ID A0A0D2AGQ2_9PEZI Unreviewed; 1001 AA.
AC A0A0D2AGQ2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=GPI ethanolamine phosphate transferase 1 {ECO:0000256|ARBA:ARBA00020831, ECO:0000256|RuleBase:RU367138};
DE EC=2.-.-.- {ECO:0000256|RuleBase:RU367138};
GN ORFNames=PV09_03267 {ECO:0000313|EMBL:KIW06098.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW06098.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW06098.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW06098.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) 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|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; KN847536; KIW06098.1; -; Genomic_DNA.
DR RefSeq; XP_016215967.1; XM_016356444.1.
DR AlphaFoldDB; A0A0D2AGQ2; -.
DR STRING; 253628.A0A0D2AGQ2; -.
DR GeneID; 27311240; -.
DR VEuPathDB; FungiDB:PV09_03267; -.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; A0A0D2AGQ2; -.
DR OrthoDB; 6598at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000053259; Unassembled WGS sequence.
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 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:UP000053259};
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 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 458..483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 495..514
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 520..538
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 586..603
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 610..632
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 638..657
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 678..701
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 713..731
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 738..755
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 844..863
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 883..906
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 918..937
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 949..969
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT DOMAIN 448..942
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
SQ SEQUENCE 1001 AA; 110543 MW; 3BB9027267B03C63 CRC64;
MARLGRLGFL AVAVVFHFTY IYSIFDIYFV SPIVGGMREF SVPGEAPARR LVLYVGDGLR
ADKCFQSFPD PSPSKNDTDA LTPRPLTPFL RNKVLKEGTF GVSHTRVPTE SRPGHVALIA
GLYEDVSAVT TGWKLNPVNF DSVFNKSRHT WSWGSPDILP MFEKGAVPGR VDAFTYGAEY
EDFTSNAVEL DIWVFDRVKA LFEEAKTNPD LDAQLRQDKI VFFLHLLGLD TTGHGFRPYS
KEYLHNIKIV DQGVKEITEL IDNFYNDGKT AYVFTADHGM SDWGSHGDGH PDNTRTPLIT
WGSGIAKPVK KMLGTAPGHE DGFSADWGLS NIQRHDVAQA DVAALMAYLI GVPFPVNSVG
ELPLSYLAAS PKVKAEALLT NAKGILEMYK VKEAEKKATK LRYRPFSGFG DETHSIEYRI
AQIETSIEKN RASDAIAQCK ELIHLGLQGL RYLQTYDWLF LRALVTLGYL GWIVYAVTLV
IDLHVLQGST EPQRTVVSNM GFSSALVALF SLLFVQKSPI TYYIYAVFPV FFWEEVFARR
NAISRGKDIL FGSTSTKSSP AGSLLKFLGF LALLEVLVQS YHHRELYTIC YLLAIAWPAF
YGTEFCKKHA ILVLTWMTSC ASMSVFTLLP AMKVENPTLI FSAGVLMGAI GVMYLVFEDR
IVNQLEGVTV EQSPFARTIF GLQIGLVFLS MVVTRSGISS ISAKQGLPIG TQIVGWLTLI
ASLTVPFLHG IEPNSHYIHR LMVIFLTFSP LFIILTISYE GYFYIAFCVT LVTWVRLEHA
IYVHTTKAAI QKTHVVKGKS NGQPSPSGRA GLTPVKQTSV TAQDQHQAVS TGQHRPLTLA
DARVALFSLF LLQSAFFSTG NIASVSSFSL DAVYRLIPVF DPWSQGALLM FKIFVPFVVL
SANLGILNHR LGVAPSALFM IVMAIGDVLT LSFFWMVRDE GSWLDIGTSI SHFCIGSGLC
VFVSGLEVVS EVFVKGVEFG DDRPGVELVG NGTTGNDKKA N
//
