KLRBA_MOUSE
ID KLRBA_MOUSE Reviewed; 227 AA.
AC P27811; Q1AG01; Q1WJB8; Q61972; Q61973; Q91V25; Q925G4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Killer cell lectin-like receptor subfamily B member 1A;
DE Short=NKR-P1A;
DE AltName: Full=CD161 antigen-like family member A;
DE AltName: Full=Lymphocyte antigen 55A;
DE Short=Ly-55A;
DE AltName: Full=NKR-P1.7;
DE AltName: Full=Natural killer cell surface protein P1-2;
DE Short=NKR-P1 2;
DE AltName: CD_antigen=CD161a;
GN Name=Klrb1a; Synonyms=Ly55, Ly55a, Nkrp1a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1880421;
RA Giorda R., Trucco M.;
RT "Mouse NKR-P1. A family of genes selectively coexpressed in adherent
RT lymphokine-activated killer cells.";
RL J. Immunol. 147:1701-1708(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1680927;
RA Yokoyama W.M., Ryan J.C., Hunter J.J., Smith H.R.C., Stark M., Seaman W.E.;
RT "cDNA cloning of mouse NKR-P1 and genetic linkage with LY-49.
RT Identification of a natural killer cell gene complex on mouse chromosome
RT 6.";
RL J. Immunol. 147:3229-3236(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=1517565;
RA Giorda R., Weisberg E.P., Ip T.K., Trucco M.;
RT "Genomic structure and strain-specific expression of the natural killer
RT cell receptor NKR-P1.";
RL J. Immunol. 149:1957-1963(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J, and SJL/J;
RX PubMed=10229823;
RA Kung S.K.P., Su R.-C., Shannon J., Miller R.G.;
RT "The NKR-P1B gene product is an inhibitory receptor on SJL/J NK cells.";
RL J. Immunol. 162:5876-5887(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=11685472; DOI=10.1007/s002510100367;
RA Plougastel B., Matsumoto K., Dubbelde C., Yokoyama W.M.;
RT "Analysis of a 1-Mb BAC contig overlapping the mouse Nkrp1 cluster of
RT genes: cloning of three new Nkrp1 members, Nkrp1d, Nkrp1e, and Nkrp1f.";
RL Immunogenetics 53:592-598(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=BALB/cByJ, and BALB/cJ; TISSUE=Spleen;
RX PubMed=16751398; DOI=10.4049/jimmunol.176.12.7511;
RA Carlyle J.R., Mesci A., Ljutic B., Belanger S., Tai L.-H., Rousselle E.,
RA Troke A.D., Proteau M.-F., Makrigiannis A.P.;
RT "Molecular and genetic basis for strain-dependent NK1.1 alloreactivity of
RT mouse NK cells.";
RL J. Immunol. 176:7511-7524(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 89-227, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=21600988; DOI=10.1016/j.jsb.2011.05.001;
RA Kolenko P., Rozbesky D., Vanek O., Kopecky V. Jr., Hofbauerova K.,
RA Novak P., Pompach P., Hasek J., Skalova T., Bezouska K., Dohnalek J.;
RT "Molecular architecture of mouse activating NKR-P1 receptors.";
RL J. Struct. Biol. 175:434-441(2011).
CC -!- FUNCTION: Plays a stimulatory role on natural killer (NK) cell
CC cytotoxicity. {ECO:0000269|PubMed:16751398}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with tyrosine kinase
CC LCK (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in natural killer cells.
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DR EMBL; M77676; AAA39822.1; -; mRNA.
DR EMBL; M77753; AAA39366.1; -; mRNA.
DR EMBL; X64716; CAA45971.1; -; Genomic_DNA.
DR EMBL; X64717; CAA45971.1; JOINED; Genomic_DNA.
DR EMBL; X64718; CAA45971.1; JOINED; Genomic_DNA.
DR EMBL; X64724; CAA45971.1; JOINED; Genomic_DNA.
DR EMBL; X64723; CAA45976.1; -; mRNA.
DR EMBL; AF354261; AAK39101.1; -; mRNA.
DR EMBL; AF354262; AAK39102.1; -; mRNA.
DR EMBL; AF285840; AAK83003.1; -; Genomic_DNA.
DR EMBL; AF285839; AAK83003.1; JOINED; Genomic_DNA.
DR EMBL; DQ143102; ABA43353.1; -; Genomic_DNA.
DR EMBL; DQ237927; ABB72025.1; -; mRNA.
DR EMBL; BC120707; AAI20708.1; -; mRNA.
DR PIR; A46467; A46467.
DR RefSeq; NP_001153374.1; NM_001159902.1.
DR RefSeq; NP_034867.3; NM_010737.3.
DR PDB; 2M94; NMR; -; A=89-227.
DR PDB; 3M9Z; X-ray; 1.70 A; A=89-227.
DR PDB; 3T3A; X-ray; 2.30 A; A/B=89-227.
DR PDBsum; 2M94; -.
DR PDBsum; 3M9Z; -.
DR PDBsum; 3T3A; -.
DR AlphaFoldDB; P27811; -.
DR BMRB; P27811; -.
DR SMR; P27811; -.
DR STRING; 10090.ENSMUSP00000032512; -.
DR PaxDb; P27811; -.
DR PRIDE; P27811; -.
DR ProteomicsDB; 265010; -.
DR DNASU; 17057; -.
DR GeneID; 17057; -.
DR KEGG; mmu:17057; -.
DR CTD; 17057; -.
DR MGI; MGI:107540; Klrb1a.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P27811; -.
DR OrthoDB; 1341815at2759; -.
DR PhylomeDB; P27811; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 17057; 3 hits in 70 CRISPR screens.
DR EvolutionaryTrace; P27811; -.
DR PRO; PR:P27811; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P27811; protein.
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; IDA:MGI.
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..227
FT /note="Killer cell lectin-like receptor subfamily B member
FT 1A"
FT /id="PRO_0000046675"
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..227
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 31..34
FT /note="LCK-binding motif"
FT /evidence="ECO:0000250"
FT DISULFID 94..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:21600988"
FT DISULFID 122..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:21600988"
FT DISULFID 189..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:21600988"
FT CONFLICT 39
FT /note="L -> S (in Ref. 1; AAA39822 and 3; CAA45971)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="I -> T (in Ref. 3; CAA45976)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="H -> Q (in Ref. 1; AAA39822, 2; AAA39366, 4;
FT AAK39102, 5; AAK83003 and 7; AAI20708)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="E -> K (in Ref. 4; AAK39101)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="I -> L (in Ref. 3; CAA45976)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="D -> G (in Ref. 1; AAA39822, 2; AAA39366, 4;
FT AAK39102, 5; AAK83003 and 7; AAI20708)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="E -> D (in Ref. 4; AAK39101)"
FT /evidence="ECO:0000305"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3M9Z"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:3M9Z"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:3M9Z"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:3M9Z"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3M9Z"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:3M9Z"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:2M94"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:2M94"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:3M9Z"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:3M9Z"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:3M9Z"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:3M9Z"
SQ SEQUENCE 227 AA; 25782 MW; B8283253E076C673 CRC64;
MDTARVYFGL KPPRTPGAWH ESPPSLPPDA CRCPRSHRLA LKLSCAGLIL LVVTLIGMSV
LVRVLIQKPS IEKCYVLIQE NLNKTTDCSA KLECPQDWLS HRDKCFHVSH VSNTWEEGLV
DCDGKGATLM LIQDQEELRF LLDSIKEKYN SFWIGLRYTL PDMNWKWING STLNSDVLKI
TDDTENDSCA AISGDKVTFE SCNSDNRWIC QKELYHETLS NYVGYGH
