KLRB1_RAT
ID KLRB1_RAT Reviewed; 214 AA.
AC Q0ZUP0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Killer cell lectin-like receptor subfamily B member 1;
DE AltName: Full=Immunoreceptor NKR-P1E;
DE AltName: Full=Killer cell lectin-like receptor subfamily B member 1G;
DE AltName: Full=Natural killer cell surface protein NKR-P1G;
DE AltName: Full=Natural killer lectin-like receptor 1E;
GN Name=Klrb1;
GN Synonyms=Klrb1d {ECO:0000312|EMBL:ABO15820.1}, Klrb1g,
GN Klrb6 {ECO:0000312|EMBL:ABA41356.1}, Nkrp1e {ECO:0000312|EMBL:ABA40405.1},
GN Nkrp1g {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:0000312|EMBL:ABO15820.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=WAG {ECO:0000312|EMBL:ABO15820.1};
RC TISSUE=Spleen {ECO:0000312|EMBL:ABO15820.1};
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).
RN [2] {ECO:0000312|EMBL:ABA41356.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PVG {ECO:0000312|EMBL:ABA41356.1};
RA Fossum S., Flornes L.M., Saether P.C., Dissen E.;
RT "Gene homogenization of exons encoding the ligand binding parts of
RT regulatory leukocyte receptors.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:ABA41356.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DA {ECO:0000312|EMBL:ABA40406.1}, and
RC PVG {ECO:0000312|EMBL:ABA40405.1};
RA Dai K.-Z., Naper C., Vaage J.T.;
RT "Novel NKR-P1E receptor expressed by rat NK cells.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
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DR EMBL; DQ157011; ABA40405.1; -; mRNA.
DR EMBL; DQ157012; ABA40406.1; -; mRNA.
DR EMBL; DQ113420; ABA41356.1; -; mRNA.
DR EMBL; EF100680; ABO15820.1; -; mRNA.
DR RefSeq; NP_001078874.1; NM_001085405.1.
DR AlphaFoldDB; Q0ZUP0; -.
DR SMR; Q0ZUP0; -.
DR STRING; 10116.ENSRNOP00000036493; -.
DR PaxDb; Q0ZUP0; -.
DR Ensembl; ENSRNOT00000084289; ENSRNOP00000072670; ENSRNOG00000057410.
DR GeneID; 689817; -.
DR KEGG; rno:689817; -.
DR UCSC; RGD:1587563; rat.
DR CTD; 3820; -.
DR RGD; 1587563; Klrb1.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154685; -.
DR HOGENOM; CLU_049894_8_2_1; -.
DR InParanoid; Q0ZUP0; -.
DR OMA; WHRVALK; -.
DR OrthoDB; 1341815at2759; -.
DR PhylomeDB; Q0ZUP0; -.
DR TreeFam; TF337735; -.
DR PRO; PR:Q0ZUP0; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000057410; Expressed in jejunum and 2 other tissues.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; 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..214
FT /note="Killer cell lectin-like receptor subfamily B member
FT 1"
FT /id="PRO_0000317214"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 98..208
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 119..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 186..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 214 AA; 23963 MW; CE2AC7D1C9417D90 CRC64;
MDAPVLYAEL HLANTQGLRC TSPPSPRQDA CWGSGWHRVA LKLGCVGLIL LLMGLSVLVG
FLVQKPPIEK CSVAVQENKT EPTVRSTILE CPRDWHLHWN KCLFISQTSR PWAEGLADCS
LRGATLLLIG DGKELKLLQD FSKGKGQQFF IGLKYVQEDK VWKWMNGSIL NTNLLRITGK
NEENSCALIS HTEVFSDSCS SDNHWICQKT LKRV