NKG2C_MACMU
ID NKG2C_MACMU Reviewed; 231 AA.
AC Q9MZK6; Q9MZK4;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=NKG2-C type II integral membrane protein;
DE AltName: Full=CD159 antigen-like family member C;
DE AltName: Full=NK cell receptor C;
DE AltName: Full=NKG2-C-activating NK receptor;
DE AltName: CD_antigen=CD159c;
GN Name=KLRC2; Synonyms=NKG2C;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10866118; DOI=10.1007/s002510050650;
RA LaBonte M.L., Levy D.B., Letvin N.L.;
RT "Characterization of rhesus monkey CD94/NKG2 family members and
RT identification of novel transmembrane-deleted forms of NKG2-A, B, C, and
RT D.";
RL Immunogenetics 51:496-499(2000).
CC -!- FUNCTION: Immune activating receptor involved in self-nonself
CC discrimination. In complex with KLRD1 on cytotoxic lymphocyte subsets,
CC recognizes non-classical major histocompatibility MHC-E loaded with
CC signal sequence-derived peptides from non-classical MHC-G molecules,
CC likely playing a role in the generation and effector functions of
CC adaptive natural killer (NK) cells and in maternal-fetal tolerance
CC during pregnancy. Regulates the effector functions of terminally
CC differentiated cytotoxic lymphocyte subsets, and in particular may play
CC a role in adaptive NK cell response to viral infection. Upon MHC-E-
CC peptide binding, transmits intracellular signals via the adapter
CC protein TYROBP/DAP12, triggering the phosphorylation of proximal
CC signaling molecules and cell activation.
CC {ECO:0000250|UniProtKB:P26717}.
CC -!- SUBUNIT: Heterodimer with KLRD1; disulfide-linked. KLRD1-KLRC2 receptor
CC complex interacts with TYROBP/DAP12 homodimer; this interaction is
CC necessary for the expression on the cell surface.
CC {ECO:0000250|UniProtKB:P26717}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26717};
CC Single-pass type II membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Natural killer cells.
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DR EMBL; AF190934; AAF74530.1; -; mRNA.
DR EMBL; AF190936; AAF74532.1; -; mRNA.
DR AlphaFoldDB; Q9MZK6; -.
DR SMR; Q9MZK6; -.
DR STRING; 9544.ENSMMUP00000024085; -.
DR eggNOG; ENOG502S6IE; Eukaryota.
DR InParanoid; Q9MZK6; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0062081; F:activating MHC class Ib receptor activity; ISS:UniProtKB.
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:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0043323; P:positive regulation of natural killer cell degranulation; ISS:UniProtKB.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; 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; 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 Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Lectin; Membrane; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..231
FT /note="NKG2-C type II integral membrane protein"
FT /id="PRO_0000046663"
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..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 116..229
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 COMPBIAS 16..30
FT /note="Basic and acidic 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 DISULFID 117..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 145..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 206..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VARIANT 26
FT /note="D -> G"
FT VARIANT 35
FT /note="K -> E"
SQ SEQUENCE 231 AA; 26389 MW; 89A9336621F37681 CRC64;
MNKQRGTFSE VSLAQDPKRQ QRKPKDNKSS ISGTKQEIFQ VELNLQNPSL NHQGIDQIYD
CQGLLPPPEK LTAEVLGIIC IVLMATVLKT VVLIPFLEQN NSFPNTRTQK VRHCGHCPEE
WITYSNSCYY IGKEKRTWAE SLLACTSKNS SLLSIDNEEE MKFLTAISPS TWTGVFRDSS
HHPWVTINGL TFKHEIKDSD HAEYNCAMLH LDRLKSVQCG SSKRYYCKHK L
