KLRBC_MOUSE
ID KLRBC_MOUSE Reviewed; 223 AA.
AC P27814; Q541U5; Q925G3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Killer cell lectin-like receptor subfamily B member 1C;
DE AltName: Full=CD161 antigen-like family member C;
DE AltName: Full=Lymphocyte antigen 55c;
DE Short=Ly-55c;
DE AltName: Full=NK1.1;
DE AltName: Full=NKR-P1.9;
DE AltName: Full=NKR-P1C;
DE AltName: Full=Natural killer cell surface protein P1-40;
DE Short=NKR-P1 40;
DE AltName: CD_antigen=CD161c;
GN Name=Klrb1c; Synonyms=Ly55c, Nkrp1c;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1880421;
RA Giorda R., Trucco M.;
RT "Mouse NKR-P1. A family of genes selectively coexpressed in adherent
RT lymphokine-activated killer cells.";
RL J. Immunol. 147:1701-1708(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=1506685;
RA Ryan J.C., Turck J., Niemi E.C., Yokoyama W.M., Seaman W.E.;
RT "Molecular cloning of the NK1.1 antigen, a member of the NKR-P1 family of
RT natural killer cell activation molecules.";
RL J. Immunol. 149:1631-1635(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=10229823;
RA Kung S.K.P., Su R.-C., Shannon J., Miller R.G.;
RT "The NKR-P1B gene product is an inhibitory receptor on SJL/J NK cells.";
RL J. Immunol. 162:5876-5887(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=11685472; DOI=10.1007/s002510100367;
RA Plougastel B., Matsumoto K., Dubbelde C., Yokoyama W.M.;
RT "Analysis of a 1-Mb BAC contig overlapping the mouse Nkrp1 cluster of
RT genes: cloning of three new Nkrp1 members, Nkrp1d, Nkrp1e, and Nkrp1f.";
RL Immunogenetics 53:592-598(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart, and 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).
RN [7]
RP FUNCTION.
RX PubMed=12813047; DOI=10.1074/jbc.m212869200;
RA Ljutic B., Carlyle J.R., Zuniga-Pfluecker J.C.;
RT "Identification of upstream cis-acting regulatory elements controlling
RT lineage-specific expression of the mouse NK cell activation receptor, NKR-
RT P1C.";
RL J. Biol. Chem. 278:31909-31917(2003).
RN [8]
RP INTERACTION WITH LCK, MUTAGENESIS OF TYR-7 AND CYS-31, AND FUNCTION.
RX PubMed=15814704; DOI=10.4049/jimmunol.174.8.4789;
RA Ljutic B., Carlyle J.R., Filipp D., Nakagawa R., Julius M.,
RA Zuniga-Pfluecker J.C.;
RT "Functional requirements for signaling through the stimulatory and
RT inhibitory mouse NKR-P1 (CD161) NK cell receptors.";
RL J. Immunol. 174:4789-4796(2005).
RN [9]
RP ANTI-NK1.1 MONOCLONAL ANTIBODY.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=16751398; DOI=10.4049/jimmunol.176.12.7511;
RA Carlyle J.R., Mesci A., Ljutic B., Belanger S., Tai L.-H., Rousselle E.,
RA Troke A.D., Proteau M.-F., Makrigiannis A.P.;
RT "Molecular and genetic basis for strain-dependent NK1.1 alloreactivity of
RT mouse NK cells.";
RL J. Immunol. 176:7511-7524(2006).
CC -!- FUNCTION: Plays a stimulatory role on natural killer (NK) cells
CC cytotoxicity. Activation by cross-linking of the receptor induces
CC Ca(2+) mobilization and interferon-gamma production.
CC {ECO:0000269|PubMed:12813047, ECO:0000269|PubMed:15814704}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with tyrosine kinase
CC LCK. {ECO:0000269|PubMed:15814704}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P27814-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27814-2; Sequence=VSP_022317;
CC -!- TISSUE SPECIFICITY: Expressed in natural killer cells.
CC -!- MISCELLANEOUS: The anti-NK1.1 monoclonal antibody (PK136), recognizing
CC Klrb1b and Klrb1c genes, is known to identify NK cells from B6 and SLJ
CC mice, but not from BALB/c ones. A single mutation Thr-191 present in
CC Klrb1b and Klrb1c genes of BALB/c mice may be responsible for lack of
CC NK1.1 reactivity in these mice. Indeed, when Lys-217 of BALB/c mice
CC Klrb1c is mutated to Glu-217 present in B6 and SLJ mice, it does not
CC confer NK1.1 reactivity.
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DR EMBL; M77678; AAA39824.1; -; mRNA.
DR EMBL; AF354263; AAK39103.1; -; mRNA.
DR EMBL; AY007206; AAG02283.1; -; Genomic_DNA.
DR EMBL; AK079743; BAC37739.1; -; mRNA.
DR EMBL; BC061168; AAH61168.1; -; mRNA.
DR CCDS; CCDS39654.2; -. [P27814-2]
DR CCDS; CCDS51919.1; -. [P27814-1]
DR PIR; C46467; C46467.
DR RefSeq; NP_001153376.1; NM_001159904.1.
DR RefSeq; NP_032553.2; NM_008527.2.
DR AlphaFoldDB; P27814; -.
DR SMR; P27814; -.
DR BioGRID; 201235; 2.
DR STRING; 10090.ENSMUSP00000134504; -.
DR GlyGen; P27814; 3 sites.
DR PhosphoSitePlus; P27814; -.
DR SWISS-2DPAGE; P27814; -.
DR MaxQB; P27814; -.
DR PaxDb; P27814; -.
DR PRIDE; P27814; -.
DR ProteomicsDB; 263636; -. [P27814-1]
DR ProteomicsDB; 263637; -. [P27814-2]
DR DNASU; 17059; -.
DR GeneID; 17059; -.
DR KEGG; mmu:17059; -.
DR CTD; 17059; -.
DR MGI; MGI:107538; Klrb1c.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P27814; -.
DR OrthoDB; 1341815at2759; -.
DR PhylomeDB; P27814; -.
DR BioGRID-ORCS; 17059; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Klrb1c; mouse.
DR PRO; PR:P27814; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P27814; protein.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0030101; P:natural killer cell activation; IDA:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:MGI.
DR GO; GO:0042269; P:regulation of natural killer cell mediated cytotoxicity; 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; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..223
FT /note="Killer cell lectin-like receptor subfamily B member
FT 1C"
FT /id="PRO_0000046678"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 101..211
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 31..34
FT /note="LCK-binding motif"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 122..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 189..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 87..89
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1506685,
FT ECO:0000303|PubMed:1880421"
FT /id="VSP_022317"
FT MUTAGEN 7
FT /note="Y->F: Decreased Ca(2+) mobilization."
FT /evidence="ECO:0000269|PubMed:15814704"
FT MUTAGEN 31
FT /note="C->S: Absence of Ca(2+) mobilization and no LCK
FT association."
FT /evidence="ECO:0000269|PubMed:15814704"
SQ SEQUENCE 223 AA; 25077 MW; F7022264A3000CDA CRC64;
MDTASIYLGL KPPRTLGAWH ESPPSLPPDA CRCPRSHRLA LKLSCAGLIL LVLTLIGMSV
LVRVLVQKPS REKCCVFIQE NLNKTTDCSV NLECPQDWLL HRDKCFHVSQ VSNTWEEGQA
DCGRKGATLL LIQDQEELRF LLDSIKEKYN SFWIGLRFTL PDMNWKWING TTFNSDVLKI
TGVTENGSCA SILGDKVTPE SCASDNRWIC QKELNHETPS NDS
