ID   GWT1_YARLI              Reviewed;         478 AA.
AC   Q6CAW6;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=GPI-anchored wall transfer protein 1;
DE            EC=2.3.-.-;
GN   Name=GWT1; OrderedLocusNames=YALI0C23793g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382129; CAG82518.1; -; Genomic_DNA.
DR   RefSeq; XP_502196.1; XM_502196.1.
DR   AlphaFoldDB; Q6CAW6; -.
DR   STRING; 4952.CAG82518; -.
DR   EnsemblFungi; CAG82518; CAG82518; YALI0_C23793g.
DR   GeneID; 2909596; -.
DR   KEGG; yli:YALI0C23793g; -.
DR   VEuPathDB; FungiDB:YALI0_C23793g; -.
DR   HOGENOM; CLU_020802_2_2_1; -.
DR   InParanoid; Q6CAW6; -.
DR   OMA; GLYVMQP; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000001300; Chromosome C.
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..478
FT                   /note="GPI-anchored wall transfer protein 1"
FT                   /id="PRO_0000246294"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        449..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        367
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   478 AA;  53912 MW;  14B0491B677CD69B CRC64;
     MSSQKLLKEE HVSGLTGGSI GEIYVVTCVN LTAYVAWALL RKRYGDHSPW DVDFVIFDFL
     LNWLGLLLSV TIYSNQPLLL NALIIVPAGV WYIWGRRDRV KKRKELRPDF QQEKDKEVKR
     ADKEMPFLSV YRGSMMVITC IAILAVDFNI FPRRFAKVET WGTSMMDLGV GSFVFSMGVV
     SKPRTDEPFG PQMKKSLKHA FPVLVLGFIR LISVKSLDYQ EHVSEYGVHW NFFFTLGFLP
     PFVTLVGGLF KKTKIPLMGQ SVIIALAYDV LLSVTSLKEY ILTAPRVDIF SQNKEGIFSF
     IGYLAIFLAG QAVGTVILRT KLPEPTPANS KRTPHNLRYR QIIKYLTISS ILFHVARLYY
     DGTIEINVSR RLVNMPYYLW VCAYNTFFLG CYAAIEVILV PIRASQPATP RVPLTLDAVN
     YNGLVIFLLA NIGTGLINMS VNTLEASPAK TMVILVAYCA ALSGISLVLY KKEIRLKL