ID   GWT1_ASHGO              Reviewed;         480 AA.
AC   Q754I2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=GPI-anchored wall transfer protein 1;
DE            EC=2.3.-.-;
GN   Name=GWT1; OrderedLocusNames=AFR094C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53465.1; -; Genomic_DNA.
DR   RefSeq; NP_985641.1; NM_210995.1.
DR   AlphaFoldDB; Q754I2; -.
DR   STRING; 33169.AAS53465; -.
DR   PRIDE; Q754I2; -.
DR   EnsemblFungi; AAS53465; AAS53465; AGOS_AFR094C.
DR   GeneID; 4621884; -.
DR   KEGG; ago:AGOS_AFR094C; -.
DR   eggNOG; KOG0411; Eukaryota.
DR   HOGENOM; CLU_020802_2_2_1; -.
DR   InParanoid; Q754I2; -.
DR   OMA; GLYVMQP; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000591; Chromosome VI.
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; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
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..480
FT                   /note="GPI-anchored wall transfer protein 1"
FT                   /id="PRO_0000246285"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        450..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   480 AA;  53572 MW;  571C917B0FFBBFF1 CRC64;
     MNALKERKEA FVSGLEGGSI AEINLVTTVA LTAYFGWQLL NRRLDSVPLV VDFLLNWAGL
     LLSITVYAND PVLLNLLIAV PCIVQLQILG RSSQRKTQPQ KGKESARLGL DRKPFITAYR
     GGMLIITCLA ILAVDFPVFP RRFAKVETWG TSLMDLGVGS FVFSNGLVAA SALLKQEISG
     QRPPLWSRLV SSVRSAGILL ALGVARLVSV KGLEYQEHVT EYGTSWNFFF TLALVPLAMI
     LVDPICTYVP RVFIALLLSV FSEYLLQKEG FLQFMIMSKR DNFFNSNREG ILSFLGYCAI
     FLLGQNTGFY VLGNRPTVNN LYRPSGQSWQ QNRRQRLSAW DKWTSVTPLA GLLAWFFITV
     ALFQLTMAYH PYTVSRRFAN LPYVLWVAAY NLGFLSMYCM VDSLFNLSQH SNNVPVTLDA
     VNSNGLFVFL LANCLTGLIN MNMNTLDSTL TVQIAALFGY ATVIASVAII MYKCRIFIKL