GWT1_ASPFU
ID GWT1_ASPFU Reviewed; 501 AA.
AC Q873N1; Q4WRW4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=GPI-anchored wall transfer protein 1;
DE EC=2.3.-.-;
GN Name=gwt1; ORFNames=AFUA_1G14870;
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 [GENOMIC DNA].
RX PubMed=12753194; DOI=10.1046/j.1365-2958.2003.03481.x;
RA Tsukahara K., Hata K., Nakamoto K., Sagane K., Watanabe N.-A.,
RA Kuromitsu J., Kai J., Tsuchiya M., Ohba F., Jigami Y., Yoshimatsu K.,
RA Nagasu T.;
RT "Medicinal genetics approach towards identifying the molecular target of a
RT novel inhibitor of fungal cell wall assembly.";
RL Mol. Microbiol. 48:1029-1042(2003).
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: Probable acetyltransferase, which acetylates the inositol
CC ring of phosphatidylinositol during biosynthesis of GPI-anchor.
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 PIGW family. {ECO:0000305}.
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DR EMBL; AB092482; BAC66175.1; -; Genomic_DNA.
DR EMBL; AAHF01000004; EAL90818.1; -; Genomic_DNA.
DR RefSeq; XP_752856.1; XM_747763.1.
DR AlphaFoldDB; Q873N1; -.
DR STRING; 746128.CADAFUBP00001412; -.
DR EnsemblFungi; EAL90818; EAL90818; AFUA_1G14870.
DR GeneID; 3509879; -.
DR KEGG; afm:AFUA_1G14870; -.
DR VEuPathDB; FungiDB:Afu1g14870; -.
DR eggNOG; KOG0411; Eukaryota.
DR HOGENOM; CLU_020802_2_2_1; -.
DR InParanoid; Q873N1; -.
DR OMA; GLYVMQP; -.
DR OrthoDB; 1202772at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032216; F:glucosaminyl-phosphatidylinositol O-acyltransferase activity; IMP:AspGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:AspGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR InterPro; IPR009447; PIGW/GWT1.
DR PANTHER; PTHR20661; PTHR20661; 1.
DR Pfam; PF06423; GWT1; 1.
DR PIRSF; PIRSF017321; GWT1; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..501
FT /note="GPI-anchored wall transfer protein 1"
FT /id="PRO_0000215183"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 101..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 197
FT /note="I -> T (in Ref. 1; BAC66175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 54677 MW; 819B70CB2DB1585D CRC64;
MDPDYKARKE AFVSGLAGGS ILEINAVTLV ASVSVFLWSI LQSRLSFFTP YSAAALLVDF
LLNVLAILFA TTLYSSAPLL LNLLLISPAL LILLSTKRPR TPVKAKPPRQ SARAGKDDSK
HATALPESLP IHPFLTTYRA AMMVITCIAI LAVDFRIFPR RFAKVENWGT SLMDLGVGSF
VFSGGVVSAR SLLKSRINGS KRLPLAKRLI ASTRHSIPLL VLGLIRLYSV KGLDYAEHVT
EYGVHWNFFF TLGLLPPFVE VFDALATIIP SYEVLSVGIA VLYQVALEST DLKSYILVSP
RGPSLLSKNR EGVFSFSGYL AIFLAGRAIG IRIIPRGTSF SRSPEQARRR VLISLGVQAL
VWTTLFVLNS TYAMGYGANI PVSRRLANMP YVLWVSAFNT AQLFVFCLIE TLCFPAVHRT
TTQESESERV DFATSRIMSA FNKNSLAIFL LANLLTGAVN LSISTIDANT AQAIAVLIGY
SSIITGVALA LHHANIKVLP F
