ID A0A2K5NYU2_CERAT Unreviewed; 936 AA.
AC A0A2K5NYU2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:ENSCATP00000042565.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000042565.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000042565.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K5NYU2; -.
DR Ensembl; ENSCATT00000066999.1; ENSCATP00000042565.1; ENSCATG00000043851.1.
DR GeneTree; ENSGT00390000017600; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000043851; Expressed in bone marrow and 12 other cell types or tissues.
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:UP000233060};
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..879
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 885..904
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 936 AA; 106594 MW; 4DA58EC4B800AE5E CRC64;
MLLFFTLGLL 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 HRKFDEVVSL
CKELIHLALK GLSYYHTYDR FFLGINVVIG FVGWISYASL LIIKSHSNLI KGVSKEVKKP
SHLLPCSFVA IGILVAFFLL IQACPWTYYV YGLLPVPIWY AVLREFQVVQ DLVTSLLTYP
LSHFVGYLLV FTLGIEVLVL SFFYRYMLTA GLTAFAVWPF LTRLWTRAKV TSLSWAFFSV
LLAVFPLMPV VGRKPDIFLV MGAGLLVLLL SLCVVTSLMK RKDSFRKEEL LVHLLQVLST
VLSMYVVYST QSSLLRKQGL PLMNQIISWA TLASSLFVPL LSSPAVFQRL FSILLSLMST
YLLLSTGYEA VFPLVLFCLM FVWINIEQET LQQSGVCCKQ KLTSIQFSYN TDITQFRQLY
LDDIRRAFFL VFFLVTAFFG TGNIASINSF DLASVYCFLT VFSPFMMGAL MMWKILIPFV
LVMCAFEAVQ LTTQLSSKSL FLIVLVISDI MALHFFFLVK DYGSWLDIGT RQLLACTAWL
FIYISASPNR LWIPSDPELD LNLLHAIRAW HVKGTP
//
