ID A0A2J8W3G3_PONAB Unreviewed; 643 AA. AC A0A2J8W3G3; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 22-FEB-2023, entry version 16. 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=CR201_G0013503 {ECO:0000313|EMBL:PNJ64308.1}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601 {ECO:0000313|EMBL:PNJ64308.1}; RN [1] {ECO:0000313|EMBL:PNJ64308.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Susie {ECO:0000313|EMBL:PNJ64308.1}; RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M., RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J., RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M., RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B., RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.; RT "High-resolution comparative analysis of great ape genomes."; RL Submitted (DEC-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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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:PNJ64308.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NDHI03003401; PNJ64308.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2J8W3G3; -. DR UniPathway; UPA00196; -. 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-UniRule. DR CDD; cd16020; GPI_EPT_1; 1. DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2. 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 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 462..484 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367138" FT TRANSMEM 504..521 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367138" FT TRANSMEM 527..544 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367138" FT TRANSMEM 553..572 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367138" FT TRANSMEM 584..602 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367138" FT TRANSMEM 614..633 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367138" FT DOMAIN 451..642 FT /note="GPI ethanolamine phosphate transferase 1 C-terminal" FT /evidence="ECO:0000259|Pfam:PF04987" SQ SEQUENCE 643 AA; 73396 MW; DF070ED0E697CAA3 CRC64; MLLFFTLGLL IHFVFFASIF DIYFTSPLVH GMTPQFTPLP PPARRLVLFV ADGLRADALY KLDENGNSRA PFIRNIIMHE GSWGISHTRV PTESRPGHVA LIAGFYEDVS AVAKGWKENP VEFDSLFNES KYTWSWGSPD ILPMFAKGAS GDHVYTYSYD AKREDFGAQD ATKLDMWVFD NVKRKQLTHY LNIDVCTDSK DVVLDFFHRA RNNQSLFSKI NEEKIVFFLH LLGIDTNGHA HRPSSRDYKD NIKKVDDGVK EIVSMFNHFY GNDGKTTFIF TSDHGMTDWG SHGAGHPSET LTPLVTWGAG IKYPQRVLAQ QFDDAFLKEW RLENWKRLDV NQADIAPLMT SLIGVPFPLN SVGILPVDYL NNTDLFKAES MFTNAVQILE QFKVKMTQKK EVTLPFLFTP FKLLSDSKQF NILRKARSYI KHRKFDKVVS LCKELIHLAL KGLSYYHTYD RFFLGVNVVI GFVGWISYAS LLIIKSHSNL IKGVSKEVKK PSHLLPCSFV AIGILVAFFL LIQACPWTYY VYGLLPVPIW YAVLREFQVI QDLVASVLTY PLSHFVGYLL AFTLGIEVLV LSFFYRYMLT AGLTAFAAWP FLTRLWTRAK VTSLSWTFFS LLLAVFPLMP VVGRKPDISL VYE //