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Protein

Glucose-6-phosphatase

Gene

G6PC

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

D-glucose 6-phosphate + H2O = D-glucose + phosphate.

Pathway: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei83 – 831SubstrateSequence Analysis
Active sitei119 – 1191Proton donorSequence Analysis
Binding sitei170 – 1701SubstrateSequence Analysis
Active sitei176 – 1761NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Gluconeogenesis

Enzyme and pathway databases

UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphatase (EC:3.1.3.9)
Short name:
G-6-Pase
Short name:
G6Pase
Gene namesi
Name:G6PC
Synonyms:G6PT
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2828LumenalSequence AnalysisAdd
BLAST
Transmembranei29 – 4921HelicalSequence AnalysisAdd
BLAST
Topological domaini50 – 6011CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei61 – 8121HelicalSequence AnalysisAdd
BLAST
Topological domaini82 – 11736LumenalSequence AnalysisAdd
BLAST
Transmembranei118 – 13821HelicalSequence AnalysisAdd
BLAST
Topological domaini139 – 1479CytoplasmicSequence Analysis
Transmembranei148 – 16821HelicalSequence AnalysisAdd
BLAST
Topological domaini169 – 1702LumenalSequence Analysis
Transmembranei171 – 19121HelicalSequence AnalysisAdd
BLAST
Topological domaini192 – 20918CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei210 – 23021HelicalSequence AnalysisAdd
BLAST
Topological domaini231 – 25424LumenalSequence AnalysisAdd
BLAST
Transmembranei255 – 27521HelicalSequence AnalysisAdd
BLAST
Topological domaini276 – 29116CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei292 – 31221HelicalSequence AnalysisAdd
BLAST
Topological domaini313 – 3208LumenalSequence Analysis
Transmembranei321 – 34121HelicalSequence AnalysisAdd
BLAST
Topological domaini342 – 35716CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in G6PC are the cause of glycogen storage disease Ia (GSD-Ia); also known as von Gierke disease. GSD-Ia is characterized by hypoglycemia and hepatomegaly.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 357357Glucose-6-phosphatasePRO_0000087410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi96 – 961N-linked (GlcNAc...)By similarity

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000021606.

Structurei

3D structure databases

ProteinModelPortaliO19133.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi354 – 3574Prevents secretion from ERSequence Analysis

Sequence similaritiesi

Belongs to the glucose-6-phosphatase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG82628.
HOGENOMiHOG000264239.
HOVERGENiHBG003560.
InParanoidiO19133.
KOiK01084.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR016275. Glucose-6-phosphatase.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
PIRSFiPIRSF000905. Glucose-6-phosphatase. 1 hit.
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.

Sequencei

Sequence statusi: Complete.

O19133-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKGMDVLHD FGIQSTHYLQ VNYQDSQDWF ILVSVIADLR NAFYVLFPIW
60 70 80 90 100
FHLREAVGIK LLWVAVIGDW LNLVFKWILF GQRPYWWVMD TDYYSNTSVP
110 120 130 140 150
LIKQFPVTCE TGPGSPSGHA MGTAGVYYVM VTSTLSIFRG RKRPTYRFRC
160 170 180 190 200
LNILLWLGFW AVQLNVCLSR IYLAAHFPHQ VVAGVLSGIA VAETFRHIQS
210 220 230 240 250
IYNASLKKYF LITFFLFSFA IGFYLLLKGL GVDLLWTLEK ARRWCERPEW
260 270 280 290 300
VHIDTTPFAS LLKNVGTLFG LGVTLNSSMY RESCKGKLSK WFPFRLSCIV
310 320 330 340 350
VSLILLHLFD SLKPPSQTEL IFYTLSFCKS AAVPLASVSL IPYCLARVFD

QPDKKSL
Length:357
Mass (Da):40,969
Last modified:January 1, 1998 - v1
Checksum:iE60BFBD80485BEC1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti121 – 1211M → I in GSD-Ia. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91844 mRNA. Translation: AAB65147.1.
RefSeqiNP_001002993.1. NM_001002993.1.
UniGeneiCfa.204.

Genome annotation databases

GeneIDi403492.
KEGGicfa:403492.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91844 mRNA. Translation: AAB65147.1.
RefSeqiNP_001002993.1. NM_001002993.1.
UniGeneiCfa.204.

3D structure databases

ProteinModelPortaliO19133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000021606.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403492.
KEGGicfa:403492.

Organism-specific databases

CTDi2538.

Phylogenomic databases

eggNOGiNOG82628.
HOGENOMiHOG000264239.
HOVERGENiHBG003560.
InParanoidiO19133.
KOiK01084.

Enzyme and pathway databases

UniPathwayiUPA00138.

Miscellaneous databases

NextBioi20817007.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR016275. Glucose-6-phosphatase.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
PIRSFiPIRSF000905. Glucose-6-phosphatase. 1 hit.
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Isolation and nucleotide sequence of canine glucose-6-phosphatase mRNA: identification of mutation in puppies with glycogen storage disease type Ia."
    Kishnani P.S., Bao Y., Wu J.Y., Brix A.E., Lin J.L., Chen Y.T.
    Biochem. Mol. Med. 61:168-177(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GSD-IA ILE-121.
    Strain: Maltese.

Entry informationi

Entry nameiG6PC_CANFA
AccessioniPrimary (citable) accession number: O19133
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.