ID G6PC3_RAT Reviewed; 346 AA. AC Q6AZ83; Q811R7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 24-JAN-2024, entry version 121. DE RecName: Full=Glucose-6-phosphatase 3; DE Short=G-6-Pase 3; DE Short=G6Pase 3; DE EC=3.1.3.9; GN Name=G6pc3; 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 STRAIN=Sprague-Dawley; TISSUE=Brain; RA Middleditch C., Darakhshan F., Guionie O., Bonnefont J., Burchell A., RA Clottes E.; RT "Cloning of a glucose-6-phosphatase catalytic subunit-related sequence RT expressed in rodent tissues."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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). RN [3] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=17158265; DOI=10.1152/ajpregu.00566.2006; RA Azzout-Marniche D., Gaudichon C., Blouet C., Bos C., Mathe V., RA Huneau J.-F., Tome D.; RT "Liver glyconeogenesis: a pathway to cope with postprandial amino acid RT excess in high-protein fed rats?"; RL Am. J. Physiol. 292:R1400-R1407(2007). CC -!- FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic CC reticulum. May form with the glucose-6-phosphate transporter CC (SLC37A4/G6PT) a ubiquitously expressed complex responsible for glucose CC production through glycogenolysis and gluconeogenesis. Probably CC required for normal neutrophil function (By similarity). {ECO:0000250}. 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 -!- ACTIVITY REGULATION: Inhibited by vanadate. {ECO:0000250}. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; CC Multi-pass membrane protein {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in liver and kidney. It is the major CC glucose-6-phosphatase expressed in the small intestine. CC {ECO:0000269|PubMed:17158265}. CC -!- INDUCTION: Up-regulated upon fasting. {ECO:0000269|PubMed:17158265}. CC -!- SIMILARITY: Belongs to the glucose-6-phosphatase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY186240; AAO39165.1; -; mRNA. DR EMBL; BC078689; AAH78689.1; -; mRNA. DR RefSeq; NP_788266.2; NM_176077.3. DR AlphaFoldDB; Q6AZ83; -. DR SMR; Q6AZ83; -. DR STRING; 10116.ENSRNOP00000028375; -. DR PhosphoSitePlus; Q6AZ83; -. DR PaxDb; 10116-ENSRNOP00000028375; -. DR Ensembl; ENSRNOT00000108412.1; ENSRNOP00000080695.1; ENSRNOG00000020902.6. DR Ensembl; ENSRNOT00055056572; ENSRNOP00055046678; ENSRNOG00055032725. DR Ensembl; ENSRNOT00060023281; ENSRNOP00060018468; ENSRNOG00060013639. DR Ensembl; ENSRNOT00065048519; ENSRNOP00065039783; ENSRNOG00065028147. DR GeneID; 303565; -. DR KEGG; rno:303565; -. DR UCSC; RGD:727875; rat. DR AGR; RGD:727875; -. DR CTD; 92579; -. DR RGD; 727875; G6pc3. DR eggNOG; ENOG502QS5D; Eukaryota. DR GeneTree; ENSGT00950000183150; -. DR HOGENOM; CLU_052517_0_0_1; -. DR InParanoid; Q6AZ83; -. DR OMA; KKWCSRA; -. DR OrthoDB; 4030642at2759; -. DR PhylomeDB; Q6AZ83; -. DR TreeFam; TF324388; -. DR Reactome; R-RNO-70263; Gluconeogenesis. DR UniPathway; UPA00138; -. DR PRO; PR:Q6AZ83; -. DR Proteomes; UP000002494; Chromosome 10. DR Bgee; ENSRNOG00000020902; Expressed in testis and 20 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:RGD. DR GO; GO:0006094; P:gluconeogenesis; IDA:RGD. DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IDA:RGD. DR GO; GO:0015760; P:glucose-6-phosphate transport; ISO:RGD. DR CDD; cd03381; PAP2_glucose_6_phosphatase; 1. DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1. DR InterPro; IPR016275; Glucose-6-phosphatase. DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf. DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase. DR PANTHER; PTHR12591; GLUCOSE-6-PHOSPHATASE; 1. DR PANTHER; PTHR12591:SF2; GLUCOSE-6-PHOSPHATASE 3; 1. DR Pfam; PF01569; PAP2; 1. DR PIRSF; PIRSF000905; Glucose-6-phosphatase; 1. DR SMART; SM00014; acidPPc; 1. DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1. DR Genevisible; Q6AZ83; RN. PE 2: Evidence at transcript level; KW Endoplasmic reticulum; Gluconeogenesis; Hydrolase; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..346 FT /note="Glucose-6-phosphatase 3" FT /id="PRO_0000334514" FT TOPO_DOM 1..25 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 26..46 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 47..56 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 57..77 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 78..115 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 116..135 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 136..140 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 141..162 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 163..167 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 168..186 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 187..197 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 198..218 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 219..254 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 255..273 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 274..283 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 284..304 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 305..307 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 308..328 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 329..346 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT ACT_SITE 114 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 167 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT BINDING 79 FT /ligand="substrate" FT /evidence="ECO:0000255" FT BINDING 161 FT /ligand="substrate" FT /evidence="ECO:0000255" FT CONFLICT 106 FT /note="T -> I (in Ref. 1; AAO39165)" FT /evidence="ECO:0000305" SQ SEQUENCE 346 AA; 38834 MW; 59531F3030990F2F CRC64; MESTLSAGIM MAEALQNQLP GLENMWLWVT FLADPKNLFQ FYFPAVYYAS RRLGISLFWI AFITEWLNLV FKWFLFGDRP FWWVHESGYS AQTPVQIHQF PSSCETGPGS PSGHCMITGA ALWPVMIAIS SQVASQTRSP WVRVIPGLAY CTFLLAVGLS RVFLLAHFPH QVLAGLLAGV ILGWLLSPRV PMERELSFYG LTALTLMLGA SLMYWTLFTL GLDLSWSINL ASKWCDRPEW VLVDSRPFAS LSRDSGSALG LGIALHTPCY AQIRRVHLGN GQKIACFVLA MGLLVFLEWL GHPPQISLFY IFNFLKFTLW PCLVVALVPW MVHTLSAQEA PPIRSS //