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Q29RU6 (G6PC_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-6-phosphatase

Short name=G-6-Pase
Short name=G6Pase
EC=3.1.3.9
Gene names
Name:G6PC
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Carbohydrate biosynthesis; gluconeogenesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the glucose-6-phosphatase family.

Ontologies

Keywords
   Biological processGluconeogenesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglucose-6-phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 357357Glucose-6-phosphatase
PRO_0000350564

Regions

Topological domain1 – 2828Lumenal Potential
Transmembrane29 – 4921Helical; Potential
Topological domain50 – 6011Cytoplasmic Potential
Transmembrane61 – 8121Helical; Potential
Topological domain82 – 11736Lumenal Potential
Transmembrane118 – 13821Helical; Potential
Topological domain139 – 1479Cytoplasmic Potential
Transmembrane148 – 16821Helical; Potential
Topological domain169 – 1702Lumenal Potential
Transmembrane171 – 19121Helical; Potential
Topological domain192 – 20918Cytoplasmic Potential
Transmembrane210 – 23021Helical; Potential
Topological domain231 – 25424Lumenal Potential
Transmembrane255 – 27521Helical; Potential
Topological domain276 – 29116Cytoplasmic Potential
Transmembrane292 – 31221Helical; Potential
Topological domain313 – 3208Lumenal Potential
Transmembrane321 – 34121Helical; Potential
Topological domain342 – 35716Cytoplasmic Potential
Motif354 – 3574Prevents secretion from ER Potential

Sites

Active site1191Proton donor Potential
Active site1761Nucleophile By similarity
Binding site831Substrate Potential
Binding site1701Substrate Potential

Amino acid modifications

Glycosylation961N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q29RU6 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: B932F00C8940EFEE

FASTA35740,827
        10         20         30         40         50         60 
MEKGMNVLHD FGIQSTHYLQ VNYQNSQDWF ILVSVIADLR NAFYVLFPIW FHLREAVGIK 

        70         80         90        100        110        120 
LLWVAVIGDW LNLVFKWILF GQRPYWWVLD TDYYSNTSAP LIKQFPVTCE TGPGSPSGHA 

       130        140        150        160        170        180 
MGTAGVYYVM VTSTLSIFRG KKKPTYRFRC LNVMLWLGFW VVQLNVCLSR IYLAAHFPHQ 

       190        200        210        220        230        240 
VVAGVLSGIA VAETFRHIQS IYNASLKKYF LITCFLFSFA IGFYLLLKWL GVDLLWTLEK 

       250        260        270        280        290        300 
AKRRCERPEW VHIDTTPFAS LLKNLGTLFG LGLALNSSMY RESCKGKLSK WFPFRLSCIV 

       310        320        330        340        350 
ASLVLLHLFD SLKPPSQIEL IFYVLSFCKS AAVPLASVSL IPYCLAWVLG QPNKKTV 

« Hide

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.
IPIIPI00696584.
RefSeqNP_001069592.1. NM_001076124.1.
UniGeneBt.17113.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ29RU6.

Proteomic databases

PRIDEQ29RU6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000013436; ENSBTAP00000013436; ENSBTAG00000010184.
GeneID538710.
KEGGbta:538710.

Organism-specific databases

CTD2538.

Phylogenomic databases

eggNOGmaNOG13087.
GeneTreeENSGT00510000046465.
HOVERGENHBG003560.
InParanoidQ29RU6.
OMAYLQVNYQ.
OrthoDBEOG4ZCT4R.

Family and domain databases

InterProIPR016275. Glucose-6-phosphatase.
IPR016118. P_Acid_Pase/Cl_peroxidase_N.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
Gene3DG3DSA:1.20.144.10. P_Acid_Pase/Cl_peroxidase_N. 1 hit.
KOK01084.
PfamPF01569. PAP2. 1 hit.
[Graphical view]
PIRSFPIRSF000905. Glucose-6-phosphatase. 1 hit.
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMSSF48317. AcPase_VanPerase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameG6PC_BOVIN
AccessionPrimary (citable) accession number: Q29RU6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: April 4, 2006
Last modified: November 16, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families