KLRBF_MOUSE
ID KLRBF_MOUSE Reviewed; 217 AA.
AC Q8VD98; Q1AFZ8; Q3TDT3; Q8C9Q1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Killer cell lectin-like receptor subfamily B member 1F;
DE AltName: Full=CD161 antigen-like family member F;
DE AltName: Full=Natural killer cell surface protein NKR-P1F;
DE AltName: CD_antigen=CD161f;
GN Name=Klrb1f; Synonyms=Nkrp1f;
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 [GENOMIC DNA / MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION.
RX PubMed=12858173; DOI=10.1038/ni954;
RA Iizuka K., Naidenko O.V., Plougastel B.F.M., Fremont D.H., Yokoyama W.M.;
RT "Genetically linked C-type lectin-related ligands for the NKRP1 family of
RT natural killer cell receptors.";
RL Nat. Immunol. 4:801-807(2003).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15963483; DOI=10.1016/j.cellimm.2005.04.021;
RA Tian W., Nunez R., Cheng S., Ding Y., Tumang J., Lyddane C., Roman C.,
RA Liou H.-C.;
RT "C-type lectin OCILRP2/Clr-g and its ligand NKRP1f costimulate T cell
RT proliferation and IL-2 production.";
RL Cell. Immunol. 234:39-53(2005).
RN [7]
RP FUNCTION.
RX PubMed=16143319; DOI=10.1016/j.cellimm.2005.07.004;
RA Tian W., Feng B., Liou H.-C.;
RT "Silencing OCILRP2 leads to intrinsic defects in T cells in response to
RT antigenic stimulation.";
RL Cell. Immunol. 235:72-84(2005).
CC -!- FUNCTION: Binds CLEC2I/Clr-g leading to activation of natural killer
CC cells or costimulation of IL-2 production and proliferation of T-cells
CC in response to antigen stimulation. May contribute to the formation of
CC the immunological synapse between T-cells and antigen-presenting
CC dendritic cells. {ECO:0000269|PubMed:12858173,
CC ECO:0000269|PubMed:15963483, ECO:0000269|PubMed:16143319}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in dendritic cells. Detectable in
CC natural killer cells. {ECO:0000269|PubMed:15963483}.
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DR EMBL; AF320600; AAL37201.1; -; Genomic_DNA.
DR EMBL; AY029597; AAK38158.1; -; mRNA.
DR EMBL; DQ143105; ABA43356.1; -; Genomic_DNA.
DR EMBL; DQ237931; ABB72029.1; -; mRNA.
DR EMBL; AK041601; BAC31001.1; -; mRNA.
DR EMBL; AK154278; BAE32484.1; -; mRNA.
DR EMBL; AK170023; BAE41516.1; -; mRNA.
DR EMBL; BC127142; AAI27143.1; -; mRNA.
DR CCDS; CCDS20579.1; -.
DR RefSeq; NP_694734.1; NM_153094.2.
DR AlphaFoldDB; Q8VD98; -.
DR SMR; Q8VD98; -.
DR STRING; 10090.ENSMUSP00000032257; -.
DR GlyGen; Q8VD98; 1 site.
DR PaxDb; Q8VD98; -.
DR PRIDE; Q8VD98; -.
DR ProteomicsDB; 265011; -.
DR DNASU; 232408; -.
DR Ensembl; ENSMUST00000032257; ENSMUSP00000032257; ENSMUSG00000030154.
DR GeneID; 232408; -.
DR KEGG; mmu:232408; -.
DR UCSC; uc009efa.2; mouse.
DR CTD; 232408; -.
DR MGI; MGI:2442965; Klrb1f.
DR VEuPathDB; HostDB:ENSMUSG00000030154; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154685; -.
DR HOGENOM; CLU_049894_8_2_1; -.
DR InParanoid; Q8VD98; -.
DR OMA; QSTERSH; -.
DR OrthoDB; 1341815at2759; -.
DR PhylomeDB; Q8VD98; -.
DR TreeFam; TF337735; -.
DR BioGRID-ORCS; 232408; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Klrb1f; mouse.
DR PRO; PR:Q8VD98; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8VD98; protein.
DR Bgee; ENSMUSG00000030154; Expressed in granulocyte and 31 other tissues.
DR ExpressionAtlas; Q8VD98; baseline and differential.
DR Genevisible; Q8VD98; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; 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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Lectin; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..217
FT /note="Killer cell lectin-like receptor subfamily B member
FT 1F"
FT /id="PRO_0000271480"
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..217
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 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 122..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 189..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 43
FT /note="S -> F (in Ref. 3; BAE32484/BAE41516)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="K -> E (in Ref. 3; BAC31001)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 24681 MW; 3C5244993647E990 CRC64;
MDTSKVHGNV KPFRCPGYKQ ASSPSFSPDA CRCPHWHHLA LKSGCAGLIL LLLSLIGLSV
LVRFLVQKPP IEKCSVAAQE NRTELTGRSA ILECPRYWHP HWNKCLFVSQ ISRPWAEGRD
ACSMEDAILL LIENKEELRF VQNLIKGKEQ LFFIGLKYVQ KEKIWKWIDG SILNPNLLRI
TGKDKENSCA IISHTEVFSD SCSSDNHWIC QKTLIHV
