Reviewed,
UniProtKB/Swiss-Prot Q148G2 (G6PC3_BOVIN)
Last modified
June 16, 2009.
Version 23.
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 3 Short name=G-6-Pase 3 Short name=G6Pase 3 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 | 346 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. May form with the glucose-6-phosphate transporter (SLC37A4/G6PT) a ubiquitously expressed complex responsible for glucose production through glycogenolysis and gluconeogenesis. Probably required for normal neutrophil function By similarity. |
| Catalytic activity | D-glucose 6-phosphate + H2O = D-glucose + phosphate. |
| Enzyme regulation | Inhibited by vanadate By similarity. |
| 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 |
| Molecular function | Hydrolase |
| 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 – 346 | 346 | Glucose-6-phosphatase 3 | PRO_0000334511 | |||||
Regions | |||||||||
| Topological domain | 1 – 24 | 24 | Lumenal Potential | ||||||
| Transmembrane | 25 – 45 | 21 | Potential | ||||||
| Topological domain | 46 – 54 | 9 | Cytoplasmic Potential | ||||||
| Transmembrane | 55 – 75 | 21 | Potential | ||||||
| Topological domain | 76 – 108 | 33 | Lumenal Potential | ||||||
| Transmembrane | 109 – 129 | 21 | Potential | ||||||
| Topological domain | 130 – 140 | 11 | Cytoplasmic Potential | ||||||
| Transmembrane | 141 – 162 | 22 | Potential | ||||||
| Topological domain | 163 – 167 | 5 | Lumenal Potential | ||||||
| Transmembrane | 168 – 186 | 19 | Potential | ||||||
| Topological domain | 187 – 197 | 11 | Cytoplasmic Potential | ||||||
| Transmembrane | 198 – 218 | 21 | Potential | ||||||
| Topological domain | 219 – 254 | 36 | Lumenal Potential | ||||||
| Transmembrane | 255 – 273 | 19 | Potential | ||||||
| Topological domain | 274 – 283 | 10 | Cytoplasmic Potential | ||||||
| Transmembrane | 284 – 304 | 21 | Potential | ||||||
| Topological domain | 305 – 307 | 3 | Lumenal Potential | ||||||
| Transmembrane | 308 – 328 | 21 | Potential | ||||||
| Topological domain | 329 – 346 | 18 | Cytoplasmic Potential | ||||||
Sites | |||||||||
| Active site | 114 | 1 | Proton donor Potential | ||||||
| Active site | 167 | 1 | Nucleophile By similarity | ||||||
| Binding site | 79 | 1 | Substrate Potential | ||||||
| Binding site | 161 | 1 | Substrate Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 239 | 1 | E → G in AAP40635. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Clottes E., Mounier R., Rossignol F., Bonnefont J., Guionie O., Burchell A. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal cerebellum. |
Cross-references
Sequence databases | |
|---|---|
| AY279358 mRNA. Translation: AAP40635.1. BC118357 mRNA. Translation: AAI18358.1. | |
| IPI | IPI00696280. |
| RefSeq | NP_899208.2. |
| UniGene | Bt.23154 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAG00000016253. Bos taurus. [Contig view] |
| GeneID | 369023. |
| KEGG | bta:369023. |
Phylogenomic databases | |
| HOVERGEN | Q148G2. |
| OMA | Q148G2. GIAVLWI. |
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... |
Entry information
| Entry name | G6PC3_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q148G2 Secondary accession number(s): Q7YSF2 | ||||||||
| 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


