G6PC3_BOVIN
ID G6PC3_BOVIN Reviewed; 346 AA.
AC Q148G2; Q7YSF2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 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 [MRNA].
RC TISSUE=Testis;
RA Clottes E., Mounier R., Rossignol F., Bonnefont J., Guionie O.,
RA Burchell A.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glucose-6-phosphatase family. {ECO:0000305}.
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DR EMBL; AY279358; AAP40635.1; -; mRNA.
DR EMBL; BC118357; AAI18358.1; -; mRNA.
DR RefSeq; NP_899208.2; NM_183364.3.
DR AlphaFoldDB; Q148G2; -.
DR SMR; Q148G2; -.
DR STRING; 9913.ENSBTAP00000021621; -.
DR PaxDb; Q148G2; -.
DR PRIDE; Q148G2; -.
DR Ensembl; ENSBTAT00000021621; ENSBTAP00000021621; ENSBTAG00000016253.
DR GeneID; 369023; -.
DR KEGG; bta:369023; -.
DR CTD; 92579; -.
DR VEuPathDB; HostDB:ENSBTAG00000016253; -.
DR VGNC; VGNC:29180; G6PC3.
DR eggNOG; ENOG502QS5D; Eukaryota.
DR GeneTree; ENSGT00950000183150; -.
DR HOGENOM; CLU_052517_0_0_1; -.
DR InParanoid; Q148G2; -.
DR OMA; KKWCSRA; -.
DR OrthoDB; 743717at2759; -.
DR TreeFam; TF324388; -.
DR Reactome; R-BTA-70263; Gluconeogenesis.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000016253; Expressed in pigment epithelium of eye and 106 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; ISS:UniProtKB.
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:0015760; P:glucose-6-phosphate transport; 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; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..346
FT /note="Glucose-6-phosphatase 3"
FT /id="PRO_0000334511"
FT TOPO_DOM 1..24
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..108
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..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 239
FT /note="E -> G (in Ref. 1; AAP40635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 38742 MW; EBFB51839598E363 CRC64;
MESTLGAGIA MAEALQNQLP WLENVWLWVT FLGDPKSLFL FYFPAAYYAS RRVGIAVLWI
SLITEWLNLV FKWFLFGDRP FWWVHESGYY SQAPAQVHQF PSSCETGPGS PSGHCMITGA
ALWPIMTAVS SQMATRAHSR WVRVIPSLAY CTFLLAVGLS RVFLLAHFPH QVLAGLITGA
VLGWLMTPQV PMERELSFYG LTSLALLLGA SLIYWTLFTL GLDLSWSINL ASKWCERPEW
VHLDSRPFAS LSRDSGAALG LGIALHSPCY AQVRRAHLGY GQKLVCLVLA MGLLGPLNWL
GYPPQISLFY IFNFLKYTLW PCLVLALVPW LVHMFSAQEA PPIRSS
