KLRE1_MOUSE
ID KLRE1_MOUSE Reviewed; 226 AA.
AC Q8CJC7; Q80WP0;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Killer cell lectin-like receptor subfamily E member 1 {ECO:0000303|PubMed:12715246};
GN Name=Klre1 {ECO:0000303|PubMed:12715246};
GN Synonyms=NKG2I {ECO:0000303|PubMed:14707119};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAM44080.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=CB-17/SCID {ECO:0000312|EMBL:AAM44080.1};
RX PubMed=12782717; DOI=10.1084/jem.20021253;
RA Westgaard I.H., Dissen E., Torgersen K.M., Lazetic S., Lanier L.L.,
RA Phillips J.H., Fossum S.;
RT "The lectin-like receptor KLRE1 inhibits natural killer cell
RT cytotoxicity.";
RL J. Exp. Med. 197:1551-1561(2003).
RN [2] {ECO:0000312|EMBL:AAN31172.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAN31172.1};
RC TISSUE=Spleen {ECO:0000312|EMBL:AAN31172.1};
RX PubMed=14707119; DOI=10.1084/jem.20030851;
RA Koike J., Wakao H., Ishizuka Y., Sato T.A., Hamaoki M., Seino K.,
RA Koseki H., Nakayama T., Taniguchi M.;
RT "Bone marrow allograft rejection mediated by a novel murine NK receptor,
RT NKG2I.";
RL J. Exp. Med. 199:137-144(2004).
RN [3]
RP ERRATUM OF PUBMED:14707119.
RX DOI=10.1084/jem.20040120199137cor;
RA Koike J., Wakao H., Ishizuka Y., Sato T.A., Hamaoki M., Seino K.,
RA Koseki H., Nakayama T., Taniguchi M.;
RL J. Exp. Med. 199:435-435(2004).
RN [4] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0000305}
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=12715246; DOI=10.1007/s00251-003-0540-6;
RA Wilhelm B.T., Mager D.L.;
RT "Identification of a new murine lectin-like gene in close proximity to
RT CD94.";
RL Immunogenetics 55:53-56(2003).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15069013; DOI=10.1182/blood-2003-10-3468;
RA Shimizu E., Koike J., Wakao H., Seino K., Koseki H., Kakiuchi T.,
RA Nakayama T., Taniguchi M.;
RT "Role of a NK receptor, KLRE-1, in bone marrow allograft rejection:
RT analysis with KLRE-1-deficient mice.";
RL Blood 104:781-783(2004).
RN [7] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18713988; DOI=10.4049/jimmunol.181.5.3177;
RA Saether P.C., Westgaard I.H., Hoelsbrekken S.E., Benjamin J., Lanier L.L.,
RA Fossum S., Dissen E.;
RT "KLRE/I1 and KLRE/I2: a novel pair of heterodimeric receptors that
RT inversely regulate NK cell cytotoxicity.";
RL J. Immunol. 181:3177-3182(2008).
CC -!- FUNCTION: Lectin-like receptor for natural killer (NK) cells
CC (PubMed:14707119, PubMed:15069013, PubMed:18713988). Can either inhibit
CC or activate NK cell cytotoxic activity, depending on its binding
CC partner (PubMed:14707119, PubMed:15069013, PubMed:18713988).
CC Heterodimer formation with KLRI1 mediates NK cell inhibition whereas
CC heterodimer formation with KLRI2 mediates NK cell activation
CC (PubMed:18713988). Plays a role in allogeneic recognition by the immune
CC system (PubMed:14707119, PubMed:15069013).
CC {ECO:0000269|PubMed:14707119, ECO:0000269|PubMed:15069013,
CC ECO:0000269|PubMed:18713988}.
CC -!- SUBUNIT: Heterodimer; with KLRI1 or KLRI2.
CC {ECO:0000269|PubMed:14707119, ECO:0000269|PubMed:18713988}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12782717,
CC ECO:0000269|PubMed:14707119, ECO:0000269|PubMed:15069013,
CC ECO:0000269|PubMed:18713988}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in natural killer (NK) cells (at protein
CC level) (PubMed:12782717, PubMed:14707119, PubMed:12715246). Also
CC detected in natural killer T (NKT) cells (at protein level)
CC (PubMed:14707119, PubMed:12715246). Has little or no expression in T
CC cells (at protein level) (PubMed:14707119, PubMed:12715246).
CC {ECO:0000269|PubMed:12715246, ECO:0000269|PubMed:12782717,
CC ECO:0000269|PubMed:14707119}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile, with no gross abnormalities.
CC Development of natural killer (NK) cells appears to be normal.
CC Cytolytic activity of activated NK cells against allogeneic target
CC cells is significantly reduced. {ECO:0000269|PubMed:15069013}.
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DR EMBL; AY100458; AAM44080.1; -; mRNA.
DR EMBL; AF306663; AAN31172.1; -; mRNA.
DR EMBL; AC161602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS20589.1; -.
DR RefSeq; NP_705818.3; NM_153590.3.
DR RefSeq; XP_006506186.1; XM_006506123.3.
DR RefSeq; XP_006506189.1; XM_006506126.1.
DR RefSeq; XP_017177078.1; XM_017321589.1.
DR AlphaFoldDB; Q8CJC7; -.
DR SMR; Q8CJC7; -.
DR STRING; 10090.ENSMUSP00000055779; -.
DR GlyGen; Q8CJC7; 1 site.
DR PaxDb; Q8CJC7; -.
DR PRIDE; Q8CJC7; -.
DR ProteomicsDB; 264784; -.
DR DNASU; 243655; -.
DR Ensembl; ENSMUST00000053708; ENSMUSP00000055779; ENSMUSG00000050241.
DR GeneID; 243655; -.
DR KEGG; mmu:243655; -.
DR UCSC; uc009egb.1; mouse.
DR CTD; 243655; -.
DR MGI; MGI:2662547; Klre1.
DR VEuPathDB; HostDB:ENSMUSG00000050241; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000164373; -.
DR HOGENOM; CLU_049894_9_3_1; -.
DR InParanoid; Q8CJC7; -.
DR OMA; VWFRCSC; -.
DR OrthoDB; 1311443at2759; -.
DR PhylomeDB; Q8CJC7; -.
DR TreeFam; TF336674; -.
DR BioGRID-ORCS; 243655; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Klre1; mouse.
DR PRO; PR:Q8CJC7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8CJC7; protein.
DR Bgee; ENSMUSG00000050241; Expressed in blood and 21 other tissues.
DR ExpressionAtlas; Q8CJC7; baseline and differential.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:MGI.
DR GO; GO:0030101; P:natural killer cell activation; IDA:MGI.
DR GO; GO:0002859; P:negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; IDA:MGI.
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 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Lectin; Membrane; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..226
FT /note="Killer cell lectin-like receptor subfamily E member
FT 1"
FT /id="PRO_0000442197"
FT TOPO_DOM 1..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 69..89
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..226
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 120..225
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 113..124
FT /evidence="ECO:0000250|UniProtKB:Q13241"
FT DISULFID 141..224
FT /evidence="ECO:0000250|UniProtKB:Q13241"
FT DISULFID 202..216
FT /evidence="ECO:0000250|UniProtKB:Q13241"
FT CONFLICT 136
FT /note="D -> E (in Ref. 1; AAM44080)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 26265 MW; FE1E25C0A80B2DFD CRC64;
MDEAPVTRST LNVNSQQKSK AKNKIKNTLN SNELSSIEQR KKYQKHLKKH KNTAEDISGK
GNCSPPWRLL SSVLGAMCLL LMAVAMVMTT FTTKSSSERS SSTIQQEGLH HPCPENWVWF
RCSCYFFSKE ELIWRDSQRA CLSLNSSLIR MNKEEMNFFS LKSFFWVGVY YNETRRQWLW
EDHSVLPSGL FSKLEANMKN FCASYKSKEA YMEENCANKL TYICKK
