G6PC1_RAT
ID G6PC1_RAT Reviewed; 357 AA.
AC P43428; Q5FVC9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glucose-6-phosphatase catalytic subunit 1;
DE EC=3.1.3.9 {ECO:0000250|UniProtKB:P35575};
DE AltName: Full=Glucose-6-phosphatase;
DE Short=G-6-Pase;
DE Short=G6Pase;
GN Name=G6pc1; Synonyms=G6pc, G6pt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7860767; DOI=10.1172/jci117733;
RA Haber B.A., Chin S., Chuang E., Buikuisen W., Naji A., Taub R.A.;
RT "High levels of glucose-6-phosphatase gene and protein expression reflect
RT an adaptive response in proliferating liver and diabetes.";
RL J. Clin. Invest. 95:832-841(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=8198588; DOI=10.1006/bbrc.1994.1702;
RA Lange A.J., Argaud D.M., El-Maghrabi M.R., Pan W., Subir M., Pilkis S.J.;
RT "Isolation of a cDNA for the catalytic subunit of rat liver glucose-6-
RT phosphatase: regulation of gene expression in FAO hepatoma cells by
RT insulin, dexamethasone and cAMP.";
RL Biochem. Biophys. Res. Commun. 201:302-309(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8865366;
RA Shingu R., Nakajima H., Horikawa Y., Hamaguchi T., Yamasaki T.,
RA Miyagawa J., Namba M., Hanafusa T., Matsuzawa Y.;
RT "Expression and distribution of glucose-6-phosphatase catalytic subunit
RT messenger RNA and its changes in the diabetic state.";
RL Res. Commun. Mol. Pathol. Pharmacol. 93:13-24(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic
CC reticulum. Forms with the glucose-6-phosphate transporter
CC (SLC37A4/G6PT) the complex responsible for glucose production in the
CC terminal step of glycogenolysis and gluconeogenesis. Hence, it is the
CC key enzyme in homeostatic regulation of blood glucose levels.
CC {ECO:0000250|UniProtKB:P35575}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + H2O = D-glucose + phosphate;
CC Xref=Rhea:RHEA:16689, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:61548; EC=3.1.3.9;
CC Evidence={ECO:0000250|UniProtKB:P35575};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000250|UniProtKB:P35575}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P35575}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74381.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH90067.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L37333; AAA74381.1; ALT_INIT; mRNA.
DR EMBL; U07993; AAA19966.1; -; mRNA.
DR EMBL; D78592; BAA24348.1; -; mRNA.
DR EMBL; BC090067; AAH90067.2; ALT_INIT; mRNA.
DR PIR; JC2371; JC2371.
DR RefSeq; NP_037230.2; NM_013098.2.
DR AlphaFoldDB; P43428; -.
DR BioGRID; 247663; 1.
DR STRING; 10116.ENSRNOP00000028033; -.
DR BindingDB; P43428; -.
DR ChEMBL; CHEMBL4759; -.
DR GlyGen; P43428; 1 site.
DR PRIDE; P43428; -.
DR Ensembl; ENSRNOT00000085831; ENSRNOP00000071453; ENSRNOG00000053448.
DR GeneID; 25634; -.
DR KEGG; rno:25634; -.
DR UCSC; RGD:2644; rat.
DR CTD; 2538; -.
DR RGD; 2644; G6pc1.
DR eggNOG; ENOG502QS9B; Eukaryota.
DR GeneTree; ENSGT00950000183207; -.
DR HOGENOM; CLU_052517_0_0_1; -.
DR InParanoid; P43428; -.
DR OMA; RRWCERP; -.
DR OrthoDB; 743717at2759; -.
DR BRENDA; 3.1.3.9; 5301.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR SABIO-RK; P43428; -.
DR UniPathway; UPA00138; -.
DR PRO; PR:P43428; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000051171; Expressed in liver and 9 other tissues.
DR Genevisible; P43428; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:RGD.
DR GO; GO:0042301; F:phosphate ion binding; ISO:RGD.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0006094; P:gluconeogenesis; IDA:RGD.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IDA:RGD.
DR GO; GO:0042593; P:glucose homeostasis; IMP:RGD.
DR GO; GO:0015760; P:glucose-6-phosphate transport; ISO:RGD.
DR GO; GO:0005980; P:glycogen catabolic process; ISO:RGD.
DR GO; GO:0005977; P:glycogen metabolic process; ISO:RGD.
DR GO; GO:0055088; P:lipid homeostasis; IMP:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IDA:RGD.
DR GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; IDA:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR GO; GO:0032094; P:response to food; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:1904638; P:response to resveratrol; IEP:RGD.
DR GO; GO:0008202; P:steroid metabolic process; ISO:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR GO; GO:0046415; P:urate metabolic process; ISO:RGD.
DR InterPro; IPR016275; Glucose-6-phosphatase.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR PIRSF; PIRSF000905; Glucose-6-phosphatase; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Gluconeogenesis; Glycoprotein; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..357
FT /note="Glucose-6-phosphatase catalytic subunit 1"
FT /id="PRO_0000087415"
FT TOPO_DOM 1..28
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..117
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..170
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..254
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..320
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT MOTIF 354..357
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 176
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CONFLICT 118
FT /note="G -> V (in Ref. 2; AAA19966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 40556 MW; C44960E102F4244D CRC64;
MEERMNVLHD FGIQSTRYLQ VNYEDSQDWF VLVSVIADLR NAFYVLFPIW FHIQETVGIN
LLWVAVVGDW FNLVFKWILF GQRPYWWVLD TDYYSNSSVP LIKQFPVTCE TGPGSPSGHA
MGTAGVYYVM VTSTLAIFRG KKKSTYGFRC LNVVLWLGYW AVQLNVCLSR IYLAAHFPHQ
VVAGVLSGIA VAETFSHIRG IYNASLQRYC LITFFLFGFA LGFYLLLKGL GVDLLWTLEK
AKRWCERPEW VHLDTTPFAS LFKNLGTLLG LGLALNSSMY RKSCKGELRK SLPFRLACIV
ASLGLLHLFD SLKPPSQIES IFYILSFCKS ATVPFASVSL IPYCLARLLG QTHKKSL
