KLRBA_RAT
ID KLRBA_RAT Reviewed; 223 AA.
AC P27471; A4KW96; A4KWA2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Killer cell lectin-like receptor subfamily B member 1A;
DE Short=NKR-P1A;
DE AltName: Full=Antigen 3.2.3;
DE AltName: Full=CD161 antigen-like family member A;
DE AltName: Full=Natural killer cell surface protein P1-3.2.3;
DE Short=NKR-P1 3.2.3;
DE AltName: CD_antigen=CD161a;
GN Name=Klrb1a; Synonyms=Nkrp1a;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2399464; DOI=10.1126/science.2399464;
RA Giorda R., Rudert W.A., Vavassori C., Chambers W.H., Hiserodt J.C.,
RA Trucco M.;
RT "NKR-P1, a signal transduction molecule on natural killer cells.";
RL Science 249:1298-1300(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344, Sprague-Dawley, and WAG; TISSUE=Spleen;
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 [3]
RP INTERACTION WITH LCK.
RX PubMed=9022000; DOI=10.1002/eji.1830270111;
RA Campbell K.S., Giorda R.;
RT "The cytoplasmic domain of rat NKR-P1 receptor interacts with the N-
RT terminal domain of p56(lck) via cysteine residues.";
RL Eur. J. Immunol. 27:72-77(1997).
RN [4]
RP FUNCTION.
RX PubMed=12618485; DOI=10.1093/intimm/dxg046;
RA Li J., Rabinovich B.A., Hurren R., Shannon J., Miller R.G.;
RT "Expression cloning and function of the rat NK activating and inhibitory
RT receptors NKR-P1A and -P1B.";
RL Int. Immunol. 15:411-416(2003).
CC -!- FUNCTION: Plays a stimulatory role on natural killer (NK) cell
CC cytotoxicity. {ECO:0000269|PubMed:12618485}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with tyrosine kinase
CC LCK. {ECO:0000269|PubMed:9022000}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in natural killer cells.
CC -!- MISCELLANEOUS: Ligand binding may be calcium dependent.
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DR EMBL; M62891; AAA41710.1; -; mRNA.
DR EMBL; EF100677; ABO15817.1; -; mRNA.
DR EMBL; EF100681; ABO15821.1; -; mRNA.
DR EMBL; EF100683; ABO15823.1; -; mRNA.
DR PIR; A35917; A35917.
DR RefSeq; NP_001010964.1; NM_001010964.1.
DR AlphaFoldDB; P27471; -.
DR SMR; P27471; -.
DR STRING; 10116.ENSRNOP00000009594; -.
DR BindingDB; P27471; -.
DR ChEMBL; CHEMBL3308948; -.
DR PaxDb; P27471; -.
DR GeneID; 362443; -.
DR KEGG; rno:362443; -.
DR UCSC; RGD:1586149; rat.
DR CTD; 17057; -.
DR RGD; 1586149; Klrb1a.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P27471; -.
DR OrthoDB; 1341815at2759; -.
DR TreeFam; TF337735; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR PRO; PR:P27471; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P27471; 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; ISO:RGD.
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 1A"
FT /id="PRO_0000046677"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..63
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 93..212
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 32..35
FT /note="LCK-binding motif"
FT DISULFID 94..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 122..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 189..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 66
FT /note="L -> F (in Ref. 2; ABO15823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 24551 MW; FCD12B212DDF4330 CRC64;
MDTARVYLSL KPSKTAAGAQ CVSPPSLPPD ACRCPRSHRL ALKLSCAGLI LLVLALVGMS
ILVRVLVQKP SVEPCRVLIQ ENLSKTGSPA KLKCPKDWLS HRDKCFHVSQ TSITWKESLA
DCGGKGATLL LVQDQEELRF LRNLTKRISS SFWIGLSYTL SDENWKWING STLNSDVLSI
TGDTEKDSCA SVSQDKVLSE SCDSDNIWVC QKELKCECMC NDS
