ID F4WHC1_ACREC Unreviewed; 396 AA.
AC F4WHC1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Prostaglandin E synthase 2 {ECO:0000313|EMBL:EGI66398.1};
GN ORFNames=G5I_05081 {ECO:0000313|EMBL:EGI66398.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI66398.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins. {ECO:0000256|ARBA:ARBA00002549}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409}.
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DR EMBL; GL888158; EGI66398.1; -; Genomic_DNA.
DR RefSeq; XP_011052925.1; XM_011054623.1.
DR AlphaFoldDB; F4WHC1; -.
DR STRING; 103372.F4WHC1; -.
DR EnsemblMetazoa; XM_011054623.1; XP_011052925.1; LOC105145201.
DR GeneID; 105145201; -.
DR KEGG; aec:105145201; -.
DR eggNOG; KOG3029; Eukaryota.
DR InParanoid; F4WHC1; -.
DR OrthoDB; 1226at2759; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03197; GST_C_mPGES2; 1.
DR CDD; cd03040; GST_N_mPGES2; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 6.20.200.30; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR034334; PGES2.
DR InterPro; IPR034335; PGES2_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12782; MICROSOMAL PROSTAGLANDIN E SYNTHASE-2; 1.
DR PANTHER; PTHR12782:SF5; PROSTAGLANDIN E SYNTHASE 2; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01203; Prostaglandin_E_synthase_like1; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 114..160
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 396 AA; 45508 MW; BA9D7733CFD85607 CRC64;
MAAIRNLARF TERAKFLNKC YFASQNGILR SFSINGAVIG LSRETQTLVK FGLISAATGI
AVGASYAYYK INETRKNIAL EGTELNTALL EHKPPVTPSR KIAYSGDITG LKLTLFQYQT
CPFCCKVRAF LDYYGISYDV VEVDPVLRKE IGWSSYKKVP ILLTQVEGGY QPLNDSTMIV
SLLASYLYDR SQKIEEFADY YPSVGMHDET GKFKYEIINK YFLMFNNQLP KNRTMDDIIE
ERKWRKWADD VFVHTLSPNV YRTLDESYKT FSWFSEVGKW EEYFPTWERL LIVNVGAMAM
WLIGKRLKKR HRLKNDVRQS LYDEANYWLR GIKARGTTFM GGNKPDLSDL AIYGILKSIE
GCDAFQDLKT HTNMGVWYNA MKEQVDAHSG SANLSR
//
