KLRA1_MOUSE
ID KLRA1_MOUSE Reviewed; 262 AA.
AC P20937;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=T-cell surface glycoprotein YE1/48;
DE AltName: Full=Lymphocyte antigen 49a;
DE Short=Ly-49a;
DE AltName: Full=T lymphocyte antigen A1;
GN Name=Klra1; Synonyms=Ly-49, Ly-49a, Ly49, Ly49A;
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=2783949;
RA Chan P.-Y., Takei F.;
RT "Molecular cloning and characterization of a novel murine T cell surface
RT antigen, YE1/48.";
RL J. Immunol. 142:1727-1736(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2787364;
RA Yokoyama W.M., Jacobs L., Kanagawa O., Shevach E.M., Cohen D.I.;
RT "A murine T lymphocyte antigen belongs to a supergene family of type II
RT integral membrane proteins.";
RL J. Immunol. 143:1379-1386(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 127-262 IN COMPLEX WITH
RP UNGLYCOSYLATED H-2D, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=10604468; DOI=10.1038/45170;
RA Tormo J., Natarajan K., Margulies D.H., Mariuzza R.A.;
RT "Crystal structure of a lectin-like natural killer cell receptor bound to
RT its MHC class I ligand.";
RL Nature 402:623-631(1999).
CC -!- FUNCTION: Receptor on natural killer (NK) cells for H-2d alleles.
CC Inhibits the activity of NK cells thus preventing cell lysis.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:10604468}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: High, in T-lymphoma lines, very low in normal
CC lymphocytes.
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DR EMBL; M25775; AAA40578.1; ALT_SEQ; mRNA.
DR EMBL; M25812; AAA37242.1; -; mRNA.
DR CCDS; CCDS20602.1; -.
DR PIR; A30573; A30573.
DR PIR; A45813; A45813.
DR PDB; 1QO3; X-ray; 2.30 A; C/D=126-262.
DR PDBsum; 1QO3; -.
DR AlphaFoldDB; P20937; -.
DR SMR; P20937; -.
DR STRING; 10090.ENSMUSP00000032288; -.
DR GlyGen; P20937; 3 sites.
DR MaxQB; P20937; -.
DR PaxDb; P20937; -.
DR PRIDE; P20937; -.
DR ProteomicsDB; 263556; -.
DR MGI; MGI:101907; Klra1.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P20937; -.
DR PhylomeDB; P20937; -.
DR ChiTaRS; Klra1; mouse.
DR EvolutionaryTrace; P20937; -.
DR PRO; PR:P20937; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P20937; protein.
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:0038023; F:signaling receptor activity; IDA:MGI.
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; Cell adhesion; Disulfide bond; Glycoprotein; Lectin;
KW Membrane; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..262
FT /note="T-cell surface glycoprotein YE1/48"
FT /id="PRO_0000046679"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 45..66
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..262
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 138..257
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 137..139
FT /note="Cell attachment site"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 145..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:10604468"
FT DISULFID 163..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:10604468"
FT DISULFID 167..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:10604468"
FT DISULFID 232..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:10604468"
FT CONFLICT 76..78
FT /note="NCE -> KLQ (in Ref. 2; AAA37242)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="I -> M (in Ref. 2; AAA37242)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="A -> T (in Ref. 2; AAA40578/AAA37242)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="G -> R (in Ref. 2; AAA37242)"
FT /evidence="ECO:0000305"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1QO3"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:1QO3"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:1QO3"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:1QO3"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:1QO3"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1QO3"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1QO3"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1QO3"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1QO3"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:1QO3"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:1QO3"
SQ SEQUENCE 262 AA; 30498 MW; 3C3328D265F71B5E CRC64;
MSEQEVTYSM VRFHKSAGLQ KQVRPEETKG PREAGYRRCS FHWKFIVIAL GIFCFLLLVA
VSVLAIKIFQ YDQQKNCEEF LNHHNNCSNM QSDINLKDEM LKNKSIECDL LESLNRDQNR
LYNKTKTVLD SLQHTGRGDK VYWFCYGMKC YYFVMDRKTW SGCKQACQSS SLSLLKIDDE
DELKFLQLVV PSDSCWVGLS YDNKKKDWAW IDNRPSKLAL NTGKYNIRDG GCMLLSKTRL
DNGNCDQVFI CICGKRLDKF PH
