KLRI2_RAT
ID KLRI2_RAT Reviewed; 247 AA.
AC Q5DT37;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Killer cell lectin-like receptor subfamily I member 2 {ECO:0000303|PubMed:15650876};
GN Name=Klri2 {ECO:0000303|PubMed:15650876};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|EMBL:AAR00557.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Fischer 344 {ECO:0000312|EMBL:AAR00557.1};
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:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3] {ECO:0000305}
RP FUNCTION, SUBUNIT, INTERACTION WITH KLRE1, 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 NK cell cytolytic activity.
CC {ECO:0000269|PubMed:18713988}.
CC -!- SUBUNIT: Heterodimer with KLRE1. {ECO:0000269|PubMed:18713988}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15650876,
CC ECO:0000269|PubMed:18713988}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in natural killer (NK) cells.
CC {ECO:0000269|PubMed:15650876}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY324871; AAR00557.1; -; mRNA.
DR EMBL; AC108288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001012666.1; NM_001012648.1.
DR AlphaFoldDB; Q5DT37; -.
DR SMR; Q5DT37; -.
DR STRING; 10116.ENSRNOP00000036796; -.
DR GlyGen; Q5DT37; 4 sites.
DR PhosphoSitePlus; Q5DT37; -.
DR PaxDb; Q5DT37; -.
DR Ensembl; ENSRNOT00000082002; ENSRNOP00000074478; ENSRNOG00000057643.
DR GeneID; 503650; -.
DR KEGG; rno:503650; -.
DR UCSC; RGD:1359205; rat.
DR CTD; 320407; -.
DR RGD; 1359205; Klri2.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000164228; -.
DR HOGENOM; CLU_049894_9_2_1; -.
DR InParanoid; Q5DT37; -.
DR OMA; SKNDECS; -.
DR OrthoDB; 1105684at2759; -.
DR PhylomeDB; Q5DT37; -.
DR TreeFam; TF336674; -.
DR PRO; PR:Q5DT37; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000057643; Expressed in spleen and 6 other tissues.
DR ExpressionAtlas; Q5DT37; baseline.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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: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 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 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..247
FT /note="Killer cell lectin-like receptor subfamily I member
FT 2"
FT /id="PRO_0000442202"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..247
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 139..243
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 160..242
FT /evidence="ECO:0000250|UniProtKB:Q13241"
FT DISULFID 221..234
FT /evidence="ECO:0000250|UniProtKB:Q13241"
SQ SEQUENCE 247 AA; 28814 MW; 90134CE6377ACA3B CRC64;
MPRKKQNERG TNKQEIINIE TKSSTFQEKQ RQSKTDQIST VWRKEQKKQE LKVHTELHPQ
HRTGFNEDKG TDPWLTTWRI ITVILGTSCI ILVTKVGFLI PNLFSRGEKR SRELSLLDSL
CLKNNDSFCD LCSHDWIAFG NNFYLFFRGT KTWAESKSAC EELNSYLLDI DSRAELENLL
LFEINGWILF KTDAINRSLR KNYIKIHQTL FNDSEKKNHS CHYLSGNQFS AGDCSSKKAY
TCEFNLQ
