ID G8Y500_PICSO Unreviewed; 999 AA.
AC G8Y500;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=GPI ethanolamine phosphate transferase 1 {ECO:0000256|ARBA:ARBA00020831, ECO:0000256|RuleBase:RU367138};
DE EC=2.-.-.- {ECO:0000256|RuleBase:RU367138};
GN Name=Piso0_005396 {ECO:0000313|EMBL:CCE85768.1};
GN ORFNames=GNLVRS01_PISO0M13850g {ECO:0000313|EMBL:CCE85768.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE85768.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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|ARBA:ARBA00024850, 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; FO082047; CCE85768.1; -; Genomic_DNA.
DR AlphaFoldDB; G8Y500; -.
DR STRING; 559304.G8Y500; -.
DR eggNOG; KOG2124; Eukaryota.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; G8Y500; -.
DR OMA; HIMLTTS; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000005222; Chromosome M.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037671; PIGN_N.
DR PANTHER; PTHR12250:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 1; 1.
DR PANTHER; PTHR12250; PHOSPHATIDYLINOSITOL GLYCAN, CLASS N; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF04987; PigN; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
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 Reference proteome {ECO:0000313|Proteomes:UP000005222};
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 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 479..501
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 513..532
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 649..670
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 715..732
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 744..760
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 806..832
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 852..875
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 887..907
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 919..943
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT DOMAIN 463..911
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
FT REGION 960..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 999 AA; 112847 MW; 7EB5CEA2E92CB584 CRC64;
MNRNRYFLLV LGVLFHVFYL WSIFDIYFVS PLVHGMRPYK STDVAPAKRL FLIVGDGVRA
DTAFQKLVHP KTGESKYLMP FIRSIVNEKG SWGISNTRMP TESRPGHVAM IAGFYEDVSA
VTKGWKENPV DFDSFLNQAK HTYSFGSPDI LPMFAYGKSV EPGKVDMFMY GHEFEDFTQS
SIELDAFVFN KLDALFKNST VNETLDKEIR QDGNAFFLHL LGPDTAGHSY RPYSVEYHNN
VEYIDKQVSK LVEQVNAFFG DEDTAFVFTA DHGMSDFGSH GDGHPNNTRT PLVAWGPGIS
KPVLLSELEN ESLQREIQDP VKSGFEKDYF NTWDFDHLQR NDVNQADIAS LMSYLIGANY
PANAVGKVPI KFLNASSLTK VKALYSNALT IVEQYIVKEQ EIRDVQLKYK PFPLFDVKPI
SAYDREIGQL ILKIAEADNE NEAKLLEEQA TIVTDELIEA SLKGLNYLQT YNWSLLRSIV
VLGFLGWILY SFIIFLKLFI IPEHLLEAPK NLLLLKVSAI ASFLVFVVLF LYQRSPLNYH
IYTIFPHYFW YSIIDDFSNL KLGINRFLLG VNNTLRFFIL IAFVGVYEGI VYGFFERYCF
SIISFLIGTY PFFVQPPKST TLQKLAWLGS CLIMSVFTDL DPIKTESLFQ INLGAFLALL
LAAVSSSFIF RRGINSYNRA LGVAQVLVSV LTLYATNMSV SSLQARKGLP LYSQIIGWVC
LVLSLLVIPS LYAIDPSSDY QHRLFVIFLT FIPTFIILTI SYELLFYVGF SLILLQWLIL
EQGFSANSGE HQETSTLKDK DIPKGYWLQV IRVAIIGFFF MQLAFFGTGN IASISSFSLD
SVYRLIPIFD PFPMGALLMV KLIIPYILLS SCLGIMNLQL GIKKFTISTL IISTSDYLSL
NFFFLVRTEG SWLDIGISIS NYCLAILSSL FMLILEIVSS VLLRGVQLLS KVSYDNVTDS
PETGQNGTLE NGDLPANVSE SPISSRVKRR TRASKLSSS
//
