ID E1ZYB1_CAMFO Unreviewed; 358 AA.
AC E1ZYB1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Prostaglandin E synthase 2 {ECO:0000313|EMBL:EFN73810.1};
GN ORFNames=EAG_06452 {ECO:0000313|EMBL:EFN73810.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN73810.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL435204; EFN73810.1; -; Genomic_DNA.
DR AlphaFoldDB; E1ZYB1; -.
DR STRING; 104421.E1ZYB1; -.
DR EnsemblMetazoa; XM_011266201.3; XP_011264503.1; LOC105256356.
DR InParanoid; E1ZYB1; -.
DR OMA; DYCLTEG; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000000311; 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..122
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 358 AA; 41354 MW; 3DD58EF4BAA9DAA0 CRC64;
MQQPQKTQSL VKIGLIGAVT GVVLGAGYAL HEINKTRENI ALEGTQAEIT LLKYKPPVTP
SRKIASPVDT TGLNVTLFQY QTCPFCCKVR VFLDYYGISY DVVEVDPVLR KEIGWSSYKK
VPILLTKVEE GYQPLNDSSM IISLLASHLH DKSYKVEELA NYYPSIAMHD EHGKFKYEII
NKYFLMFNKN LPKDRSINDI TEERNWRKWA DEILVHTLSP NVYRTIDESY RTFNWFSEVG
KWEEYFPLWE RMLIVNVGAT AMWLIGKRLK KRHRLKDDVR QSLYDEVNYW LRAIRSRGTE
FMGGSKPDLS DLAVYGILKS IEGCDAFQDL LTHTKIGIWY NGMKEQVDTH SGSVNLSR
//
