ID A0A1R1PLU6_ZANCU Unreviewed; 1016 AA.
AC A0A1R1PLU6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=AX774_g4605 {ECO:0000313|EMBL:OMH81934.1};
OS Zancudomyces culisetae (Gut fungus) (Smittium culisetae).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Zancudomyces.
OX NCBI_TaxID=1213189 {ECO:0000313|EMBL:OMH81934.1, ECO:0000313|Proteomes:UP000188320};
RN [1] {ECO:0000313|Proteomes:UP000188320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL-18-3 {ECO:0000313|Proteomes:UP000188320};
RA Wang Y., White M., Kvist S., Moncalvo J.-M.;
RL Submitted (JAN-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMH81934.1}.
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DR EMBL; LSSK01000779; OMH81934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1PLU6; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000188320; 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; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000188320};
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 384..401
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 506..523
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 585..604
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 611..628
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 634..655
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 703..722
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 734..753
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 765..784
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 868..887
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 907..931
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 940..959
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 979..1004
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT DOMAIN 153..265
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT DOMAIN 363..416
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
FT DOMAIN 486..966
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
SQ SEQUENCE 1016 AA; 115307 MW; 0F40ACDEC427B54F CRC64;
MRKLIETEAT FGVSHTRVPT ESRPGHVALI AGFYEDVSAV TKGWKMNPVK FDSLINQTRY
TWSFGSPDIL PMFAEGATDK TKVETIMYGA ESEDFGGAAW HLDEFVYLKV KEMFETAKVD
GGLRDKLNKD KIVIFMHMLG LDTNGHAFRP TSREYLDNIG YVDKIVQDTV KMVDEFYGHD
GKTTYVFSAD HGMEDHGVHG DGHPDNTRTP LVAWGAGINK PVKGGRGGER AKGHDEFSEN
WGLDQYERND VNQADIAPLM SSMLGIPLPM NSVGKIPLSY LSGTDEFKAQ ALYANARQIA
EQFKTKEREK KKYRLSFVPF EASTSAGGGG IDTHLLRISQ RLLMREYKEA ISLSEEVIQL
GLDGLSYYQK YDWILLKTVI TLGYLGWMAF SAIFIIENYV LQGKASREIK RIREEDKREK
DEKQREKEKK RTGKKKWTVS VVDYFVGEED YLPSKEILEQ QAKDRLEEDK KKGRIRLEQW
GLFEYVMVIS VFVVLSLLLY VQNLPYIYYA YIAFPYYFWI ASCKQLSELF QLTDTSLNFK
AQFKDLTANL ATGVSNRFGQ TIPMLVTVIA LEMLVYTYYE RRVYTVILLL MGFSWPFVIP
KSVIRQEWKT VASFTFFCCA TSVFTLLPVK MAENQFLCLV GGFLITGFGV FAMFFTDSII
AEVSGFDSSL SSNSSSKSSS KPTARYTTAI PGLEPSKSMY DRYLLAFQSF LVFAATLVVY
STSCSLQQRK GLPLFNQILA WLLFAVSILP IIVFPRASRY LNQHFICRLF NLFLAFAVPM
VLLTISFESL FYFCFFGLMM SLLILEQIMY RVKNASILSL PLSYIPISAI SASTSTSTST
STHLSAKNST ISSDRNTYRP ISYSDLRISI MFLMFINLAF FGTGNLASIS SFYLESVYRL
ITTFSPFFMT FLLLLKIFIP FLLVSSIFVV LNTMRNLPDF CLFLLALSTT DLMTLNFFFN
VRDEGSWLDI GTSISHFCIS SLSVLFSTVL FVISYWGLIG NALVPVSSVR KHFKSN
//
