GenomeNet

Database: UniProt
Entry: W2LQR0_PHYPR
LinkDB: W2LQR0_PHYPR
Original site: W2LQR0_PHYPR 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system