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Database: UniProt
Entry: M4B4L5_HYAAE
LinkDB: M4B4L5_HYAAE
Original site: M4B4L5_HYAAE 
ID   M4B4L5_HYAAE            Unreviewed;       894 AA.
AC   M4B4L5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830};
OS   Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS   (Peronospora arabidopsidis).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Hyaloperonospora.
OX   NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP801214, ECO:0000313|Proteomes:UP000011713};
RN   [1] {ECO:0000313|Proteomes:UP000011713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX   PubMed=21148394; DOI=10.1126/science.1195203;
RA   Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA   Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA   Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA   Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA   Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA   Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA   Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA   Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA   Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA   Tyler B.M.;
RT   "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT   arabidopsidis genome.";
RL   Science 330:1549-1551(2010).
RN   [2] {ECO:0000313|EnsemblProtists:HpaP801214}
RP   IDENTIFICATION.
RC   STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP801214};
RG   EnsemblProtists;
RL   Submitted (JUN-2015) 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. PIGG subfamily.
CC       {ECO:0000256|ARBA:ARBA00005315}.
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DR   EMBL; JH598325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M4B4L5; -.
DR   STRING; 559515.M4B4L5; -.
DR   EnsemblProtists; HpaT801214; HpaP801214; HpaG801214.
DR   VEuPathDB; FungiDB:HpaG801214; -.
DR   eggNOG; KOG2125; Eukaryota.
DR   HOGENOM; CLU_004770_0_0_1; -.
DR   InParanoid; M4B4L5; -.
DR   OMA; DHIGHKT; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000011713; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:InterPro.
DR   CDD; cd16024; GPI_EPT_2; 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; IPR037674; PIG-G_N.
DR   InterPro; IPR039527; PIGG/GPI7.
DR   InterPro; IPR045687; PIGG/GPI7_C.
DR   PANTHER; PTHR23072:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 2; 1.
DR   PANTHER; PTHR23072; PHOSPHATIDYLINOSITOL GLYCAN-RELATED; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   Pfam; PF19316; PIGO_PIGG; 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   Reference proteome {ECO:0000313|Proteomes:UP000011713};
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   TRANSMEM        464..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        497..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        528..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        558..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        620..639
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        651..675
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        701..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        775..794
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        814..836
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          705..843
FT                   /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19316"
SQ   SEQUENCE   894 AA;  97960 MW;  FFC325500A15ADB0 CRC64;
     MTSPFRLRLL CLSAGVGAYL SASGLLRLHE VFSLSSSPPL NPQEHTKQQQ DTDNCLDVAY
     DRLVVVLIDA LRADMVLGSG AMRKDQEVNG YDGKEELNVY MPFTRALVTS GSALGYVAHA
     SVPTVTMPRV KALVTGKAPV FIDILKNFNS GALEEDANLV SLMATSGKRV VFYGDDTWLK
     LFPTTFARAE GTSGFYTRDT VDVDNNVTRH LTEELDPTMR HAKSGDWDVL VLHYLGLDHV
     GHLRGPRSKL MQEKMQEMDR VMQLVVDSVR EQDAWRKKKD GSARPSLILL CSDHGMSEVG
     NHGGATLEES SALLVFMRGD GEPMLSSADV AYKQQRSQVD LVPTISLLFG LPIPFYSTGL
     LLDDVVRASS GSVVRHSSYY VRALYRNFQQ LYALAKTKFP ASALASFDQQ FEAPIRQLHK
     GLQLDEKYFE IDHQMTAMVL RACMILRAKV AQSDGSEYNM TATFSGLLLL FASSVFATAI
     LIAHYQVDVK SRTNRSTSNH LFFAVVGVGS VLQIASLSSS SSIENEHATA FFMTTSLLVN
     VAVRLLRQEN LAPNSARPSA AVAIVGLLLI VTRMLRARNQ VINFWRLNGL VIDPNLPGNE
     FAKDDSVSIL STAPMLPSSI LPLGVCIAFV CGIVLRKTAR HAMRALRTGA LLQFVVGASS
     GVLFVAGMLA CLAVKELSNL IITDETGSRA WTWWMPLDAD ASALVVYGSI ALISVFAVLA
     ARTLRLSLVE MIVWLLVCLL QRDANYPTLC LLCLQLELVA MLLEYESGRG IRHTGITVAG
     LASWLSQAAF FALGNSHLVT TIDISQSYHG LSSYSQSLVG ILTFVSVFSG PLLCFVQLAQ
     WLRITVPGKA SAKFTGLLIL DYPRSTNTRW TTCLALFTYQ TLRFAVYSVF APKV
//
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