GPI7_ASPFU
ID GPI7_ASPFU Reviewed; 767 AA.
AC Q4WDM5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=GPI ethanolamine phosphate transferase 2;
DE EC=2.-.-.-;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 7;
GN Name=las21; Synonyms=gpi7; ORFNames=AFUA_6G05260;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=YJ-407;
RA Ouyang H., Jin C.;
RT "Phosphoethanolamine transferases gene, Afpig7, which is involved in the
RT biosynthesis of glycosylphosphatidylinositol in Aspergillus fumigatus
RT YJ407.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the GPI second mannose (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ426544; ABD84045.1; -; mRNA.
DR EMBL; AAHF01000012; EAL85513.1; -; Genomic_DNA.
DR RefSeq; XP_747551.1; XM_742458.1.
DR AlphaFoldDB; Q4WDM5; -.
DR SMR; Q4WDM5; -.
DR STRING; 746128.CADAFUBP00009039; -.
DR PRIDE; Q4WDM5; -.
DR EnsemblFungi; EAL85513; EAL85513; AFUA_6G05260.
DR GeneID; 3504993; -.
DR KEGG; afm:AFUA_6G05260; -.
DR VEuPathDB; FungiDB:Afu6g05260; -.
DR eggNOG; KOG2125; Eukaryota.
DR HOGENOM; CLU_004770_0_0_1; -.
DR InParanoid; Q4WDM5; -.
DR OMA; HIGHKTG; -.
DR OrthoDB; 848878at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0051267; F:CP2 mannose-ethanolamine phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR CDD; cd16024; GPI_EPT_2; 1.
DR Gene3D; 3.40.720.10; -; 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; PTHR23072; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF19316; PIGO_PIGG; 2.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..767
FT /note="GPI ethanolamine phosphate transferase 2"
FT /id="PRO_0000246187"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..715
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 733..755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 767 AA; 85692 MW; 0039F215C57EDA68 CRC64;
MAFKGEHRAI LIANILIVVA ISIFSSGFFP YKSLLPGLAT FAETNIGTVA PKVFDRVIFM
VIDALRSDFV YSKTSGFSFT QSLIRSGAAL PFTAHASSPT VTMPRLKAMT TGSVPSFLDV
ILNIAESDTS STLAYQDTWL AQIKAQGGQL VMYGDDTWIK LFPGVFDRCD GTTSFFVSDF
TEVDHNVTRH VPRELSERDW SAFIMHFLGL DHIGHKAGPK SRHMMTKQRE MDSIVALIYA
AMEEQEHLQS TLFVLCGDHG MNDAGNHGGS SPGEISPALL FISPKFQTKT TPEDSPVEAF
SDLQYYRTVE QVDITPTLAG LLGLPIPLNS LGVFIPEFLM MWDNDAHRID ILLRNAKQML
SAMKGTFPDL DVEAITPPHG CDKHVLRSAQ DVMSSTASKY NTTRLYLGLF VAALAVLLSF
FPAYGLGSKY SYAVTFLMLI IISYGGMMFA SSYVEEEQQF WYWVVTAWTV YLHIKSLRPW
HGSKDTRRWN QTGQKFAAEP DIARDFFPRH QNILWALIIL TYFDTCMHLC LNSHSSNIWR
SAAILTTIAA FFFKLVFVAS DSPELLYESL LSPIQKSLEE MPLVPPARLS KAVNIPIFLM
FRLQAIILDF LKMSAIEVTL TSLLSQNMTF FAFGGSNAIS SVDLSNAYNG IGSYSVVLVG
VLTFISNWAG PIWWASAARL LYSNPTFAER YGQRTLLTFH AATSLMSVMA ACTMLRTHLF
IWTVFSPKYL YTLAWTILNH MFINLPATAN VSQVLNWQYA FHSVACR
