G6PC1_HAPNU
ID G6PC1_HAPNU Reviewed; 352 AA.
AC O42153;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 73.
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 Haplochromis nubilus (Blue Victoria mouthbrooder) (Tilapia nubila).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=51172;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10565541; DOI=10.3109/10425179909033932;
RA Nagl S., Mayer W.E., Klein J.;
RT "Isolation and sequencing of cDNA clones coding for the catalytic unit of
RT glucose-6-phosphatase from two haplochromine cichlid fishes.";
RL DNA Seq. 10:25-29(1999).
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; AF008945; AAB69285.1; -; mRNA.
DR AlphaFoldDB; O42153; -.
DR UniPathway; UPA00138; -.
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:0004346; F:glucose-6-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
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; Hydrolase; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..352
FT /note="Glucose-6-phosphatase catalytic subunit 1"
FT /id="PRO_0000087411"
FT TOPO_DOM 1..27
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..113
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..166
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..256
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 257..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..324
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT MOTIF 349..352
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 172
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 352 AA; 39904 MW; 7E9F1DF417298BAA CRC64;
MDLLHSWGVE LAVYLQTRYG KYEGLFDLAS TVADLHTTFF WLFPIWFHLR RDTALRLIWV
AVIGDWLNLV LKWVLFGERP YWWVHETKFY GAGPAPSLQQ FPITCETGPG SPSGHAMGAA
GVWYVMVTAL LSIAREKQCP PLLYRFLYIG LWMLMGLVEL VVCISRVYMA AHFPHQVIAG
IITGTLVAEV VSKEKWIYSA SLKKYFLITL FLTSFAVGFY VLLKALDVDL LWTMEKAQKW
CIRPEWVHLD SAPFASLLRN MGSLFGLGLG LHSPFYKTTK MRIMSAPLRI GCIVISVSLL
HLLDGWTFSP ENHMTFYALS FGKSAVALLI PTTLVPWALS KIYPVKTEGK NL
