Primary structure of lymphocyte function-associated antigen 3 (LFA-3). The ligand of the T lymphocyte CD2 glycoprotein.
We have isolated the cDNA for human lymphocyte function-associated antigen 3 (LFA-3), the ligand of the T lymphocyte CD2 molecule. The identity of the clones was established by comparison of the deduced amino acid sequence to the LFA-3 NH2-terminal and tryptic peptide sequences. The cDNA defines a mature protein of 222 amino acids that structurally resembles typical membrane-anchored proteins. An extracellular domain with six N-linked glycosylation sites is followed by a hydrophobic putative transmembrane region and a short cytoplasmic domain. The mature glycoprotein is estimated to be 44-68% carbohydrate. Southern blots of human genomic DNA indicate that only one gene codes for human LFA-3. Northern blot analysis demonstrates that the LFA-3 mRNA of 1.3 kb is widely distributed in human tissues and cell lines.
Wallner
B P
BP
Biogen Research Corporation, Cambridge, Massachusetts 02142.
Frey
A Z
AZ
Tizard
R
R
Mattaliano
R J
RJ
Hession
C
C
Sanders
M E
ME
Dustin
M L
ML
Springer
T A
TA
D000595:Amino Acid Sequence; D000945:Antigens, Differentiation, T-Lymphocyte / Q000378:metabolism*; D000954:Antigens, Surface / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis; D006801:Humans; D016169:Lymphocyte Function-Associated Antigen-1; D008969:Molecular Sequence Data; D010449:Peptide Mapping
D000945:Antigens, Differentiation, T-Lymphocyte; D000954:Antigens, Surface; D016169:Lymphocyte Function-Associated Antigen-1; D004247:DNA