ID W2LQR0_PHYPR Unreviewed; 997 AA.
AC W2LQR0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=GPI ethanolamine phosphate transferase 1 {ECO:0000256|ARBA:ARBA00020831, ECO:0000256|RuleBase:RU367138};
DE EC=2.-.-.- {ECO:0000256|RuleBase:RU367138};
DE Flags: Fragment;
GN ORFNames=L917_03451 {ECO:0000313|EMBL:ETL99736.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL99736.1};
RN [1] {ECO:0000313|EMBL:ETL99736.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL99736.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the first alpha-1,4-linked mannose of the
CC glycosylphosphatidylinositol precursor of GPI-anchor.
CC {ECO:0000256|RuleBase:RU367138}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687,
CC ECO:0000256|RuleBase:RU367138}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367138}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
CC {ECO:0000256|ARBA:ARBA00008400, ECO:0000256|RuleBase:RU367138}.
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DR EMBL; KI678243; ETL99736.1; -; Genomic_DNA.
DR AlphaFoldDB; W2LQR0; -.
DR EnsemblProtists; ETL99736; ETL99736; L917_03451.
DR VEuPathDB; FungiDB:PPTG_08539; -.
DR UniPathway; UPA00196; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd16020; GPI_EPT_1; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007070; GPI_EtnP_transferase_1.
DR InterPro; IPR017852; GPI_EtnP_transferase_1_C.
DR InterPro; IPR037671; PIGN_N.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR12250:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 1; 1.
DR PANTHER; PTHR12250; PHOSPHATIDYLINOSITOL GLYCAN, CLASS N; 1.
DR Pfam; PF04987; PigN; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367138};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502,
KW ECO:0000256|RuleBase:RU367138};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367138};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367138};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367138};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367138}.
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 487..508
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 528..545
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 591..609
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 615..631
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 668..686
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 804..820
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 840..862
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 874..902
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 923..942
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 954..979
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT DOMAIN 241..317
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT DOMAIN 478..947
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETL99736.1"
SQ SEQUENCE 997 AA; 111235 MW; 17292CB016562FAF CRC64;
GQNSPDVMTK AGGGLAQLLV LGVLFHALYV LSIFDIYFTS PVVPHIESVI YTDSPPAKRV
VVFVADGCRA DKFFETNTSS NARDSNAELR VSFLRNMMQT HGSWGVSHTR VPTESRPGHV
ALFAGMYEDV SAVTKGWADN PVDFDSVFNQ SSSAFLFGSP DIVPMFARHV SQAHEEHYSH
EEEDFAKGDA SELDVWVFRH LQNLLIGAKE DTNLYTKLHS DGVVVFCHYL GIDSNGHAHR
PNSKDYLNNI ALVDELVEKT HRMVEDFYGY DGRTAYVFTA DHGMGLKGAH GDGDPANTRT
PLVVWGAGVQ GPTTVEKKGE FEIDLPTQSR AQVKAQLQAQ EEQEQAAVGD WGALKNLVRK
DVMQADVAPL ISALLGLPYP RNSVGVLPFS YLAKGAYRAN AVRSNAQQLY LHALRKEQEK
RSRTLLRFAP YGPFRDRVPE LLKQLAEAYE TSIQGDNSES YERVEVLSQE LIEICLATLE
YFQRYDWFFL LGIVVLGYVG WMVVVGVAYL HPRDFALKWL LGAHGKQLDI KLIVVVFAAF
VYLALEGSPI TYYLYLLFPL VFGVFTWNHI DLIQQAWVSG SSNKSKSHWK RWAEIALIVL
CLELVVFGYE RRGVFGVLFS LLAFWPYVGN ATNDENQSGR STLPSRCWTI SCLLISVFPY
LPSEYGEHTA LVNIGGLLTL LFTSAVQSTS NQTSWKRPSF MLSVSPLILS LMTLHGTMQY
LDGDRSKPPF SLTVANWLLS GAPIVLLIAR LQRRKSSLSR ILETGTHRHE DGFQTDTEFY
VRRLIEVVLA FSPSFVLLSI AYEVLFYVVL CAVLVSWLLL EAQASEASTS SMWREIQRAF
VFLLLVNIAF FGTGNVASMS SFEISSTYRF VTVFAPFTMG ALLVGKILIP FMVVACTFHL
ILLLPSASAS ADAKKPRLPA TRYFLLVVAM SDVLALHFLF LVKNEGSWKE IGNSISMFGI
VNAQIVFIPL LFLLAGAFVR DLAKVTDAQV FHDKKHQ
//