ID A0A0N5AVC9_9BILA Unreviewed; 930 AA.
AC A0A0N5AVC9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000884501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000884501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU367138}.
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DR AlphaFoldDB; A0A0N5AVC9; -.
DR STRING; 451379.A0A0N5AVC9; -.
DR WBParaSite; SMUV_0000884501-mRNA-1; SMUV_0000884501-mRNA-1; SMUV_0000884501.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000046393; Unplaced.
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; 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; 2.
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 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 444..461
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 467..483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 504..522
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 528..550
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 562..578
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 584..603
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 615..633
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 639..656
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 668..690
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 710..733
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 785..803
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 823..848
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 860..878
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 890..907
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT DOMAIN 401..882
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
SQ SEQUENCE 930 AA; 106166 MW; B7300D5B52378D57 CRC64;
MAFNHVKLVF LGIFVHGVLL YSIFDIYYTS PLVQGTKPHP ITKGNGLAKR LVVISADGLR
SDIFFQNPNK SPFLHRIIRN NEGCWGISTS HVPTESRPGH VALLAGFYED VSAVARGWKL
NPVPFDSIIN RSQIAWAWGS PDIVPMFTKG IHHATGYVYS SDDEKFFNGD AAQLDRWVFK
NFEVYSCNYS QDFIRGDKTG KIFSDRTVFF LHLLGLDTNG HGSKPHSKNY IDNINVVDKG
IEAIVRLLDE VFNDNKTAFV FVSDHGMTDW GSHGAGTDSE ILTPFVAWGS GVDTSPFLAA
LLGVAIPMNS VGVLPHECLD ATSKYIFQSS FANFQQMSEQ FIIKRQEKKD HSFSFFFREY
NVLTPQKLFD IRTEIHRFAD LGRYEAATFT SLQWIPHIRA GLLYFHRYER SLLGLATLLT
FVFWMLLLMD IMDDIRSLYM LNRFTLGPFV IVGCLLIILR FPLSSDLYIL LPFYLGSILF
NILTKRKIEH TGYMAILLQY FDKAAVLSAS EFMIIILKIF VLSAFSGILL TALTSVFTRR
SLLSMLLIFL SFFPHVKSKT KWFWSILCFI LAIFPQLSPV GRTPSPLLCI FSPILSALLL
YFISHNEYFK LMANSFRILS LIHAFTAIVI GVTEFCRHLD WVGECFALIM LIYSFWENQM
TYIYLFQPIF SVLRILCWSS LPIAFLLPAF TPKLLIGRVI IWFSSMFVPY SLLSLSYESL
FLIIFFLFLV VYVRMSFDHL SDKSFWEMPI VKKRQLRKHQ IYVYRNVKFF ADEAVLTSMI
MWSHAVVVVI FVEVSFFGTG NIASLNSFNP SFLRCFLNVF SPFLMAGLLV FKVALPFFAI
TLALIVVLEA SGASTVKFSL ILLIITDAMA MVFFFQLVDN GSWLEIGTSI SHYVISMLTS
VIVFILLQSA QYLLSFSLLE LTVYKEYQLD
//
