Cloning and sequence analysis of the beta subunit of the human translocon-associated protein.
A cDNA corresponding to the beta subunit of the human translocon-associated protein was cloned and sequenced. The polypeptide is 183 amino acids long and 96% homologous to its canine counterpart. Both polypeptides contain a cleavable signal sequence, an NH2-terminal domain extruding in the endoplasmic reticulum lumen, a transmembrane domain and a COOH-terminal domain located in the cytoplasm.
Bodescot
M
M
Laboratoire d'Oncologie Moléculaire, CNRS URA 1158, Institut Gustave Roussy, Villejuif, France.
Brison
O
O
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002135:Calcium-Binding Proteins; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry; D004285:Dogs; D004721:Endoplasmic Reticulum / Q000737:chemistry; D006801:Humans; D008562:Membrane Glycoproteins; D008969:Molecular Sequence Data; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry / Q000235:genetics*; D018000:Receptors, Peptide / Q000737:chemistry / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
D002135:Calcium-Binding Proteins; D018076:DNA, Complementary; D008562:Membrane Glycoproteins; D018160:Receptors, Cytoplasmic and Nuclear; D018000:Receptors, Peptide; C066973:signal sequence receptor