ID   G6PC3_DANRE             Reviewed;         339 AA.
AC   A1A5Z0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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; ORFNames=zgc:158425;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic
CC       reticulum. May be responsible for glucose production through
CC       glycogenolysis and gluconeogenesis (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   -!- 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; BC128866; AAI28867.1; -; mRNA.
DR   RefSeq; NP_001073535.1; NM_001080066.1.
DR   AlphaFoldDB; A1A5Z0; -.
DR   SMR; A1A5Z0; -.
DR   STRING; 7955.ENSDARP00000027964; -.
DR   PaxDb; A1A5Z0; -.
DR   PeptideAtlas; A1A5Z0; -.
DR   GeneID; 790919; -.
DR   KEGG; dre:790919; -.
DR   CTD; 92579; -.
DR   ZFIN; ZDB-GENE-061215-19; g6pc3.
DR   eggNOG; ENOG502QS5D; Eukaryota.
DR   InParanoid; A1A5Z0; -.
DR   OrthoDB; 743717at2759; -.
DR   PhylomeDB; A1A5Z0; -.
DR   Reactome; R-DRE-70263; Gluconeogenesis.
DR   UniPathway; UPA00138; -.
DR   PRO; PR:A1A5Z0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:ZFIN.
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..339
FT                   /note="Glucose-6-phosphatase 3"
FT                   /id="PRO_0000334515"
FT   TOPO_DOM        1..26
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..54
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        76..114
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..143
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..169
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..195
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        217..308
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..339
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"
SQ   SEQUENCE   339 AA;  38003 MW;  A22AE6F35F354057 CRC64;
     MESLYRQGVW MAEALQQNSR SLEDLWLVAS HMGDPKAAVL LVFPVVFYIH RRTGIAVLWV
     AALSEWLNLV FKWILFGERP YWWIGQSGLF SEKPPEVQQF QSTCESGPGS PSGHAMVTSA
     VWWVIISSLA SFSQAYTGSK ILSAVLYLLY AVFLGCVGLS RIFILAHFPH QVVAGLLTGV
     LLGVFLKRSV PERRPLLFFF RFSMALLGAA LIFHAVLEKT GIDLSWSISL AKRWCSRSEW
     VRMDTAPFSS LNRDAGVLLG LGLAQYWKPG GWTLPRAPRT LCLALSSLAL HYISRFPLPT
     VPPLLFYSLF FLKYSIVPQV VMVLVPGFVH LLTAKPKRE