G6PC1_CANLF
ID G6PC1_CANLF Reviewed; 357 AA.
AC O19133;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT GSD-IA ILE-121, AND INVOLVEMENT IN
RP GSD-IA.
RC STRAIN=Maltese;
RX PubMed=9259982; DOI=10.1006/bmme.1997.2600;
RA Kishnani P.S., Bao Y., Wu J.Y., Brix A.E., Lin J.L., Chen Y.T.;
RT "Isolation and nucleotide sequence of canine glucose-6-phosphatase mRNA:
RT identification of mutation in puppies with glycogen storage disease type
RT Ia.";
RL Biochem. Mol. Med. 61:168-177(1997).
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 -!- DISEASE: Note=Defects in G6PC1 are the cause of glycogen storage
CC disease Ia (GSD-Ia); also known as von Gierke disease. GSD-Ia is
CC characterized by hypoglycemia and hepatomegaly.
CC {ECO:0000269|PubMed:9259982}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphatase family. {ECO:0000305}.
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DR EMBL; U91844; AAB65147.1; -; mRNA.
DR AlphaFoldDB; O19133; -.
DR STRING; 9615.ENSCAFP00000021606; -.
DR PaxDb; O19133; -.
DR eggNOG; ENOG502QS9B; Eukaryota.
DR InParanoid; O19133; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002254; Unplaced.
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:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Disease variant; Endoplasmic reticulum; Gluconeogenesis; Glycoprotein;
KW Hydrolase; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..357
FT /note="Glucose-6-phosphatase catalytic subunit 1"
FT /id="PRO_0000087410"
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:0000250"
FT VARIANT 121
FT /note="M -> I (in GSD-Ia)"
FT /evidence="ECO:0000269|PubMed:9259982"
SQ SEQUENCE 357 AA; 40969 MW; E60BFBD80485BEC1 CRC64;
MEKGMDVLHD FGIQSTHYLQ VNYQDSQDWF ILVSVIADLR NAFYVLFPIW FHLREAVGIK
LLWVAVIGDW LNLVFKWILF GQRPYWWVMD TDYYSNTSVP LIKQFPVTCE TGPGSPSGHA
MGTAGVYYVM VTSTLSIFRG RKRPTYRFRC LNILLWLGFW AVQLNVCLSR IYLAAHFPHQ
VVAGVLSGIA VAETFRHIQS IYNASLKKYF LITFFLFSFA IGFYLLLKGL GVDLLWTLEK
ARRWCERPEW VHIDTTPFAS LLKNVGTLFG LGVTLNSSMY RESCKGKLSK WFPFRLSCIV
VSLILLHLFD SLKPPSQTEL IFYTLSFCKS AAVPLASVSL IPYCLARVFD QPDKKSL
