G6PC3_RAT
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 03-AUG-2022, entry version 115.
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}.
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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 PaxDb; Q6AZ83; -.
DR Ensembl; ENSRNOT00000108412; ENSRNOP00000080695; ENSRNOG00000020902.
DR GeneID; 303565; -.
DR KEGG; rno:303565; -.
DR UCSC; RGD:727875; rat.
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; 743717at2759; -.
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 tissues.
DR Genevisible; Q6AZ83; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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; 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 GO; GO:0006796; P:phosphate-containing compound metabolic process; IDA:RGD.
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;
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
