ID A0A0F8VPG9_9EURO Unreviewed; 859 AA.
AC A0A0F8VPG9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-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=ARAM_003137 {ECO:0000313|EMBL:KKK25071.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK25071.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK25071.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK25071.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) 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: 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:KKK25071.1}.
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; JZBS01000835; KKK25071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8VPG9; -.
DR STRING; 308745.A0A0F8VPG9; -.
DR OrthoDB; 5479199at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000034291; 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; 1.
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:UP000034291};
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 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 442..460
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 498..515
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 527..546
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 578..596
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 603..624
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 648..670
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 691..712
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 732..751
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 763..783
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 803..826
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 838..856
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT DOMAIN 435..857
FT /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19316"
SQ SEQUENCE 859 AA; 95306 MW; 258723FBE172D65F CRC64;
MAIKPAIWPV LLANILIPIS ILIFSLGFFP YKPLIPGLAT FEEARNAPAP IFNKVVFMVV
DALRSDFVYS DKSGFLFTQG LIRSGAAVPF TAYAGSPTVT MPRLKALTTG SVPSFLDVIL
NIAESDTSST LAFQDTWLAQ IKRRGEKLIM YGDDTWLKLF PGMFSRADGT TSFFVSDFTE
VDTNVTRHIP HELLQDDWSA LIMHYLGLDH IGHKAGPQSP YMITKQREMD AIVSQVYEAM
NQEAHLESTL FVVCGDHGMN DAGNHGGSSV GETSPALLFI SPKFQTIEGM RQSPIAAFKD
MQYYRVVDQT DITPTLAGLL GLPIPLNSLG VFIPELLDLW HSGSQRIQLL IENSKQLLDT
VKEAYPGFSV DRDAMEAGCN SKSQTSVEET RCAWFHAQEL LRQFDADNGS ASQSEVESSL
LHFLKTSQSL MSSAASNYNL KYLSLGIFVS GLAVLFALPA SYRVLSGEKH AGLFFALSIL
SYGALMFASS YVEEEQQFWY WIFTGWAFYL HIRSSRRLTE RHSKGRGTYG ALATLFPKFS
PVILAVSHRI LRRWNQTGQK FAADPDISRT FFPNHPGSLW VLVALSYADI SLHIIGHTSS
SMAWRLLCFG VTTLAFTFKL VFAASESPEL ISKPVLHNVT VLLNQVPLLL YARLVLGGIM
LLVVFSTISA RQNKRPTKQR VSPSAVFHEA LALFLMTQSR VTNVPLFLIL RVQLKALASM
DLSPNEVTVT SLFMQYITFF AFGGSNAISS VDLSNAYNGV GNYNIVLVGI LTFAGNWAGP
IWWVSATKLL RSSQSGDEKR SHFTLLTFST AATLLSVMAA CTALRTHLFI WTVFSPKYLY
TISWAIIHHF GVNLLWEIF
//
