ID G6PC1_FELCA Reviewed; 357 AA. AC Q19KA1; DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 92. 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; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis. OX NCBI_TaxID=9685; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=17852328; DOI=10.1080/10425170701574920; RA Lindbloom S., LeCluyse M., Schermerhorn T.; RT "Cloning and comparative bioinformatic analysis of feline glucose-6- RT phosphatase catalytic subunit cDNA."; RL DNA Seq. 19:256-263(2008). 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 --------------------------------------------------------------------------- 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; DQ525410; ABF82030.1; -; mRNA. DR RefSeq; NP_001035837.1; NM_001042378.1. DR AlphaFoldDB; Q19KA1; -. DR STRING; 9685.ENSFCAP00000025827; -. DR GlyCosmos; Q19KA1; 1 site, No reported glycans. DR PaxDb; 9685-ENSFCAP00000012186; -. DR Ensembl; ENSFCAT00000047985.3; ENSFCAP00000025827.1; ENSFCAG00000036883.3. DR GeneID; 723970; -. DR KEGG; fca:723970; -. DR VGNC; VGNC:99060; G6PC1. DR eggNOG; ENOG502QS9B; Eukaryota. DR GeneTree; ENSGT00950000183150; -. DR HOGENOM; CLU_052517_0_0_1; -. DR InParanoid; Q19KA1; -. DR OMA; WFILVSM; -. DR OrthoDB; 4030642at2759; -. DR TreeFam; TF324388; -. DR BRENDA; 3.1.3.9; 2235. DR UniPathway; UPA00138; -. DR Proteomes; UP000011712; Chromosome E1. DR Bgee; ENSFCAG00000036883; Expressed in liver and 2 other cell types or tissues. 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; IBA:GO_Central. DR GO; GO:0042301; F:phosphate ion binding; IEA:Ensembl. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:Ensembl. DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl. DR GO; GO:0015760; P:glucose-6-phosphate transport; IEA:Ensembl. DR GO; GO:0005980; P:glycogen catabolic process; IEA:Ensembl. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl. DR GO; GO:0008202; P:steroid metabolic process; IEA:Ensembl. DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl. DR GO; GO:0046415; P:urate metabolic process; IEA:Ensembl. 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:SF3; GLUCOSE-6-PHOSPHATASE CATALYTIC SUBUNIT 1; 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. 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_0000350563" 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..209 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P35575" FT TRANSMEM 210..230 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 231..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:0000255" SQ SEQUENCE 357 AA; 40761 MW; E821097701C7FF16 CRC64; MEKGMNVLHD FGIQSTHYLQ VNYQDSQDWF ILVSVIADLR NAFYVLFPIW FHLREAVGIK LLWVAVIGDW LNLVFKWILF GQRPYWWVMD TDYYSNASVP LIKQFPVTCE TGPGSPSGHA MGTAGVYYVM VTSTLSMFRG KKKPTYRFRC LNVILWLGFW AVQLNVCLSR IYLAAHFPHQ VVAGVLSGIA VAETFRHIQS IYNASLKKYF FITFFLLSFA IGFYLLLKGL GVDLLWTLEK ARRWCERPEW VHIDTTPFAS LLKNVGTLFG LGLALNSSMY RESCKGTLSK WFPFRLSCIV VSLILLHLFD SLKPPSQIEL IFYVLSFCKS AAVPLASVSL IPYCLARVLG QPDKKSL //