SLQACASKNS SSLLSIDNEE EMKFLASILP SSWIGVFCNS
     SHHPWVTING LAFKHEIKDS DHAERNCAML HVCGLISDQC GSSRIIRRGF IMLTRLVLNS