Glucose-6-phosphatase - Rattus norvegicus (Rat)

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P43428 (G6PC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 84. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glucose-6-phosphatase
Short name=G-6-Pase
Short name=G6Pase
EC=3.1.3.9

Gene names

Name:	G6pc
Synonyms:	G6pt

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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	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.

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 direct assay. Source: RGD glucose 6-phosphate metabolic process Inferred from direct assay. Source: RGD glucose homeostasis Inferred from mutant phenotype. Source: RGD lipid homeostasis Inferred from mutant phenotype. Source: RGD phosphorylated carbohydrate dephosphorylation Inferred from direct assay. Source: RGD response to food Inferred from expression pattern. Source: RGD
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from direct assay. Source: RGD
Molecular function	glucose-6-phosphatase activity Inferred from direct assay. Source: RGD
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_0000087415

Regions

Topological domain

1 – 28

Lumenal Potential

Transmembrane

29 – 49

Helical; Potential

Topological domain

50 – 60

Cytoplasmic Potential

Transmembrane

61 – 81

Helical; Potential

Topological domain

82 – 117

Lumenal Potential

Transmembrane

118 – 138

Helical; Potential

Topological domain

139 – 147

Cytoplasmic Potential

Transmembrane

148 – 168

Helical; Potential

Topological domain

169 – 170

Lumenal Potential

Transmembrane

171 – 191

Helical; Potential

Topological domain

192 – 211

Cytoplasmic Potential

Transmembrane

212 – 232

Helical; Potential

Topological domain

233 – 254

Lumenal Potential

Transmembrane

255 – 275

Helical; Potential

Topological domain

276 – 291

Cytoplasmic Potential

Transmembrane

292 – 312

Helical; Potential

Topological domain

313 – 320

Lumenal Potential

Transmembrane

321 – 341

Helical; Potential

Topological domain

342 – 357

Cytoplasmic Potential

Motif

354 – 357

Prevents secretion from ER Potential

Sites

Active site

119

Proton donor Potential

Active site

176

Nucleophile By similarity

Binding site

Substrate Potential

Binding site

170

Substrate Potential

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) By similarity

Experimental info

Sequence conflict

118

G → V in AAA19966. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P43428 [UniParc].

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

FASTA

357

40,556

        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' referencesShow '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: 7860767] [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: 8198588] [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: 8865366] [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: 15489334] [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.
IPI	IPI00200360.
PIR	JC2371.
RefSeq	NP_037230.2. NM_013098.2.
UniGene	Rn.10992.
3D structure databases
ProteinModelPortal	P43428.
ModBase	Search...
Protein-protein interaction databases
STRING	P43428.
Proteomic databases
PRIDE	P43428.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	25634.
KEGG	rno:25634.
Organism-specific databases
CTD	2538.
RGD	2644. G6pc.
Phylogenomic databases
eggNOG	maNOG13087.
GeneTree	ENSGT00510000046461.
HOVERGEN	HBG003560.
InParanoid	P43428.
Gene expression databases
ArrayExpress	P43428.
Genevestigator	P43428.
GermOnline	ENSRNOG00000036805. Rattus norvegicus.
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...
Other
NextBio	607447.

Entry information

Entry name

G6PC_RAT

Accession

Primary (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:	November 16, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents