Cloning and preliminary characterization of a 121 kDa protein with multiple predicted C2 domains.
In the course of characterizing proteins present in a preparation of vesicles from rat adipocytes containing glucose transporters, we examined a protein that migrated at 115 kDa upon SDS gel electrophoresis (designated vp115). Sequences of tryptic peptides were obtained, and from this information the cDNA for rat vp115 was cloned. The cDNA encodes an open reading frame for a protein of 121 kDa. Computer-aided sequence analysis predicted that vp115 has a potential membrane-inserted or membrane-spanning domain toward its amino terminus, followed by five C2 domains. Immunoblotting revealed that vp115 was not actually a component of the glucose transporter-containing vesicles, was most abundant in the plasma membranes and high density microsome fractions of rat adipocytes, and was expressed in all the major rat tissues.
Morris
N J
NJ
Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
Ross
S A
SA
Neveu
J M
JM
Lane
W S
WS
Lienhard
G E
GE
D017667:Adipocytes / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D015151:Immunoblotting; D008565:Membrane Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D051381:Rats; D017385:Sequence Homology; D013347:Subcellular Fractions / Q000378:metabolism
C119896:Esyt1 protein, rat; D008565:Membrane Proteins