ID M3XL09_LATCH Unreviewed; 355 AA.
AC M3XL09;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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:ENSLACP00000023415.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000023415.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000023415.1}
RP IDENTIFICATION.
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 EMBL; AFYH01119083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01119084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01119085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_014347075.1; XM_014491589.1.
DR AlphaFoldDB; M3XL09; -.
DR STRING; 7897.ENSLACP00000023415; -.
DR Ensembl; ENSLACT00000026376.1; ENSLACP00000023415.1; ENSLACG00000022170.1.
DR GeneID; 102352326; -.
DR KEGG; lcm:102352326; -.
DR CTD; 57818; -.
DR eggNOG; ENOG502QS9B; Eukaryota.
DR GeneTree; ENSGT00950000183150; -.
DR HOGENOM; CLU_052517_0_0_1; -.
DR InParanoid; M3XL09; -.
DR OMA; EEHLFYV; -.
DR OrthoDB; 4030642at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008672; 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 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:UP000008672};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..194
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-1"
FT ACT_SITE 174
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-1"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-2"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-2"
SQ SEQUENCE 355 AA; 40607 MW; BA65176369A559CA CRC64;
MDFLHSNGVL IIQHLQKNYK GYQDFLNFMS SVGDPRNIFS IYFPLWFQLS QMIGTKMIWV
AVIGDWFNLI FKWILFGHRP YWWVQESQFY QNLSVPQLEQ FPITCETGPG SPSGHAMGSS
CVWYVMITAA LSYLKPRKAK SLSPLYWLAW TILWIAFWII QISVCISRVF VATHFPHQVV
LGVLGGIIVA EAFEYVPFIH TASLRIYIKT NLFLFFFALG LYLVLKMIDI DLLWSVPKAV
KWCANPDWIH IGTTPFAGLV RNLGAFFGLG IAINSEMFIQ SCKGKNGYRT SFKLMCVAAS
LTTLLLYDFI KIPTHTEFLF YILSFCKSAA IPLTVIALIP YFIHLLLGQT GKKID
//
