KRBBA_RAT
ID KRBBA_RAT Reviewed; 223 AA.
AC A4KWA1; Q62983;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Killer cell lectin-like receptor subfamily B member 1B allele A;
DE AltName: Full=CD161 antigen-like family member B;
DE AltName: Full=Natural killer cell surface protein NKR-P1B allele RNK/SD/BN/F344;
DE AltName: CD_antigen=CD161b;
GN Name=Klrb1b {ECO:0000312|RGD:2975};
GN Synonyms=Nkrp1b {ECO:0000312|EMBL:AAB01986.1};
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:ABO15822.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND POLYMORPHISM.
RC STRAIN=Fischer 344 {ECO:0000312|EMBL:ABO15822.1}, and
RC Sprague-Dawley {ECO:0000312|EMBL:ABO15824.1}; TISSUE=Natural killer cell;
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:0000305, ECO:0000312|EMBL:AAB01986.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344 {ECO:0000312|EMBL:AAB01986.1};
RC TISSUE=Natural killer cell;
RA Ryan J.C., Dissen E., Seaman W.E., Fossum S.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3] {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).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF100682; ABO15822.1; -; mRNA.
DR EMBL; EF100684; ABO15824.1; -; mRNA.
DR EMBL; U56936; AAB01986.1; -; mRNA.
DR RefSeq; NP_775414.2; NM_173292.2.
DR PDB; 5J2S; X-ray; 2.00 A; A/B=78-223.
DR PDBsum; 5J2S; -.
DR AlphaFoldDB; A4KWA1; -.
DR SMR; A4KWA1; -.
DR STRING; 10116.ENSRNOP00000009904; -.
DR PaxDb; A4KWA1; -.
DR PRIDE; A4KWA1; -.
DR Ensembl; ENSRNOT00000111200; ENSRNOP00000095158; ENSRNOG00000007310.
DR GeneID; 25192; -.
DR KEGG; rno:25192; -.
DR CTD; 80782; -.
DR RGD; 2975; Klrb1b.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154685; -.
DR HOGENOM; CLU_049894_8_2_1; -.
DR InParanoid; A4KWA1; -.
DR OrthoDB; 1341815at2759; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007310; Expressed in spleen and 16 other tissues.
DR ExpressionAtlas; A4KWA1; baseline and differential.
DR Genevisible; A4KWA1; RN.
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 3D-structure; Disulfide bond; Lectin; Membrane; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..223
FT /note="Killer cell lectin-like receptor subfamily B member
FT 1B allele A"
FT /id="PRO_0000292984"
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"
FT CONFLICT 87..88
FT /note="DS -> EV (in Ref. 1; AAB01986)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="H -> L (in Ref. 1; AAB01986)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="S -> I (in Ref. 1; AAB01986)"
FT /evidence="ECO:0000305"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5J2S"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:5J2S"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:5J2S"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:5J2S"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:5J2S"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:5J2S"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:5J2S"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:5J2S"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:5J2S"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:5J2S"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5J2S"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:5J2S"
SQ SEQUENCE 223 AA; 24772 MW; 87CF74BBEA40BE52 CRC64;
MDTAVVYADL HLARTGEPKR EPPPSLSPDT CQCPRWHRLA LKLGCACLIL LVLSVIGLGV
LVLTLLQKPL IQNSPADVQE NRTKTTDSPA KLKCPKDWHS HQDKCFHVSQ TSITWKGSLA
DCGGKGATLL LVQDQEELRF LRNLTKRISS SFWIGLSYTL SDEKWKWING STLNSDALNI
TGDTEKDSCA SVSQDKVLSE SCDSDNIWIC QKELKRESTC NDS
