Reviewed,
UniProtKB/Swiss-Prot P43428 (G6PC_RAT)
Last modified
June 16, 2009.
Version 65.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glucose-6-phosphatase Short name=G-6-Pase Short name=G6Pase EC=3.1.3.9 | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 357 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production through glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels By similarity. |
| Catalytic activity | D-glucose 6-phosphate + H2O = D-glucose + phosphate. |
| Pathway | |
| Subcellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein. |
| Sequence similarities | Belongs to the glucose-6-phosphatase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Gluconeogenesis |
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Transmembrane |
| Molecular function | Hydrolase |
| PTM | Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | gluconeogenesis Ref.3 Inferred from direct assay. Source: RGD glucose 6-phosphate metabolic processInferred from direct assay. Source: RGD phosphorylated carbohydrate dephosphorylationInferred from direct assay. Source: RGD response to foodInferred from expression pattern. Source: RGD |
| Cellular component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW microsomeInferred from direct assay. Source: RGD |
| Molecular function | glucose-6-phosphatase activity Ref.3 Inferred from direct assay. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 357 | 357 | Glucose-6-phosphatase | PRO_0000087415 | |||||
Regions | |||||||||
| Topological domain | 1 – 28 | 28 | Lumenal Potential | ||||||
| Transmembrane | 29 – 49 | 21 | Potential | ||||||
| Topological domain | 50 – 60 | 11 | Cytoplasmic Potential | ||||||
| Transmembrane | 61 – 81 | 21 | Potential | ||||||
| Topological domain | 82 – 117 | 36 | Lumenal Potential | ||||||
| Transmembrane | 118 – 138 | 21 | Potential | ||||||
| Topological domain | 139 – 147 | 9 | Cytoplasmic Potential | ||||||
| Transmembrane | 148 – 168 | 21 | Potential | ||||||
| Topological domain | 169 – 170 | 2 | Lumenal Potential | ||||||
| Transmembrane | 171 – 191 | 21 | Potential | ||||||
| Topological domain | 192 – 211 | 20 | Cytoplasmic Potential | ||||||
| Transmembrane | 212 – 232 | 21 | Potential | ||||||
| Topological domain | 233 – 254 | 22 | Lumenal Potential | ||||||
| Transmembrane | 255 – 275 | 21 | Potential | ||||||
| Topological domain | 276 – 291 | 16 | Cytoplasmic Potential | ||||||
| Transmembrane | 292 – 312 | 21 | Potential | ||||||
| Topological domain | 313 – 320 | 8 | Lumenal Potential | ||||||
| Transmembrane | 321 – 341 | 21 | Potential | ||||||
| Topological domain | 342 – 357 | 16 | Cytoplasmic Potential | ||||||
| Motif | 354 – 357 | 4 | Prevents secretion from ER Potential | ||||||
Sites | |||||||||
| Active site | 119 | 1 | Proton donor Potential | ||||||
| Active site | 176 | 1 | Nucleophile By similarity | ||||||
| Binding site | 83 | 1 | Substrate Potential | ||||||
| Binding site | 170 | 1 | Substrate Potential | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 96 | 1 | N-linked (GlcNAc...) By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 118 | 1 | G → V in AAA19966. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "High levels of glucose-6-phosphatase gene and protein expression reflect an adaptive response in proliferating liver and diabetes." Haber B.A., Chin S., Chuang E., Buikuisen W., Naji A., Taub R.A. J. Clin. Invest. 95:832-841(1995) [PubMed: 7860767] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "Isolation of a cDNA for the catalytic subunit of rat liver glucose-6-phosphatase: regulation of gene expression in FAO hepatoma cells by insulin, dexamethasone and cAMP." Lange A.J., Argaud D.M., El-Maghrabi M.R., Pan W., Subir M., Pilkis S.J. Biochem. Biophys. Res. Commun. 201:302-309(1994) [PubMed: 8198588] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. |
| [3] | "Expression and distribution of glucose-6-phosphatase catalytic subunit messenger RNA and its changes in the diabetic state." Shingu R., Nakajima H., Horikawa Y., Hamaguchi T., Yamasaki T., Miyagawa J., Namba M., Hanafusa T., Matsuzawa Y. Res. Commun. Mol. Pathol. Pharmacol. 93:13-24(1996) [PubMed: 8865366] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| L37333 mRNA. Translation: AAA74381.1. Different initiation. U07993 mRNA. Translation: AAA19966.1. D78592 mRNA. Translation: BAA24348.1. BC090067 mRNA. Translation: AAH90067.2. Different initiation. | |
| IPI | IPI00200360. |
| PIR | JC2371. |
| RefSeq | NP_037230.2. |
| UniGene | Rn.10992 |
3D structure databases | |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P43428. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000036805. Rattus norvegicus. [Contig view] |
| GeneID | 25634. |
| KEGG | rno:25634. |
Organism-specific databases | |
| RGD | 2644. G6pc. |
Phylogenomic databases | |
| HOVERGEN | P43428. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.9. 248. |
Gene expression databases | |
| ArrayExpress | P43428. |
| GermOnline | ENSRNOG00000036805. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR016275. Glucose-6-phosphatase. IPR000326. P_Acid_Pase_2/haloperoxidase. [Graphical view] |
| Pfam | PF01569. PAP2. 1 hit. [Graphical view] |
| PIRSF | PIRSF000905. Glucose-6-phosphatase. 1 hit. |
| SMART | SM00014. acidPPc. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 607447. |
Entry information
| Entry name | G6PC_RAT | ||||||||
| Accession | Primary (citable) accession number: P43428 Secondary accession number(s): Q5FVC9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


