Q29RU6 (G6PC_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 42.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 357 AA. |
| Sequence status | Complete. |
| 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 By similarity. |
| Sequence similarities | Belongs to the glucose-6-phosphatase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Gluconeogenesis |
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Transmembrane Transmembrane helix |
| Molecular function | Hydrolase |
| PTM | Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | glucose-6-phosphatase activity Inferred from electronic annotation. Source: EC |
| 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_0000350564 | |||||
Regions | |||||||||
| Topological domain | 1 – 28 | 28 | Lumenal Potential | ||||||
| Transmembrane | 29 – 49 | 21 | Helical; Potential | ||||||
| Topological domain | 50 – 60 | 11 | Cytoplasmic Potential | ||||||
| Transmembrane | 61 – 81 | 21 | Helical; Potential | ||||||
| Topological domain | 82 – 117 | 36 | Lumenal Potential | ||||||
| Transmembrane | 118 – 138 | 21 | Helical; Potential | ||||||
| Topological domain | 139 – 147 | 9 | Cytoplasmic Potential | ||||||
| Transmembrane | 148 – 168 | 21 | Helical; Potential | ||||||
| Topological domain | 169 – 170 | 2 | Lumenal Potential | ||||||
| Transmembrane | 171 – 191 | 21 | Helical; Potential | ||||||
| Topological domain | 192 – 209 | 18 | Cytoplasmic Potential | ||||||
| Transmembrane | 210 – 230 | 21 | Helical; Potential | ||||||
| Topological domain | 231 – 254 | 24 | Lumenal Potential | ||||||
| Transmembrane | 255 – 275 | 21 | Helical; Potential | ||||||
| Topological domain | 276 – 291 | 16 | Cytoplasmic Potential | ||||||
| Transmembrane | 292 – 312 | 21 | Helical; Potential | ||||||
| Topological domain | 313 – 320 | 8 | Lumenal Potential | ||||||
| Transmembrane | 321 – 341 | 21 | Helical; 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...) Potential | ||||||
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Testis. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC114011 mRNA. Translation: AAI14012.1. |
| IPI | IPI00696584. |
| RefSeq | NP_001069592.1. NM_001076124.1. |
| UniGene | Bt.17113. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q29RU6. |
Proteomic databases | |
| PRIDE | Q29RU6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000013436; ENSBTAP00000013436; ENSBTAG00000010184. |
| GeneID | 538710. |
| KEGG | bta:538710. |
Organism-specific databases | |
| CTD | 2538. |
Phylogenomic databases | |
| eggNOG | maNOG13087. |
| GeneTree | ENSGT00510000046465. |
| HOVERGEN | HBG003560. |
| InParanoid | Q29RU6. |
| OMA | YLQVNYQ. |
| OrthoDB | EOG4ZCT4R. |
Family and domain databases | |
| InterPro | IPR016275. Glucose-6-phosphatase. IPR016118. P_Acid_Pase/Cl_peroxidase_N. IPR000326. P_Acid_Pase_2/haloperoxidase. [Graphical view] |
| Gene3D | G3DSA:1.20.144.10. P_Acid_Pase/Cl_peroxidase_N. 1 hit. |
| KO | K01084. |
| Pfam | PF01569. PAP2. 1 hit. [Graphical view] |
| PIRSF | PIRSF000905. Glucose-6-phosphatase. 1 hit. |
| SMART | SM00014. acidPPc. 1 hit. [Graphical view] |
| SUPFAM | SSF48317. AcPase_VanPerase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | G6PC_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q29RU6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with