ID A0A093UW33_TALMA Unreviewed; 719 AA.
AC A0A093UW33;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830, ECO:0000256|RuleBase:RU367106};
GN ORFNames=GQ26_0510100 {ECO:0000313|EMBL:KFX41934.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX41934.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX41934.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX41934.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KFX41934.1}.
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DR EMBL; JPOX01000051; KFX41934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093UW33; -.
DR eggNOG; KOG2125; Eukaryota.
DR HOGENOM; CLU_004770_0_0_1; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000029285; 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 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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 385..407
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 413..436
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 443..464
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 512..530
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 542..561
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 588..610
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT DOMAIN 379..710
FT /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19316"
SQ SEQUENCE 719 AA; 78726 MW; 71088431494ADDB7 CRC64;
MAGALSKWTL FLANALIPVA VLLFCSGYFP YKPILSGAAE PPVWGKAPPV FDKVILMVVD
ALRSLIRTGA AWPFTAHASS PTVTMPRIKA ITTGSVPSFS DVVLNIAESE TEVRPSWEDV
DDFTEVDNNV TRHVSPELAQ DDWSVMVLHY LGLDHIGHKA GPKSSHMIPK QREMDGIVEE
IYNAMLSETH LDSTLLVLLG DHGMNEAGNH GGSSAGETSP ALTFISPKLQ KHSENSELKG
RDSPIEAENF EFYHTVEQSD ITPTLAGLLG VPIPLNSLGV FIPEFLGLWG NEVDRVTMLL
ENTVQIQNVI KMAYPKFSTN GDKINEVSSA NGTGLGSSAL ERLEYEFIAA GLSMSPDEKS
TRTHYKFLHS AQSLMSGAAS SYKLSMLYSG TLTVAFACLV SAFIAYYTLP TPLVASTVFL
FITSVLHGAM MFASSFVEEE QQFWYWITTA WTVYIHLRAT SFGLNRLSTK SIIYSISFAA
AGRIMRRWNQ TGQKFAGEPD IVQYLSSSQP KLLWALVLLT YMVNCQSMIG SAPFRNVFGK
SLWTILSIAV SFAAVVFKVS FTAADAPELL DPLILRITRW GFQTSLVFQA RLVFIGIASL
LVICVISSFT SRGVQNGRKR LFHEAITLFL ITQSRATNIP LFVLFKVQAS IIERVDLNSI
ETTLNLILMQ HVAFFAFGGS NALSSVDLST AYNGVSDYNV VVVGLLTFVT SLDSNGGNE
//
