ID   GWT1_ASPOR              Reviewed;         500 AA.
AC   Q2UQH4;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=GPI-anchored wall transfer protein 1;
DE            EC=2.3.-.-;
GN   Name=gwt1; ORFNames=AO090005001245;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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; AP007151; BAE56191.1; -; Genomic_DNA.
DR   RefSeq; XP_001818193.1; XM_001818141.1.
DR   AlphaFoldDB; Q2UQH4; -.
DR   STRING; 510516.Q2UQH4; -.
DR   EnsemblFungi; BAE56191; BAE56191; AO090005001245.
DR   GeneID; 5990138; -.
DR   KEGG; aor:AO090005001245; -.
DR   VEuPathDB; FungiDB:AO090005001245; -.
DR   HOGENOM; CLU_020802_2_2_1; -.
DR   OMA; GLYVMQP; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000006564; 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; IEA:EnsemblFungi.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
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..500
FT                   /note="GPI-anchored wall transfer protein 1"
FT                   /id="PRO_0000246286"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
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        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..368
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          100..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   500 AA;  54484 MW;  9541EE5CF9600274 CRC64;
     MDSSYKARKE AFVSNLAGGS ILEINAVTLV APTSVLLWSV LQSRLSFFIP YGALALVTDF
     FLNVLPILFA TTLYSSAPWT LNILLALPAL ILLFTSTPSR TQQKAKPPRP SAAAKKNTPK
     HASDSPEPLP VHPFLTTYRA AMMVITCVAI LAVDFRIFPR RFAKAENWGT SLMDLGVGSF
     VFSSGVVSAR SILKGRNSHS KKAGLWQRLA ASARHSIPLL VLGLVRLYSV KGLDYAEHVT
     EYGVHWNFFF TLGLLPPFVE IFDALAAIIP SYEILSLGIV VLYQVALEST DLKSYILVSP
     RGPDLLSKNR EGVFSFLGYL AIFLTGRAIG IRIIPRGTSA SRSPQQARKS VLISLGLQTL
     VWTTLFVFNS THAMGLGAGI PVSRRLANMP YVLWVSAFNN AQLFLFCLLE STFFPSIHRE
     TGKDGELERT SFATSRIMTA FNKNGLALFL VANLLTGAVN LSVPTLDVTT AHAMVVLIAY
     VAMITGVALA LDRANIKLSL