KLRA7_MOUSE
ID KLRA7_MOUSE Reviewed; 280 AA.
AC Q60654; Q60655; Q60656; Q60683;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Killer cell lectin-like receptor 7;
DE AltName: Full=Lymphocyte antigen 49g;
DE Short=Ly-49g;
DE AltName: Full=T-cell surface glycoprotein Ly-49G;
GN Name=Klra7; Synonyms=Ly-49g, Ly49-g, Ly49g, Ly49g4;
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/6J; TISSUE=Spleen;
RX PubMed=8027540;
RA Smith H.R.C., Karlhofer F.M., Yokoyama W.M.;
RT "Ly-49 multigene family expressed by IL-2-activated NK cells.";
RL J. Immunol. 153:1068-1079(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LY-49G.2).
RC STRAIN=B10.A;
RX PubMed=7964501; DOI=10.1084/jem.180.6.2287;
RA Brennan J., Mager D., Jefferies W., Takei F.;
RT "Expression of different members of the Ly-49 gene family defines distinct
RT natural killer cell subsets and cell adhesion properties.";
RL J. Exp. Med. 180:2287-2295(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 156-280, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=18426793; DOI=10.1074/jbc.m801526200;
RA Deng L., Cho S., Malchiodi E.L., Kerzic M.C., Dam J., Mariuzza R.A.;
RT "Molecular architecture of the major histocompatibility complex class I-
RT binding site of Ly49 natural killer cell receptors.";
RL J. Biol. Chem. 283:16840-16849(2008).
CC -!- FUNCTION: Receptor on natural killer (NK) cells for class I MHC.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:18426793}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Ly-49G.1;
CC IsoId=Q60654-1; Sequence=Displayed;
CC Name=Ly-49G.2;
CC IsoId=Q60654-2; Sequence=VSP_003070;
CC Name=Ly-49G.3;
CC IsoId=Q60654-3; Sequence=VSP_003069;
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DR EMBL; U10093; AAA50221.1; -; mRNA.
DR EMBL; U10094; AAA50222.1; -; mRNA.
DR EMBL; U10095; AAA50223.1; -; mRNA.
DR EMBL; U12890; AAA58705.1; -; mRNA.
DR CCDS; CCDS39668.1; -. [Q60654-2]
DR CCDS; CCDS51928.1; -. [Q60654-1]
DR PIR; I49052; I49052.
DR PIR; I49053; I49053.
DR PIR; I49054; I49054.
DR RefSeq; NP_001103793.1; NM_001110323.1.
DR RefSeq; NP_055009.5; NM_014194.5. [Q60654-2]
DR PDB; 3CAD; X-ray; 2.60 A; A/B=156-280.
DR PDBsum; 3CAD; -.
DR AlphaFoldDB; Q60654; -.
DR SMR; Q60654; -.
DR STRING; 10090.ENSMUSP00000032286; -.
DR GlyGen; Q60654; 2 sites.
DR MaxQB; Q60654; -.
DR PaxDb; Q60654; -.
DR PRIDE; Q60654; -.
DR ProteomicsDB; 265007; -. [Q60654-1]
DR ProteomicsDB; 265008; -. [Q60654-2]
DR ProteomicsDB; 265009; -. [Q60654-3]
DR DNASU; 16638; -.
DR Ensembl; ENSMUST00000049304; ENSMUSP00000037917; ENSMUSG00000067599. [Q60654-2]
DR Ensembl; ENSMUST00000088011; ENSMUSP00000085326; ENSMUSG00000067599. [Q60654-2]
DR GeneID; 16638; -.
DR KEGG; mmu:16638; -.
DR UCSC; uc009ehx.2; mouse. [Q60654-2]
DR CTD; 16638; -.
DR MGI; MGI:101901; Klra7.
DR VEuPathDB; HostDB:ENSMUSG00000067599; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00390000008117; -.
DR InParanoid; Q60654; -.
DR OMA; NHEKHAL; -.
DR OrthoDB; 1180904at2759; -.
DR PhylomeDB; Q60654; -.
DR BioGRID-ORCS; 16638; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Klra7; mouse.
DR EvolutionaryTrace; Q60654; -.
DR PRO; PR:Q60654; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q60654; protein.
DR Bgee; ENSMUSG00000067599; Expressed in blood and 60 other tissues.
DR ExpressionAtlas; Q60654; baseline and differential.
DR Genevisible; Q60654; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF08391; Ly49; 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; Alternative splicing; Cell adhesion; Disulfide bond;
KW Glycoprotein; Lectin; Membrane; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..280
FT /note="Killer cell lectin-like receptor 7"
FT /id="PRO_0000046685"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..66
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 156..275
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 163..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:18426793"
FT DISULFID 181..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:18426793"
FT DISULFID 185..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:18426793"
FT DISULFID 250..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:18426793"
FT VAR_SEQ 117..193
FT /note="Missing (in isoform Ly-49G.3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003069"
FT VAR_SEQ 142..154
FT /note="Missing (in isoform Ly-49G.2)"
FT /evidence="ECO:0000303|PubMed:7964501"
FT /id="VSP_003070"
FT CONFLICT 44
FT /note="K -> Q (in Ref. 2; AAA58705)"
FT /evidence="ECO:0000305"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:3CAD"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:3CAD"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:3CAD"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:3CAD"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:3CAD"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:3CAD"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:3CAD"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:3CAD"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:3CAD"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:3CAD"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:3CAD"
SQ SEQUENCE 280 AA; 32522 MW; 4704A2D87D5E83FB CRC64;
MSEQEVTYST VRFHESSRLQ KLVRTEEPQR PREACYREYS VPWKLIVIAC GILCFLLLVT
VALLAITIFQ HSQQKHELQE TLNCHDNCSP TQSDVNLKDE LLRNKSIECR PGNDLLESLS
RDQNRWYSET KTFSDSSQHT GVHERPISKA EGKGRGFEKY WFCYGIKCYY FNMDRKTWSG
CKQTCQISSL SLLKIDNEDE LKFLQNLAPS DISWIGLSYD NKKKDWVWID NGPSKLALNT
TKYNIRDGLC MSLSKTRLDN GDCDKSYICI CGKRLDKFPH
