G6PC1_BOVIN
ID G6PC1_BOVIN Reviewed; 357 AA.
AC Q29RU6;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BC114011; AAI14012.1; -; mRNA.
DR RefSeq; NP_001069592.1; NM_001076124.2.
DR AlphaFoldDB; Q29RU6; -.
DR STRING; 9913.ENSBTAP00000013436; -.
DR PaxDb; Q29RU6; -.
DR Ensembl; ENSBTAT00000013436; ENSBTAP00000013436; ENSBTAG00000010184.
DR GeneID; 538710; -.
DR KEGG; bta:538710; -.
DR CTD; 2538; -.
DR VEuPathDB; HostDB:ENSBTAG00000010184; -.
DR VGNC; VGNC:29178; G6PC1.
DR eggNOG; ENOG502QS9B; Eukaryota.
DR GeneTree; ENSGT00950000183150; -.
DR HOGENOM; CLU_052517_0_0_1; -.
DR InParanoid; Q29RU6; -.
DR OMA; RRWCERP; -.
DR OrthoDB; 743717at2759; -.
DR TreeFam; TF324388; -.
DR Reactome; R-BTA-70263; Gluconeogenesis.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000010184; Expressed in metanephros cortex and 31 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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_0000350564"
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; 40827 MW; B932F00C8940EFEE CRC64;
MEKGMNVLHD FGIQSTHYLQ VNYQNSQDWF ILVSVIADLR NAFYVLFPIW FHLREAVGIK
LLWVAVIGDW LNLVFKWILF GQRPYWWVLD TDYYSNTSAP LIKQFPVTCE TGPGSPSGHA
MGTAGVYYVM VTSTLSIFRG KKKPTYRFRC LNVMLWLGFW VVQLNVCLSR IYLAAHFPHQ
VVAGVLSGIA VAETFRHIQS IYNASLKKYF LITCFLFSFA IGFYLLLKWL GVDLLWTLEK
AKRRCERPEW VHIDTTPFAS LLKNLGTLFG LGLALNSSMY RESCKGKLSK WFPFRLSCIV
ASLVLLHLFD SLKPPSQIEL IFYVLSFCKS AAVPLASVSL IPYCLAWVLG QPNKKTV
