The primary structure of the human leukocyte antigen CD37, a species homologue of the rat MRC OX-44 antigen

J Exp Med. 1989 Apr 1;169(4):1497-502. doi: 10.1084/jem.169.4.1497.

Abstract

Comparison of NH2-terminal protein sequence from the rat OX-44 antigen with the sequence of the human CD37 antigen deduced from a cDNA clone shows that these antigens are species homologues. The CD37 sequence is 244 amino acids in length and lacks a conventional leader sequence. The molecule is likely to have an NH2-terminal cytoplasmic domain followed by three transmembrane sequences that lie within the first 110 amino acids. The rest of the molecule is hydrophillic and contains three sites for N-linked glycosylation.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antigens, CD*
  • Antigens, CD20
  • Antigens, Differentiation / genetics*
  • Antigens, Differentiation, B-Lymphocyte
  • Antigens, Differentiation, T-Lymphocyte / genetics
  • Antigens, Neoplasm*
  • Base Sequence
  • DNA / genetics
  • Glycoproteins / genetics*
  • Glycoproteins / ultrastructure*
  • Molecular Sequence Data
  • RNA, Messenger / genetics
  • Solubility
  • Tetraspanin 25
  • Tetraspanins

Substances

  • Antigens, CD
  • Antigens, CD20
  • Antigens, Differentiation
  • Antigens, Differentiation, B-Lymphocyte
  • Antigens, Differentiation, T-Lymphocyte
  • Antigens, Neoplasm
  • CD37 protein, human
  • CD53 protein, human
  • Cd53 protein, rat
  • Glycoproteins
  • RNA, Messenger
  • Tetraspanin 25
  • Tetraspanins
  • DNA

Associated data

  • GENBANK/X14046
  • GENBANK/X53517