ID A0A0D9S006_CHLSB Unreviewed; 931 AA.
AC A0A0D9S006;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=PIGN {ECO:0000313|Ensembl:ENSCSAP00000014195.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014195.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000014195.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000014195.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; AQIB01127725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01127726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008012067.1; XM_008013876.1.
DR RefSeq; XP_008012068.1; XM_008013877.1.
DR AlphaFoldDB; A0A0D9S006; -.
DR STRING; 60711.ENSCSAP00000014195; -.
DR Ensembl; ENSCSAT00000016275.1; ENSCSAP00000014195.1; ENSCSAG00000018179.1.
DR GeneID; 103244175; -.
DR CTD; 23556; -.
DR eggNOG; KOG2124; Eukaryota.
DR GeneTree; ENSGT00390000017600; -.
DR OMA; QSYFHRE; -.
DR OrthoDB; 6598at2759; -.
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 103244175; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 18.
DR Bgee; ENSCSAG00000018179; Expressed in liver and 7 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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:UP000029965};
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 441..463
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 483..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 544..564
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 570..586
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 593..611
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 617..638
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 680..701
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 730..746
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 787..805
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 825..848
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 860..880
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 892..912
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT DOMAIN 430..884
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
SQ SEQUENCE 931 AA; 105769 MW; 492544E3D4CEC325 CRC64;
MLLFFILGLL IHFVFFASIF DIYFTSPLVH GMTPQFTPLP PPARRLVLFV ADGLRADTLY
ELDENGTSRA PFIRNIIMHE GSWGISHTRV PTESRPGHVA LIAGFYEDVS AVAKGWKENP
VEFDSLFNES KYTWSWGSPD ILPMFAKGAS GDHVYTYSYD AKREDFGAQD ATKLDTWVFD
NVKDFFRHAR NNQSLFSKIN EEKIVFFLHL LGIDTNGHAH RPSSRDYKDN IKKVDDGVKE
IVSMFNHFYG NDGKTTFIFT SDHGMTDWGS HGAGHPSETL TPLVTWGAGI NYPQRVSAQQ
FDDSFLKEWR LENWKRLDVN QADIAPLMTS LIGVPFPLNS VGILPVDYLN NTDLFKAESM
FTNAVQILEQ FKVKMTQKKE VTLPFLFTPF KLLSDSKQFN ILRKARSYIK HRKFDKVVSL
CKELIHLALK GLAYYHTYDR FFLGINVVTG FVGWISYASL LIIKSHSNLI KGVSKEVKKP
SHLLPCSFVA IGILVAFFLL IQACPWTYYV YGLLPVPIWY AVLREFQVVQ DLVTSLLTYP
LSHFVGYLLV FTLGIEVLVL SFFYRYMLTA GLTAFAVWPF LTRLWTRAKV TSLSWAFFSV
LLAVFPLMPV VGRKPDISLV MGAGLLVLLL SLCVVTSLMK RKDSFRKEEL LVHLLQVLST
VLSMYVVYST QSSLLRKQGL PLMNQIISWA TLASSLVVPL LSSPAVFQRL FSILLSLMST
YLLLSTGYEA VFPLVLSCLM FVWINIEQET LQQSGVCYKQ KLTSIQFSYN TDITQFRQLY
LDDIRRAFFL VFFLVTAFFG TGNIASINSF DLASVYCFLT VFSPFMMGAL MMWKILIPFV
LVMCAFEAVQ LTTQLSSKSL FLIVLVISDI MALHFFFLVK DYGSWLDIGT SISHYVIVMS
MTIFLVFLNG LAQLLTTKKL SLCGKPKSHF M
//
