ID G3SXL5_LOXAF Unreviewed; 356 AA.
AC G3SXL5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Glucose-6-phosphatase {ECO:0000256|ARBA:ARBA00012634, ECO:0000256|PIRNR:PIRNR000905};
DE EC=3.1.3.9 {ECO:0000256|ARBA:ARBA00012634, ECO:0000256|PIRNR:PIRNR000905};
GN Name=G6PC2 {ECO:0000313|Ensembl:ENSLAFP00000005155.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000005155.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000005155.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000005155.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000005155.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000005155.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|PIRNR:PIRNR000905}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphatase family.
CC {ECO:0000256|ARBA:ARBA00009266, ECO:0000256|PIRNR:PIRNR000905}.
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DR AlphaFoldDB; G3SXL5; -.
DR STRING; 9785.ENSLAFP00000005155; -.
DR Ensembl; ENSLAFT00000006146.2; ENSLAFP00000005155.2; ENSLAFG00000006146.2.
DR eggNOG; ENOG502QS9B; Eukaryota.
DR GeneTree; ENSGT00950000183150; -.
DR HOGENOM; CLU_052517_0_0_1; -.
DR InParanoid; G3SXL5; -.
DR OMA; EEHLFYV; -.
DR TreeFam; TF324388; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004346; F:glucose-6-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl.
DR CDD; cd03381; PAP2_glucose_6_phosphatase; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR016275; Glucose-6-phosphatase.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR12591; GLUCOSE-6-PHOSPHATASE; 1.
DR PANTHER; PTHR12591:SF1; GLUCOSE-6-PHOSPHATASE 2; 1.
DR Pfam; PF01569; PAP2; 1.
DR PIRSF; PIRSF000905; Glucose-6-phosphatase; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR000905};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|PIRNR:PIRNR000905};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000905};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000905};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..195
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-1"
FT ACT_SITE 175
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-1"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-2"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-2"
SQ SEQUENCE 356 AA; 40801 MW; 6354FF4FCF00AFA9 CRC64;
KMDFLHRNGV LVIQHLQKDY RAYYDFLNFM SSVGDPRNIF SIYFPLWFQL NQTVGTKMIW
VAVIGDWFNL IFKWILFGHR PYWWVQETQI YPNHSSPCLE QFPTTCETGP GSPSGHAMGS
SCVWYVMVTA ALSYTVSQLD KSSITFHRLT WSFLWSLFWL IQISVCISRV FIATHFPHQV
ILGVIGGMLV AEAFEHTPGI QTASLSTYLK TNLFLFLFAL GFYLLLSLLN IDLLWSVPIA
KKWCANPDWI HIDTTPFAGL VRNLGVLFGL GFAINSEMFL LSCQGENGYK LSFRLLCVMT
SLTTLQLYHF IKIPTHTEHL FYVLSFCKSA SIPLTVVALI PYCIHTLMKP SEKKTK
//
