ID A0A0C7NGB4_9SACH Unreviewed; 817 AA.
AC A0A0C7NGB4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830, ECO:0000256|RuleBase:RU367106};
GN ORFNames=LALA0_S13e01882g {ECO:0000313|EMBL:CEP64737.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP64737.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP64737.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP64737.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the GPI second mannose.
CC {ECO:0000256|RuleBase:RU367106}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687,
CC ECO:0000256|RuleBase:RU367106}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367106}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367106}. 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, ECO:0000256|RuleBase:RU367106}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU367106}.
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DR EMBL; LN736372; CEP64737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7NGB4; -.
DR STRING; 1245769.A0A0C7NGB4; -.
DR HOGENOM; CLU_004770_0_0_1; -.
DR OrthoDB; 5479199at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000054304; 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 GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16024; GPI_EPT_2; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
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 ECO:0000256|RuleBase:RU367106};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502,
KW ECO:0000256|RuleBase:RU367106};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367106};
KW Reference proteome {ECO:0000313|Proteomes:UP000054304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367106};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367106};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367106}.
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 426..448
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 759..781
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 793..816
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT DOMAIN 392..814
FT /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19316"
SQ SEQUENCE 817 AA; 92112 MW; 030F1AE6B027C48D CRC64;
MGILSKTIGL LALQIVAILT FSAGFFPQKS FLKGDAQFLH LPEEQQDVQP RFEKLVLVVI
DALRADYLFQ DEMSQFSFVH GLLNDGHAWG YTAYSNPPTV TLPRLKGITT GSTPNFLDAI
LNVAGEDSSS SLEEQDSLLR QFRIKQKTIN FFGDETWLKL FPRHFFDVVD GTNSFFVSDF
EEVDYNVTRH LPRQLASQES WDVMILHYLG LDHIGHKGGA FSTFMRPKHR EMDAVIEQIY
NSVDDNTLIC VMGDHGMNDM GNHGGSSAGE TSSAMAFISK KLAGFSKPVA QRTEHIPIKA
KSEDYKYLTK VNQIDFVPTV ATLFNLPIPK NNIGVLIPDF LRLFSSHEAH IKVMDNFEQI
SSVAGQPCKE LGSTDAHIAM MRDIQARLAK TATKYDYKLL GIGFTLLAFA TFGVSKVCLE
SLQISVSFLI LIVVCFLLSL STFGSSFVEE EHQLWWWASV GFALISLAKA PRQTGSIFLA
SVGLRFIRGW NNSGQKYIYE HTTSELLKTH SEWQWILNVF TILGSSLVLR QQPTSSILAD
FPLSALCLVY KASWSVANGE NVPLWLQKVV SNIVPGVAND LNPTEVLKSQ LVPMARIFFS
WAIAQVFIEL MAHKREWPRR RTLIERIHPI ITLILIFQTP STNIPQFLVF QIIAPQIESL
WHQLSDSNVT ALMTVGLILQ HLTFFQFGGT NSIATVSLTN AYNGVSENYS IHAVGFLMCL
SNFAPSIYWS TTCLKMLLQR QPRVVPKKWQ FFAISRLPAL FFYCIFGCFL LGSCFILRYH
LFIWSVFSPK LCYYVSWNLF MNVVIGWTLE AVIIAMS
//
