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P43428 (G6PC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 101. 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
Synonyms:G6pt
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

Sequence similarities

Belongs to the glucose-6-phosphatase family.

Sequence caution

The sequence AAA74381.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH90067.2 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 357357Glucose-6-phosphatase
PRO_0000087415

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 – 21120Cytoplasmic Potential
Transmembrane212 – 23221Helical; Potential
Topological domain233 – 25422Lumenal 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...) By similarity

Experimental info

Sequence conflict1181G → V in AAA19966. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P43428 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: C44960E102F4244D

FASTA35740,556
        10         20         30         40         50         60 
MEERMNVLHD FGIQSTRYLQ VNYEDSQDWF VLVSVIADLR NAFYVLFPIW FHIQETVGIN 

        70         80         90        100        110        120 
LLWVAVVGDW FNLVFKWILF GQRPYWWVLD TDYYSNSSVP LIKQFPVTCE TGPGSPSGHA 

       130        140        150        160        170        180 
MGTAGVYYVM VTSTLAIFRG KKKSTYGFRC LNVVLWLGYW AVQLNVCLSR IYLAAHFPHQ 

       190        200        210        220        230        240 
VVAGVLSGIA VAETFSHIRG IYNASLQRYC LITFFLFGFA LGFYLLLKGL GVDLLWTLEK 

       250        260        270        280        290        300 
AKRWCERPEW VHLDTTPFAS LFKNLGTLLG LGLALNSSMY RKSCKGELRK SLPFRLACIV 

       310        320        330        340        350 
ASLGLLHLFD SLKPPSQIES IFYILSFCKS ATVPFASVSL IPYCLARLLG QTHKKSL 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L37333 mRNA. Translation: AAA74381.1. Different initiation.
U07993 mRNA. Translation: AAA19966.1.
D78592 mRNA. Translation: BAA24348.1.
BC090067 mRNA. Translation: AAH90067.2. Different initiation.
PIRJC2371.
RefSeqNP_037230.2. NM_013098.2.
UniGeneRn.10992.

3D structure databases

ProteinModelPortalP43428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4577794.

Chemistry

BindingDBP43428.
ChEMBLCHEMBL4759.

Proteomic databases

PRIDEP43428.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000028033; ENSRNOP00000028033; ENSRNOG00000036806.
GeneID25634.
KEGGrno:25634.
UCSCRGD:2644. rat.

Organism-specific databases

CTD2538.
RGD2644. G6pc.

Phylogenomic databases

GeneTreeENSGT00510000046461.
HOGENOMHOG000264239.
HOVERGENHBG003560.
InParanoidP43428.
KOK01084.
OMAGSSINTH.

Enzyme and pathway databases

SABIO-RKP43428.
UniPathwayUPA00138.

Gene expression databases

GenevestigatorP43428.

Family and domain databases

Gene3D1.20.144.10. 1 hit.
InterProIPR016275. Glucose-6-phosphatase.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamPF01569. PAP2. 1 hit.
[Graphical view]
PIRSFPIRSF000905. Glucose-6-phosphatase. 1 hit.
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMSSF48317. SSF48317. 1 hit.
ProtoNetSearch...

Other

NextBio607447.

Entry information

Entry nameG6PC_RAT
AccessionPrimary (citable) accession number: P43428
Secondary accession number(s): Q5FVC9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 14, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways