Abstract
We have previously described the distribution of a surface glycoprotein recognized by monoclonal antibody B721. We now report the molecular characterization of this molecule at the protein, cDNA, and genomic level. A 75-kDa glycoprotein can be immunoprecipitated from B721+ tissues. We have isolated a near full-length cDNA containing the complete coding region and a full-length genomic clone. We present evidence that this protein has similarity to several classes of nuclear transcription factors, particularly the myc family of proteins. The 721P protein was found to have a leucine zipper-like structure, a possible basic region immediately upstream from the leucine zipper, and a protein kinase A phosphorylation site. 721P protein is encoded by a gene distinct from any deposited in existing data bases, and displays several features associated with proteins involved in signal transduction and gene regulation.
MeSH Terms
Amino Acid Sequence
Animals
Antibodies, Monoclonal
Antigens
Base Sequence
Cell Line
Chorionic Villi/physiology
Cloning, Molecular/methods
DNA/genetics,isolation & purification
Endothelium, Vascular/physiology
Female
Gene Library
Humans
Leucine Zippers/genetics
Membrane Glycoproteins/genetics
Molecular Sequence Data
Pregnancy
Protein Conformation
Proto-Oncogene Proteins c-myc/genetics
Sequence Homology, Amino Acid
Transcription Factors/genetics
Transfection
Umbilical Veins
Chemicals
Antibodies, Monoclonal
Antigens
Membrane Glycoproteins
Proto-Oncogene Proteins c-myc
Transcription Factors
AKAP17A protein, human
DNA
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Voland J R
Department of Biology and Cancer Center, University of California, San Diego, La Jolla 92093-0063.
Wyzykowski R J
Huang M
Dutton R W
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