Linked Life Data

14765991

Source:http://linkedlifedata.com/resource/pubmed/id/14765991

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-2-9
pubmed:abstractText
Glucose-6-phosphatase (G6Pase) catalyzes the final step in the gluconeogenic and glycogenolytic pathways, the hydrolysis of glucose-6-phosphate (G6P) to glucose and phosphate. This paper describes the identification and characterization of a cDNA and the gene encoding the mouse ubiquitously expressed G6Pase catalytic subunit-related protein (UGRP). The open reading frame of this UGRP cDNA encodes a protein (346 amino acids (aa); Mr 38,755) that shares 36% overall identity (56% similarity) with the mouse G6Pase catalytic subunit (357 aa; Mr 40,454). UGRP exhibits a similar predicted transmembrane topology and conservation of many of the catalytically important residues with the G6Pase catalytic subunit; however, unlike the G6Pase catalytic subunit, UGRP does not catalyze G6P hydrolysis and does not contain a carboxy-terminal di-lysine endoplasmic reticulum retention signal. UGRP mRNA was detected by RNA blot analysis in every mouse tissue examined with the highest expression in heart, brain, testis and kidney. Database analysis showed that the mouse UGRP gene is composed of six exons, spans approximately 4.2 kbp of genomic DNA and is located on chromosome 11 along with the G6Pase catalytic subunit gene. The UGRP gene transcription start sites were mapped by primer extension analysis, and the activity of the mouse UGRP gene promoter was analyzed using luciferase fusion gene constructs. In contrast to the G6Pase catalytic subunit gene promoter, the UGRP promoter was highly active in all cell lines examined.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0952-5041
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33-53
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:14765991-Amino Acid Sequence, pubmed-meshheading:14765991-Animals, pubmed-meshheading:14765991-COS Cells, pubmed-meshheading:14765991-Catalytic Domain, pubmed-meshheading:14765991-Cells, Cultured, pubmed-meshheading:14765991-Cercopithecus aethiops, pubmed-meshheading:14765991-Chromosomes, pubmed-meshheading:14765991-Cloning, Molecular, pubmed-meshheading:14765991-DNA, Complementary, pubmed-meshheading:14765991-Glucose-6-Phosphatase, pubmed-meshheading:14765991-Glucose-6-Phosphate, pubmed-meshheading:14765991-HeLa Cells, pubmed-meshheading:14765991-Humans, pubmed-meshheading:14765991-Islets of Langerhans, pubmed-meshheading:14765991-Liver, pubmed-meshheading:14765991-Mice, pubmed-meshheading:14765991-Molecular Sequence Data, pubmed-meshheading:14765991-Muscles, pubmed-meshheading:14765991-Sequence Alignment, pubmed-meshheading:14765991-Tissue Distribution
pubmed:year
2004
pubmed:articleTitle
Identification and characterization of a cDNA and the gene encoding the mouse ubiquitously expressed glucose-6-phosphatase catalytic subunit-related protein.
pubmed:affiliation
Department of Molecular Physiology and Biophysics, 761 PRB, Vanderbilt University Medical School, Nashville, Tennessee 37232-0615, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't