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KLRI1_MOUSE
ID   KLRI1_MOUSE             Reviewed;         248 AA.
AC   B2KG20; Q5DT35;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Killer cell lectin-like receptor subfamily I member 1 {ECO:0000303|PubMed:15650876};
GN   Name=Klri1 {ECO:0000303|PubMed:15650876};
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 {ECO:0000312|Proteomes:UP000000589};
RN   [1] {ECO:0000312|EMBL:AAR00559.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAR00559.1};
RX   PubMed=15650876; DOI=10.1007/s00251-004-0759-x;
RA   Saether P.C., Westgaard I.H., Flornes L.M., Hoelsbrekken S.E., Ryan J.C.,
RA   Fossum S., Dissen E.;
RT   "Molecular cloning of KLRI1 and KLRI2, a novel pair of lectin-like natural
RT   killer-cell receptors with opposing signalling motifs.";
RL   Immunogenetics 56:833-839(2005).
RN   [2] {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   [3] {ECO:0000305}
RP   FUNCTION, 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       Heterodimer formation with KLRE1 mediates inhibition of NK cell
CC       cytolytic activity. {ECO:0000269|PubMed:18713988}.
CC   -!- SUBUNIT: Heterodimer with KLRE1. Interacts with PTPN6.
CC       {ECO:0000250|UniProtKB:Q5DT39}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18713988};
CC       Single-pass type II membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in natural killer (NK) cells.
CC       {ECO:0000269|PubMed:15650876}.
CC   -!- DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred to as
CC       the immunoreceptor tyrosine-based inhibitor motif (ITIM). The
CC       phosphorylated ITIM motif can bind the SH2 domain of several SH2-
CC       containing phosphatases leading to down-regulation of cell activation.
CC       {ECO:0000250|UniProtKB:P27812}.
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DR   EMBL; AY324874; AAR00559.1; -; mRNA.
DR   EMBL; AC171002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS20593.1; -.
DR   RefSeq; NP_001012538.2; NM_001012520.2.
DR   AlphaFoldDB; B2KG20; -.
DR   SMR; B2KG20; -.
DR   STRING; 10090.ENSMUSP00000085362; -.
DR   GlyGen; B2KG20; 3 sites.
DR   PaxDb; B2KG20; -.
DR   PRIDE; B2KG20; -.
DR   Ensembl; ENSMUST00000088046; ENSMUSP00000085362; ENSMUSG00000067610.
DR   GeneID; 503550; -.
DR   KEGG; mmu:503550; -.
DR   UCSC; uc009egq.1; mouse.
DR   CTD; 503550; -.
DR   MGI; MGI:3530275; Klri1.
DR   VEuPathDB; HostDB:ENSMUSG00000067610; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000164228; -.
DR   HOGENOM; CLU_049894_9_2_1; -.
DR   InParanoid; B2KG20; -.
DR   OMA; CAKLNSH; -.
DR   OrthoDB; 1105684at2759; -.
DR   PhylomeDB; B2KG20; -.
DR   TreeFam; TF336674; -.
DR   BioGRID-ORCS; 503550; 4 hits in 72 CRISPR screens.
DR   PRO; PR:B2KG20; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; B2KG20; protein.
DR   Bgee; ENSMUSG00000067610; Expressed in spleen and 18 other tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
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   Cell membrane; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..248
FT                   /note="Killer cell lectin-like receptor subfamily I member
FT                   1"
FT                   /id="PRO_0000442199"
FT   TOPO_DOM        1..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        81..101
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          139..245
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   MOTIF           16..21
FT                   /note="ITIM motif 1"
FT                   /evidence="ECO:0000250|UniProtKB:P27812"
FT   MOTIF           47..52
FT                   /note="ITIM motif 2"
FT                   /evidence="ECO:0000250|UniProtKB:P27812"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        132..145
FT                   /evidence="ECO:0000250|UniProtKB:Q13241"
FT   DISULFID        161..244
FT                   /evidence="ECO:0000250|UniProtKB:Q13241"
FT   DISULFID        223..236
FT                   /evidence="ECO:0000250|UniProtKB:Q13241"
FT   CONFLICT        72
FT                   /note="Q -> H (in Ref. 1; AAR00559)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   248 AA;  28642 MW;  6A82D2A10CACE120 CRC64;
     MLHSKRREYT ANNQDVTYTE LKTCKSPWKH RIPTVKQSPV VLCEEQLKYG ELTFHRTPQP
     QPRKQAMGRK RQGPKSTVWR VVTGMLGALC VVLMTTTGIL LPKLFSSQEE QCRKTSLHPL
     RCPKDDASCD LCSSDWIAFG NNFYCVFKEN TKTWAESQSA CEELNSHLVI IDSKAEVENL
     LLFEMDGWIL HKMDGTNSSW LWRNDIKIQN TLTNDSEKKN HSCHYLRGNL FMPDECSAKK
     SYICEFNI
 
 
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