KLRBF_RAT
ID KLRBF_RAT Reviewed; 217 AA.
AC Q63378;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Killer cell lectin-like receptor subfamily B member 1F;
DE AltName: Full=Natural killer cell surface protein NKR-P1F;
GN Name=Klrb1f {ECO:0000250|UniProtKB:Q8VD98};
GN Synonyms=Klrb1c {ECO:0000312|EMBL:ABO15819.1}, Nkrp1b,
GN Nkrp1d {ECO:0000303|PubMed:9390275}, Nkrp1f {ECO:0000303|PubMed:17462921};
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:0000305, ECO:0000312|EMBL:CAA66111.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Fischer 344 {ECO:0000312|EMBL:CAA66111.1};
RX PubMed=9390275;
RA Appasamy P.M., Kenniston T.W., Brissette-Storkus C.S., Chambers W.H.;
RT "NKR-P1dim/TCR alpha beta + T cells and natural killer cells share
RT expression of NKR-P1A and NKR-P1D.";
RL Nat. Immunol. 15:259-268(1996).
RN [2] {ECO:0000312|EMBL:ABO15819.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:ABO15825.1}, and
RC WAG {ECO:0000312|EMBL:ABO15819.1};
RC TISSUE=Spleen {ECO:0000312|EMBL:ABO15819.1};
RX PubMed=17462921; DOI=10.1016/j.immuni.2007.03.013;
RA Voigt S., Mesci A., Ettinger J., Fine J.H., Chen P., Chou W., Carlyle J.R.;
RT "Cytomegalovirus evasion of innate immunity by subversion of the NKR-
RT P1B:Ocil/Clr-b missing-self axis.";
RL Immunity 26:617-627(2007).
CC -!- FUNCTION: Binds CLEC2I/Clr-g leading to activation of natural killer
CC cells or stimulation of IL-2 production and proliferation of T-cells in
CC response to antigen stimulation. May contribute to the formation of the
CC immunological synapse between T-cells and antigen-presenting dendritic
CC cells (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in natural killer cells and a subset of
CC T-cells. {ECO:0000269|PubMed:9390275}.
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DR EMBL; X97477; CAA66111.1; -; mRNA.
DR EMBL; EF100679; ABO15819.1; -; mRNA.
DR EMBL; EF100685; ABO15825.1; -; mRNA.
DR RefSeq; NP_001078872.1; NM_001085403.1.
DR RefSeq; XP_008761551.1; XM_008763329.1.
DR RefSeq; XP_008761552.1; XM_008763330.2.
DR AlphaFoldDB; Q63378; -.
DR SMR; Q63378; -.
DR STRING; 10116.ENSRNOP00000010312; -.
DR PaxDb; Q63378; -.
DR Ensembl; ENSRNOT00000010312; ENSRNOP00000010312; ENSRNOG00000007811.
DR GeneID; 683758; -.
DR KEGG; rno:683758; -.
DR CTD; 17059; -.
DR RGD; 1583336; LOC683758.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154685; -.
DR HOGENOM; CLU_049894_8_2_1; -.
DR InParanoid; Q63378; -.
DR OMA; QSTERSH; -.
DR OrthoDB; 1341815at2759; -.
DR PhylomeDB; Q63378; -.
DR PRO; PR:Q63378; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007811; Expressed in spleen and 11 other tissues.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; ISO:RGD.
DR GO; GO:0030101; P:natural killer cell activation; ISO:RGD.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:RGD.
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; Lectin; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..217
FT /note="Killer cell lectin-like receptor subfamily B member
FT 1F"
FT /id="PRO_0000317212"
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 DISULFID 122..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 189..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 217 AA; 24543 MW; D8ED2D1A07DEBFE4 CRC64;
MDTSRVYGNV KTFRSPGHKQ ASFPSLSTDA CRCPHWHHLA LKLGCATLIL LLLTLIGLSV
FVRFLVQKPL IEKCSMAAQE NGTEPTGRSA ILECPRHWQP HRNKCLIISQ ISRPWAEGLV
ACSMKEATLL IIENEEELKF VQNILKGRQQ LFFIGLNYVQ TEMTWKWING SVLKPNILRI
TGSEVENSCA LISHTEVFSD SCSSDNHWIC QKTLKHV
