KLRI2_MOUSE
ID KLRI2_MOUSE Reviewed; 248 AA.
AC Q5DT36; Q8BS07;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Killer cell lectin-like receptor subfamily I member 2 {ECO:0000303|PubMed:15650876};
GN Name=Klri2 {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;
RN [1] {ECO:0000312|EMBL:AAR00558.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAR00558.1};
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|EMBL:BAC30742.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC30742.1};
RC TISSUE=Aorta {ECO:0000312|EMBL:BAC30742.1}, and
RC Vein {ECO:0000312|EMBL:BAC30742.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {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 [4] {ECO:0000312|EMBL:AAI32407.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Lectin-like receptor for natural killer (NK) cells.
CC Heterodimer formation with KLRE1 mediates NK cell cytolytic activity.
CC {ECO:0000250|UniProtKB:Q5DT37}.
CC -!- SUBUNIT: Heterodimer with KLRE1. {ECO:0000250|UniProtKB:Q5DT37}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5DT37};
CC Single-pass type II membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in natural killer (NK) cells.
CC {ECO:0000269|PubMed:15650876}.
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DR EMBL; AY324873; AAR00558.1; -; mRNA.
DR EMBL; AK040915; BAC30742.1; -; mRNA.
DR EMBL; AC171002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132406; AAI32407.1; -; mRNA.
DR EMBL; BC132408; AAI32409.1; -; mRNA.
DR CCDS; CCDS20594.1; -.
DR RefSeq; NP_796129.2; NM_177155.4.
DR AlphaFoldDB; Q5DT36; -.
DR SMR; Q5DT36; -.
DR STRING; 10090.ENSMUSP00000052805; -.
DR GlyGen; Q5DT36; 3 sites.
DR iPTMnet; Q5DT36; -.
DR PhosphoSitePlus; Q5DT36; -.
DR PaxDb; Q5DT36; -.
DR PRIDE; Q5DT36; -.
DR DNASU; 320407; -.
DR Ensembl; ENSMUST00000050385; ENSMUSP00000052805; ENSMUSG00000043932.
DR GeneID; 320407; -.
DR KEGG; mmu:320407; -.
DR UCSC; uc009egr.2; mouse.
DR CTD; 320407; -.
DR MGI; MGI:2443965; Klri2.
DR VEuPathDB; HostDB:ENSMUSG00000043932; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000164228; -.
DR HOGENOM; CLU_049894_9_2_1; -.
DR InParanoid; Q5DT36; -.
DR OMA; SKNDECS; -.
DR OrthoDB; 1105684at2759; -.
DR PhylomeDB; Q5DT36; -.
DR TreeFam; TF336674; -.
DR BioGRID-ORCS; 320407; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q5DT36; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q5DT36; protein.
DR Bgee; ENSMUSG00000043932; Expressed in spleen and 6 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; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..248
FT /note="Killer cell lectin-like receptor subfamily I member
FT 2"
FT /id="PRO_0000442201"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 80..100
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..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 REGION 19..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 227
FT /note="R -> H (in Ref. 2; BAC30742)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 28848 MW; 3C2B7793879078EC CRC64;
MHKKKHIKHG TNKQEIINIG TKSPTFQEKQ RPSKTDQRST VWREEQKKQE LKVHRIFHPQ
PRTGFDVGKG IDPWLTTWQM ITVILATLCI ILVTKVGFLI PSLFSKGEKQ SRKFSLLDPL
CDRNDDSSCD FCSSDWIAFG NNFYCVFREN SKTWVESQSA CEELNSHLVI IDSKAEVENL
LLFEMDGWIL HRMDGTNSSR LWGNDIKIRN TLMNDSEKKN HSCHYLRGNI FMPDECSAKK
TYICEFNI
