KLRE1_RAT
ID KLRE1_RAT Reviewed; 226 AA.
AC Q80ZC8; Q80ST4;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Killer cell lectin-like receptor subfamily E member 1 {ECO:0000303|PubMed:12782717};
GN Name=Klre1 {ECO:0000303|PubMed:12782717};
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;
RN [1] {ECO:0000312|EMBL:AAO49445.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=DA {ECO:0000312|EMBL:AAO49445.1}, and
RC Fischer 344 {ECO:0000312|EMBL:AAO49446.1};
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:AC115156}
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:0000312|EMBL:EDM01724.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, SUBUNIT, INTERACTION WITH KLRI1 AND KLRI2, AND SUBCELLULAR
RP 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:12782717, PubMed:18713988). Can either inhibit or activate NK
CC cell cytotoxic activity, depending on its binding partner
CC (PubMed:18713988). Heterodimer formation with KLRI1 mediates NK cell
CC inhibition whereas heterodimer formation with KLRI2 mediates NK cell
CC activation (PubMed:18713988). Plays a role in allogeneic recognition by
CC the immune system (By similarity). {ECO:0000250|UniProtKB:Q8CJC7,
CC ECO:0000269|PubMed:18713988}.
CC -!- SUBUNIT: Heterodimer; with KLRI1 or KLRI2.
CC {ECO:0000269|PubMed:18713988}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12782717,
CC ECO:0000269|PubMed:18713988}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long {ECO:0000303|PubMed:12782717};
CC IsoId=Q80ZC8-1; Sequence=Displayed;
CC Name=2; Synonyms=Short {ECO:0000303|PubMed:12782717};
CC IsoId=Q80ZC8-2; Sequence=VSP_059201;
CC -!- TISSUE SPECIFICITY: Expressed in natural killer (NK) cells.
CC {ECO:0000269|PubMed:12782717}.
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DR EMBL; AF486185; AAO49444.1; -; mRNA.
DR EMBL; AF486186; AAO49445.1; -; mRNA.
DR EMBL; AF486187; AAO49446.1; -; mRNA.
DR EMBL; AC115156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473964; EDM01724.1; -; Genomic_DNA.
DR EMBL; CH473964; EDM01725.1; -; Genomic_DNA.
DR RefSeq; NP_852037.1; NM_181372.2. [Q80ZC8-1]
DR RefSeq; XP_006237144.1; XM_006237082.3. [Q80ZC8-2]
DR RefSeq; XP_008761533.1; XM_008763311.2. [Q80ZC8-2]
DR RefSeq; XP_017448082.1; XM_017592593.1. [Q80ZC8-1]
DR RefSeq; XP_017448083.1; XM_017592594.1. [Q80ZC8-1]
DR AlphaFoldDB; Q80ZC8; -.
DR SMR; Q80ZC8; -.
DR STRING; 10116.ENSRNOP00000010669; -.
DR GlyGen; Q80ZC8; 1 site.
DR PaxDb; Q80ZC8; -.
DR Ensembl; ENSRNOT00000084823; ENSRNOP00000074069; ENSRNOG00000058714. [Q80ZC8-2]
DR GeneID; 297645; -.
DR KEGG; rno:297645; -.
DR UCSC; RGD:727903; rat. [Q80ZC8-1]
DR CTD; 243655; -.
DR RGD; 727903; Klre1.
DR VEuPathDB; HostDB:ENSRNOG00000058714; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000164373; -.
DR HOGENOM; CLU_049894_9_3_1; -.
DR InParanoid; Q80ZC8; -.
DR OMA; VWFRCSC; -.
DR OrthoDB; 1311443at2759; -.
DR PhylomeDB; Q80ZC8; -.
DR TreeFam; TF336674; -.
DR PRO; PR:Q80ZC8; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Proteomes; UP000234681; Chromosome 4.
DR Bgee; ENSRNOG00000058714; Expressed in spleen and 11 other tissues.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:RGD.
DR GO; GO:0038023; F:signaling receptor activity; ISO:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISO:RGD.
DR GO; GO:2000502; P:negative regulation of natural killer cell chemotaxis; ISO:RGD.
DR GO; GO:0002859; P:negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IDA:RGD.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:RGD.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein; Lectin;
KW Membrane; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..226
FT /note="Killer cell lectin-like receptor subfamily E member
FT 1"
FT /id="PRO_0000442198"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 73..93
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..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 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 VAR_SEQ 1..24
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059201"
SQ SEQUENCE 226 AA; 26266 MW; 64334D81C03D758B CRC64;
MNQTLIICST LNVNSQQKSK AKNSMKNTFH SNELSSIEQR QKYQKHLKKD KKTAEDITGV
GNCSPPWRLI SSVLFVVCLL LMAVAMVMTI FTTRLSSERS SSNIHQEGLH HPCPENWVWF
RCSCYYFSKE KLVWRESQRA CLSFNSSLIR MNKEEMDFFS LKSFFWVGVY YDETSKQWLW
DDHSVLPSGM FSGLESSPKN FCASYKSKEA YLAENCSTKL MYICKK
