ID   GWT1_KLULA              Reviewed;         446 AA.
AC   Q6CK18;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=GPI-anchored wall transfer protein 1;
DE            EC=2.3.-.-;
GN   Name=GWT1; OrderedLocusNames=KLLA0F14278g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98429.1; -; Genomic_DNA.
DR   RefSeq; XP_455721.1; XM_455721.1.
DR   AlphaFoldDB; Q6CK18; -.
DR   STRING; 28985.XP_455721.1; -.
DR   EnsemblFungi; CAG98429; CAG98429; KLLA0_F14278g.
DR   GeneID; 2894925; -.
DR   KEGG; kla:KLLA0_F14278g; -.
DR   eggNOG; KOG0411; Eukaryota.
DR   HOGENOM; CLU_020802_2_2_1; -.
DR   InParanoid; Q6CK18; -.
DR   OMA; GLYVMQP; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000598; Chromosome F.
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..446
FT                   /note="GPI-anchored wall transfer protein 1"
FT                   /id="PRO_0000246292"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   446 AA;  50150 MW;  FE2AA4B7AEEFDDBF CRC64;
     MDASGVIDEL KHRKEAFVTG HSGSSIADLR DVTLAGIFSN AAWIYVVSNN PSYRDSFWLD
     FLLNWMGLLC SVTVFGENPF LTGILGLSAV LLFGCISKGS KRETIKETVM DNGNQSATLT
     VYRSTMLILT SIAILAVDFP IFPRKYAKVE TWGISLMDLG VGSFVFSNGI ISYKRLKSGT
     ELSKWAKIKQ SLRSTVVLVV LGFIRLFSVK AVNYQEHATE YGIHWNFFFT LSLLPLAMII
     FDFYNMRLRF VIGLIAAIIY ELCLIYHPTF LDYLLNAERI DFISANREGI FSFVGYCIIY
     LAGQQVGSMF FPISRNPMQL LWKLVALSIF SSAISYVLLH YHPLQVSRRF ASIGYSSMVI
     SFNLLILTFD QLIVECLTSK PRVPKTYRAV NGNGMLVFLI SNVTTGMVNF TFNTLDSPPY
     KAMAILTVYA LFLAVFALKV PFKLKF