ID   KLRA2_MOUSE             Reviewed;         288 AA.
AC   Q60660;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 125.
DE   RecName: Full=Killer cell lectin-like receptor 2;
DE   AltName: Full=Lymphocyte antigen 49b;
DE            Short=Ly-49b;
DE   AltName: Full=T-cell surface glycoprotein Ly-49B;
GN   Name=Klra2; Synonyms=Ly49-b, Ly49b;
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].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX   PubMed=1869832;
RA   Wong S., Freeman J.D., Kelleher C., Mager D., Takei F.;
RT   "Ly-49 multigene family. New members of a superfamily of type II membrane
RT   proteins with lectin-like domains.";
RL   J. Immunol. 147:1417-1423(1991).
CC   -!- FUNCTION: Receptor on natural killer (NK) cells for class I MHC.
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
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DR   EMBL; U10304; AAA19052.1; -; mRNA.
DR   CCDS; CCDS20603.1; -.
DR   PIR; I49058; I49058.
DR   AlphaFoldDB; Q60660; -.
DR   SMR; Q60660; -.
DR   STRING; 10090.ENSMUSP00000086252; -.
DR   GlyCosmos; Q60660; 4 sites, No reported glycans.
DR   GlyGen; Q60660; 4 sites.
DR   iPTMnet; Q60660; -.
DR   PhosphoSitePlus; Q60660; -.
DR   MaxQB; Q60660; -.
DR   ProteomicsDB; 263634; -.
DR   AGR; MGI:101906; -.
DR   MGI; MGI:101906; Klra2.
DR   InParanoid; Q60660; -.
DR   PhylomeDB; Q60660; -.
DR   PRO; PR:Q60660; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q60660; Protein.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd03593; CLECT_NK_receptors_like; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR013600; Ly49_N.
DR   InterPro; IPR033992; NKR-like_CTLD.
DR   PANTHER; PTHR46329; KILLER CELL LECTIN-LIKE RECEPTOR 2; 1.
DR   PANTHER; PTHR46329:SF1; KILLER CELL LECTIN-LIKE RECEPTOR 2; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF08391; Ly49; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Lectin; Membrane; Receptor;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..288
FT                   /note="Killer cell lectin-like receptor 2"
FT                   /id="PRO_0000046680"
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..288
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          144..263
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        151..156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        169..257
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        173..259
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        238..251
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   288 AA;  33607 MW;  B3A410A32DF8E82F CRC64;
     MSEQEVTYTT LRFHKSSGLQ NPVRPEETQR PRDVGHRECS VPWKFIVIVL GILCFLLLLT
     VAVLVIHIFR DGQEKHEQEK TLNNLRQEYQ VMKNDSSLME EMLRNKSSEC KALNDSLHYL
     NREQNRCLRK TKIVLDCSQN KGKQVEGYWF CCGMKCYYFI MDDKKWNGCK QICQDYNLTL
     LKTNDEDELK FLKSQLQRNT YWISLTHHKS KEESQQIGDR PSKLDSAARN SVPNRQKCAY
     LSSFSTEEDD CARTHGCICE KRLNKFPIPG SCAKGRTQSA LQRDEDES
//