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T-cell surface glycoprotein YE1/48 (Lymphocyte antigen 49a) (Ly-49a) (T lymphocyte antigen A1)

 KLRA1_MOUSE             Reviewed;         262 AA.
P20937;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
18-JUL-2018, entry version 134.
RecName: Full=T-cell surface glycoprotein YE1/48;
AltName: Full=Lymphocyte antigen 49a;
Short=Ly-49a;
AltName: Full=T lymphocyte antigen A1;
Name=Klra1; Synonyms=Ly-49, Ly-49a, Ly49, Ly49A;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2783949;
Chan P.-Y., Takei F.;
"Molecular cloning and characterization of a novel murine T cell
surface antigen, YE1/48.";
J. Immunol. 142:1727-1736(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2787364;
Yokoyama W.M., Jacobs L., Kanagawa O., Shevach E.M., Cohen D.I.;
"A murine T lymphocyte antigen belongs to a supergene family of type
II integral membrane proteins.";
J. Immunol. 143:1379-1386(1989).
[3]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 127-262 IN COMPLEX WITH
UNGLYCOSYLATED H-2D, SUBUNIT, AND DISULFIDE BONDS.
PubMed=10604468; DOI=10.1038/45170;
Tormo J., Natarajan K., Margulies D.H., Mariuzza R.A.;
"Crystal structure of a lectin-like natural killer cell receptor bound
to its MHC class I ligand.";
Nature 402:623-631(1999).
-!- FUNCTION: Receptor on natural killer (NK) cells for H-2d alleles.
Inhibits the activity of NK cells thus preventing cell lysis.
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000269|PubMed:10604468}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
protein.
-!- TISSUE SPECIFICITY: High, in T-lymphoma lines, very low in normal
lymphocytes.
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EMBL; M25775; AAA40578.1; ALT_SEQ; mRNA.
EMBL; M25812; AAA37242.1; -; mRNA.
CCDS; CCDS20602.1; -.
PIR; A30573; A30573.
PIR; A45813; A45813.
UniGene; Mm.24399; -.
UniGene; Mm.333431; -.
PDB; 1QO3; X-ray; 2.30 A; C/D=126-262.
PDBsum; 1QO3; -.
ProteinModelPortal; P20937; -.
SMR; P20937; -.
STRING; 10090.ENSMUSP00000032288; -.
MaxQB; P20937; -.
PaxDb; P20937; -.
PRIDE; P20937; -.
MGI; MGI:101907; Klra1.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
HOGENOM; HOG000113237; -.
HOVERGEN; HBG053176; -.
InParanoid; P20937; -.
PhylomeDB; P20937; -.
EvolutionaryTrace; P20937; -.
PRO; PR:P20937; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:MGI.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
CDD; cd03593; CLECT_NK_receptors_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR013600; Ly49_N.
InterPro; IPR033992; NKR-like_CTLD.
Pfam; PF00059; Lectin_C; 1.
Pfam; PF08391; Ly49; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Complete proteome; Disulfide bond;
Glycoprotein; Lectin; Membrane; Receptor; Reference proteome;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 262 T-cell surface glycoprotein YE1/48.
/FTId=PRO_0000046679.
TOPO_DOM 1 44 Cytoplasmic. {ECO:0000305}.
TRANSMEM 45 66 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 67 262 Extracellular. {ECO:0000305}.
DOMAIN 138 257 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
MOTIF 137 139 Cell attachment site.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 145 150 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:10604468}.
DISULFID 163 251 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:10604468}.
DISULFID 167 253 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:10604468}.
DISULFID 232 245 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:10604468}.
CONFLICT 76 78 NCE -> KLQ (in Ref. 2; AAA37242).
{ECO:0000305}.
CONFLICT 106 106 I -> M (in Ref. 2; AAA37242).
{ECO:0000305}.
CONFLICT 166 166 A -> T (in Ref. 2; AAA40578/AAA37242).
{ECO:0000305}.
CONFLICT 223 223 G -> R (in Ref. 2; AAA37242).
{ECO:0000305}.
STRAND 141 146 {ECO:0000244|PDB:1QO3}.
STRAND 149 158 {ECO:0000244|PDB:1QO3}.
HELIX 160 169 {ECO:0000244|PDB:1QO3}.
HELIX 180 189 {ECO:0000244|PDB:1QO3}.
STRAND 195 202 {ECO:0000244|PDB:1QO3}.
HELIX 203 205 {ECO:0000244|PDB:1QO3}.
STRAND 207 210 {ECO:0000244|PDB:1QO3}.
HELIX 227 229 {ECO:0000244|PDB:1QO3}.
STRAND 231 235 {ECO:0000244|PDB:1QO3}.
STRAND 240 243 {ECO:0000244|PDB:1QO3}.
STRAND 249 256 {ECO:0000244|PDB:1QO3}.
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


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