KRBBC_RAT
ID KRBBC_RAT Reviewed; 223 AA.
AC Q5NKN2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Killer cell lectin-like receptor subfamily B member 1B allele C;
DE AltName: Full=CD161 antigen-like family member B;
DE AltName: Full=Natural killer cell surface protein NKR-P1B allele TO;
DE AltName: CD_antigen=CD161b;
GN Name=Klrb1b {ECO:0000312|EMBL:AAQ11375.1};
GN Synonyms=Nkrp1b {ECO:0000250|UniProtKB:P27812};
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:AAQ11375.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=TO {ECO:0000312|EMBL:AAQ11375.1};
RA Hundrieser J., Wonigeit K.;
RT "mRNA for NKR-P1B protein of Rattus norvegicus strain TO.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=16547249; DOI=10.4049/jimmunol.176.7.4133;
RA Kveberg L., Baeck C.J., Dai K.-Z., Inngjerdingen M., Rolstad B., Ryan J.C.,
RA Vaage J.T., Naper C.;
RT "The novel inhibitory NKR-P1C receptor and Ly49s3 identify two
RT complementary, functionally distinct NK cell subsets in rats.";
RL J. Immunol. 176:4133-4140(2006).
RN [3] {ECO:0000305}
RP FUNCTION, AND POLYMORPHISM.
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: Receptor for CLEC2D/OCIL. Ligand-binding contributes to
CC inhibition of cytotoxic natural killer (NK) cells. May mediate MHC
CC class I-independent 'missing-self' recognition of allografts, tumor
CC cells and virus-infected cells. {ECO:0000269|PubMed:16547249,
CC ECO:0000269|PubMed:17462921}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with tyrosine kinase
CC LCK. Binds PTPN6/SHP-1 in a phosphorylation-dependent manner.
CC {ECO:0000250|UniProtKB:P27812, ECO:0000269|PubMed:16547249}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in a subset of natural killer cells.
CC {ECO:0000269|PubMed:16547249}.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). The
CC phosphorylated ITIM motif can bind the SH2 domain of several SH2-
CC containing phosphatases leading to down-regulation of cell activation
CC (By similarity). {ECO:0000250|UniProtKB:P27812}.
CC -!- POLYMORPHISM: Alleles A, B and C are highly divergent forms of Klrb1b.
CC Alleles A and B differ in their susceptibility to evasion of innate
CC immunity by the rat cytomegalovirus (CMV). In contrast to allele B,
CC allele A shows very low binding of a viral protein mimicking the Klrb1b
CC ligand CLEC2D as well as low susceptibility to this MHC class I-
CC independent viral evasion mechanism. {ECO:0000269|PubMed:17462921}.
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DR EMBL; AF541943; AAQ11375.1; -; mRNA.
DR AlphaFoldDB; Q5NKN2; -.
DR SMR; Q5NKN2; -.
DR UCSC; RGD:2975; rat.
DR RGD; 2975; Klrb1b.
DR PhylomeDB; Q5NKN2; -.
DR Proteomes; UP000002494; Unplaced.
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; IBA:GO_Central.
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 Disulfide bond; Lectin; Membrane; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..223
FT /note="Killer cell lectin-like receptor subfamily B member
FT 1B allele C"
FT /id="PRO_0000292986"
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 5..10
FT /note="ITIM motif"
FT MOTIF 31..34
FT /note="LCK-binding motif"
FT /evidence="ECO:0000250|UniProtKB:P27812"
FT DISULFID 122..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 189..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 223 AA; 24882 MW; F4C01C9FC6577DA2 CRC64;
MDTAVVYADL HLARTGEPKR ESPPSLSPDT CQCPRWHRLA LKLGCACFIL LVLSVIGLGV
LVLTLLQKPL LQNSPADVQE NRTKSTDSPA KLKCPKDWLS HRDKCFHVSQ TSNSWKESLA
DCDGKGATLL LIQDQEELRF VRNLTKGKDR SFWIGLSYTL PDRNWKWING STLNSDVLSI
TGDTEKGSCA SVSQDKVLSE SCDSDNIWIC QKELKRESTC NDS
