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Database: UniProt
Entry: W5P1N7_SHEEP
LinkDB: W5P1N7_SHEEP
Original site: W5P1N7_SHEEP 
ID   W5P1N7_SHEEP            Unreviewed;       357 AA.
AC   W5P1N7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Glucose-6-phosphatase {ECO:0000256|PIRNR:PIRNR000905};
DE            EC=3.1.3.9 {ECO:0000256|PIRNR:PIRNR000905};
GN   Name=G6PC1 {ECO:0000313|Ensembl:ENSOARP00000004336.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000004336.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000004336.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000004336.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000004336.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037155}.
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:0000256|ARBA:ARBA00000651};
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   EMBL; AMGL01018698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004013000.1; XM_004012951.3.
DR   AlphaFoldDB; W5P1N7; -.
DR   STRING; 9940.ENSOARP00000004336; -.
DR   PaxDb; 9940-ENSOARP00000004336; -.
DR   Ensembl; ENSOART00000004412.1; ENSOARP00000004336.1; ENSOARG00000004059.1.
DR   GeneID; 100037689; -.
DR   KEGG; oas:100037689; -.
DR   CTD; 2538; -.
DR   eggNOG; ENOG502QS9B; Eukaryota.
DR   HOGENOM; CLU_052517_0_0_1; -.
DR   OMA; WFILVSM; -.
DR   OrthoDB; 4030642at2759; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002356; Chromosome 11.
DR   Bgee; ENSOARG00000004059; Expressed in metanephros cortex and 11 other cell types or tissues.
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   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:SF3; GLUCOSE-6-PHOSPHATASE CATALYTIC SUBUNIT 1; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000002356};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        61..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        179..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        292..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          57..196
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   ACT_SITE        119
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000905-1"
FT   ACT_SITE        176
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000905-1"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000905-2"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000905-2"
SQ   SEQUENCE   357 AA;  40712 MW;  4CAF9248843AD457 CRC64;
     MEKGMNVLHD FGIQSTHYLQ VNYQNSQDWF ILVSVIADLR NAFYVLFPIW FHLREAVGIK
     LLWVAVIGDW LNLVFKWILF GQRPYWWVLD TDYYSNTSVP LIKQFPVTCE TGPGSPSGHA
     MGTAGVYYVM VTSILSIFHG KKKPTYRFRC LNVMLWLGFW IVQLNVCLSR IYLAAHFPHQ
     VVAGVFSGIA VAETFRHIQS IYNASLKKYF LITCFLFSFA IGFYLLLKWL GVDLLWTLEK
     AKRSCERPEW VHIDTTPFAS LLKNLGTLFG LGLALNSSMY RESCKGKLSK SFPFRLSCIV
     ASLVLLHLFD SLKPPSQIEL IFYVLSFCKS AAVPLASVSL IPYCLARVLG QPNKKTL
//
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