ID A0A0N4UEI6_DRAME Unreviewed; 830 AA.
AC A0A0N4UEI6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=GPI ethanolamine phosphate transferase 3 {ECO:0000256|ARBA:ARBA00020841};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000579301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000579301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
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 PIGG/PIGN/PIGO family. PIGO subfamily.
CC {ECO:0000256|ARBA:ARBA00008695}.
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DR AlphaFoldDB; A0A0N4UEI6; -.
DR WBParaSite; DME_0000579301-mRNA-1; DME_0000579301-mRNA-1; DME_0000579301.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000038040; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:InterPro.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16023; GPI_EPT_3; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037675; PIG-O_N.
DR InterPro; IPR039524; PIGO/GPI13.
DR PANTHER; PTHR23071:SF1; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 3; 1.
DR PANTHER; PTHR23071; PHOSPHATIDYLINOSITOL GLYCAN; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..830
FT /note="GPI ethanolamine phosphate transferase 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005886710"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 572..589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 639..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 710..728
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..762
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 768..787
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..826
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 830 AA; 95518 MW; 21EC5A0BAD9E1268 CRC64;
LTLSLTVSLL MFQYGILIKR VELNERSSCS DVSYSINSCW VPSQFNRIIL IIVDALRYDF
VNPTNSHTFY GGHMKNVNNL LSRNNGNSLL FHFIADPPTT TMQRLKALTT GSLPTFIDMN
SNFASASISE DNWIDQLVQS GRKIVFMGDD TWVSLFPKQF HRKYHLPSFD VYDLHTVDDM
ILGNIYNELR RSDWTVLIAH FLGVDHCGHK HGPKSPEMVA KLSQMDDFIK NMTDLMNDET
LLVVMGDHGM TETGDHGGDA DMEIDAALFL YSRKKLLHSQ FVSDSVSQVD IVPTLSLLLD
LPIPFSNIGI VIESIFPQKL LPLVLRSNTW QIIRYAQRMA SEIPELEWHL RQFESGTENL
RKYRDTMSRM QLVFRYFWTS FNSYFIMIGL LSLLEAVLNC ADSIFNGDDI SISWLIFRSG
LLFMQAATYI TGDEEHYFSV IFILLCSSVS FRIIYLLNSL LTVTYSWSTV MLLFFLFFHA
ISFFSNSFIV FESITIRFLT QQKFNRPRRF MSFLDWFKHR LEYRKILMVL LVLFLLRLGS
VFERCREEQQ SACIQTVFAE PLSKVPSDTL KIIRFITAIL SFSFANYFAY QYLQKFPSES
VHSSFLFPSA IATICHWSTE LIPDKVLNHF PAFSHITAQV VYVISLCGML AICVRLIRKG
PFRLFEGCSY SYMLCISEIL ALILGDGLAL SLTIVLSVLF ISLRFIDNEY HLVLFLTLFS
SHSFFALAHQ STFTSIPWNA AFVGIPGNFI YHWIPATLII MHVFASQILY SFSLPLFVFS
IICATALHRR HLMMWKVFAP KFIFESLSLC IINITVVLTC CIFRNISFIK
//