GenomeNet

Database: UniProt/TrEMBL
Entry: B0XAP6_CULQU
LinkDB: B0XAP6_CULQU
Original site: B0XAP6_CULQU 
ID   B0XAP6_CULQU            Unreviewed;       349 AA.
AC   B0XAP6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=glucose-6-phosphatase {ECO:0000256|ARBA:ARBA00012634};
DE            EC=3.1.3.9 {ECO:0000256|ARBA:ARBA00012634};
GN   ORFNames=CpipJ_CPIJ016653 {ECO:0000313|EMBL:EDS43835.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS43835.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS43835.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00009266}.
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DR   EMBL; DS232592; EDS43835.1; -; Genomic_DNA.
DR   RefSeq; XP_001866718.1; XM_001866683.1.
DR   AlphaFoldDB; B0XAP6; -.
DR   STRING; 7176.B0XAP6; -.
DR   KEGG; cqu:CpipJ_CPIJ016653; -.
DR   VEuPathDB; VectorBase:CPIJ016653; -.
DR   VEuPathDB; VectorBase:CQUJHB001886; -.
DR   eggNOG; ENOG502QS9B; Eukaryota.
DR   HOGENOM; CLU_052517_0_0_1; -.
DR   InParanoid; B0XAP6; -.
DR   OMA; EEHLFYV; -.
DR   OrthoDB; 4030642at2759; -.
DR   PhylomeDB; B0XAP6; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   PANTHER; PTHR12591:SF0; FI19814P1; 1.
DR   PANTHER; PTHR12591; GLUCOSE-6-PHOSPHATASE; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        213..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        317..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..202
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01569"
SQ   SEQUENCE   349 AA;  40375 MW;  A29E859D48DCD807 CRC64;
     MKLYSSLLKS EIYQILYVQD VFSNYEDFLA LVTKAFDPKV LFLTVIPVVA AFNTRLYSRL
     LLSVLLTEYF NTILKWCVVR VVAILAEDRP FWWVRETSEF TTLNRPKLYQ NELTCEPSPG
     NPSGHLMTST TYLYVIFSVL EEAAVLRHGK PVVISLRVCY YFSLLLISIS RMYFGCHFLH
     QCIFGILAGV LLTKVTMSLS FEKYLTKLTR RRRLAYCCLI CLLLLGIYWG QKLFGVDPQW
     PVKMAFKWCD DPFFLDPNTT LVFSIVRLTG ALFAFAIVGP VLKSAGLNWK RSVPLALTMM
     GAKWAAIYYT PRYYGVIVYY LYTFLVYLIF TYGYMRLVPA IATVDNYYC
//
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