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Database: UniProt
Entry: O54707
LinkDB: O54707
Original site: O54707 
ID   KLRD1_MOUSE             Reviewed;         179 AA.
AC   O54707; O54708;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   10-APR-2019, entry version 129.
DE   RecName: Full=Natural killer cells antigen CD94;
DE   AltName: Full=Killer cell lectin-like receptor subfamily D member 1;
DE   AltName: CD_antigen=CD94;
GN   Name=Klrd1; Synonyms=Cd94;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-83.
RC   STRAIN=C57BL/6J, and CB.17 SCID;
RX   PubMed=9464811; DOI=10.1002/eji.1830271222;
RA   Vance R.E., Tanamachi D.M., Hanke T., Raulet D.H.;
RT   "Cloning of a mouse homolog of CD94 extends the family of C-type
RT   lectins on murine natural killer cells.";
RL   Eur. J. Immunol. 27:3236-3241(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=9600963; DOI=10.1073/pnas.95.11.6320;
RA   Ho E.L., Heusel J.W., Brown M.G., Matsumoto K., Scalzo A.A.,
RA   Yokoyama W.M.;
RT   "Murine Nkg2d and Cd94 are clustered within the natural killer complex
RT   and are expressed independently in natural killer cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:6320-6325(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RA   Butcher S., Cottage A., Cook G.P.;
RT   "Mouse natural killer cell receptors homologous to human CD94 and
RT   NKG2-D.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-83.
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays a role as a receptor for the recognition of MHC
CC       class I HLA-E molecules by NK cells and some cytotoxic T-cells.
CC       {ECO:0000250|UniProtKB:Q13241}.
CC   -!- SUBUNIT: Can form disulfide-bonded heterodimer with NKG2 family
CC       members (By similarity). Interacts with the adapter protein
CC       TYROBP/DAP12; the interaction leads to natural killer cell
CC       activation (By similarity). {ECO:0000250|UniProtKB:Q13241}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
CC       type II membrane protein {ECO:0000255}.
DR   EMBL; AF030311; AAC28243.1; -; mRNA.
DR   EMBL; AF030312; AAC28244.1; -; mRNA.
DR   EMBL; AF057714; AAC33713.1; -; mRNA.
DR   EMBL; AF039025; AAD02116.1; -; mRNA.
DR   EMBL; AK136548; BAE23039.1; -; mRNA.
DR   EMBL; CH466523; EDK99936.1; -; Genomic_DNA.
DR   EMBL; BC117112; AAI17113.1; -; mRNA.
DR   EMBL; BC120854; AAI20855.1; -; mRNA.
DR   CCDS; CCDS57456.1; -.
DR   RefSeq; NP_034784.1; NM_010654.3.
DR   RefSeq; XP_006505718.1; XM_006505655.1.
DR   UniGene; Mm.391515; -.
DR   ProteinModelPortal; O54707; -.
DR   SMR; O54707; -.
DR   STRING; 10090.ENSMUSP00000107694; -.
DR   PhosphoSitePlus; O54707; -.
DR   EPD; O54707; -.
DR   PaxDb; O54707; -.
DR   PRIDE; O54707; -.
DR   Ensembl; ENSMUST00000112063; ENSMUSP00000107694; ENSMUSG00000030165.
DR   GeneID; 16643; -.
DR   KEGG; mmu:16643; -.
DR   UCSC; uc009egd.2; mouse.
DR   CTD; 3824; -.
DR   MGI; MGI:1196275; Klrd1.
DR   eggNOG; KOG4297; Eukaryota.
DR   eggNOG; ENOG410XPJ1; LUCA.
DR   GeneTree; ENSGT00940000160107; -.
DR   HOGENOM; HOG000220925; -.
DR   InParanoid; O54707; -.
DR   KO; K06516; -.
DR   OMA; YSEEHHA; -.
DR   OrthoDB; 1389571at2759; -.
DR   PhylomeDB; O54707; -.
DR   TreeFam; TF336674; -.
DR   Reactome; R-MMU-2172127; DAP12 interactions.
DR   Reactome; R-MMU-2424491; DAP12 signaling.
DR   PRO; PR:O54707; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000030165; Expressed in 63 organ(s), highest expression level in blood.
DR   ExpressionAtlas; O54707; baseline and differential.
DR   Genevisible; O54707; MM.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0023024; F:MHC class I protein complex binding; ISO:MGI.
DR   GO; GO:0023030; F:MHC class Ib protein binding, via antigen binding groove; ISO:MGI.
DR   GO; GO:1990405; F:protein antigen binding; ISO:MGI.
DR   GO; GO:0002228; P:natural killer cell mediated immunity; ISO: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   2: Evidence at transcript level;
KW   Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
KW   Lectin; Membrane; Polymorphism; Receptor; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1    179       Natural killer cells antigen CD94.
FT                                /FTId=PRO_0000378458.
FT   TOPO_DOM      1     10       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     11     31       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     32    179       Extracellular. {ECO:0000255}.
FT   DOMAIN       68    175       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   CARBOHYD     93     93       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    109    109       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     58     70       {ECO:0000255|PROSITE-ProRule:PRU00040}.
FT   DISULFID     59     59       Interchain (with C-116 in NGK2A).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00040}.
FT   DISULFID     61     72       {ECO:0000255|PROSITE-ProRule:PRU00040}.
FT   DISULFID     89    174       {ECO:0000255|PROSITE-ProRule:PRU00040}.
FT   DISULFID    152    166       {ECO:0000255|PROSITE-ProRule:PRU00040}.
FT   VARIANT      83     83       K -> E. {ECO:0000269|PubMed:9464811,
FT                                ECO:0000269|Ref.5}.
SQ   SEQUENCE   179 AA;  20808 MW;  DD343419E93B3465 CRC64;
     MAVSRITRWR LMSVIFGIKC LFLMVTLGVL LINSFTIQNI QSTPSPTTTV EFQEVSECCV
     CLDKWVGHQC NCYFISKEEK SWKRSRDFCA SQNSSLLQPQ SRNELSFMNF SQTFFWIGMH
     YSEKRNAWLW EDGTVPSKDL FPEFSVIRPE HCIVYSPSKS VSAESCENKN RYICKKLPI
//
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