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
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Antigens, CD*
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Antigens, CD20
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Antigens, Differentiation / genetics*
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Antigens, Differentiation, B-Lymphocyte
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Antigens, Differentiation, T-Lymphocyte / genetics
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Antigens, Neoplasm*
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Base Sequence
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DNA / genetics
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Glycoproteins / genetics*
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Glycoproteins / ultrastructure*
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Molecular Sequence Data
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RNA, Messenger / genetics
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Solubility
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Tetraspanin 25
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Tetraspanins
Substances
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Antigens, CD
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Antigens, CD20
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Antigens, Differentiation
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Antigens, Differentiation, B-Lymphocyte
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Antigens, Differentiation, T-Lymphocyte
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Antigens, Neoplasm
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CD37 protein, human
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CD53 protein, human
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Cd53 protein, rat
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Glycoproteins
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RNA, Messenger
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Tetraspanin 25
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Tetraspanins
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DNA
Associated data
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GENBANK/X14046
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GENBANK/X53517