ID   GPI11_KLULA             Reviewed;         217 AA.
AC   Q6CTT3;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Glycosylphosphatidylinositol anchor biosynthesis protein 11;
GN   Name=GPI11; OrderedLocusNames=KLLA0C10252g;
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: Acts in the GPI biosynthetic pathway between GlcNAc-PI
CC       synthesis and GPI transfer to protein. {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 PIGF family. {ECO:0000305}.
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DR   EMBL; CR382123; CAH01507.1; -; Genomic_DNA.
DR   RefSeq; XP_452656.1; XM_452656.1.
DR   AlphaFoldDB; Q6CTT3; -.
DR   STRING; 28985.XP_452656.1; -.
DR   EnsemblFungi; CAH01507; CAH01507; KLLA0_C10252g.
DR   GeneID; 2892225; -.
DR   KEGG; kla:KLLA0_C10252g; -.
DR   eggNOG; KOG3144; Eukaryota.
DR   HOGENOM; CLU_111662_0_0_1; -.
DR   InParanoid; Q6CTT3; -.
DR   OMA; FNCDFKV; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000598; 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:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR009580; GPI_biosynthesis_protein_Pig-F.
DR   Pfam; PF06699; PIG-F; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..217
FT                   /note="Glycosylphosphatidylinositol anchor biosynthesis
FT                   protein 11"
FT                   /id="PRO_0000191767"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   217 AA;  25306 MW;  BE1CB5E05C57D88C CRC64;
     MHNRKRKTVK KTVSFSDDQN LTNANLNNHR KGHIDDDTPP VYVRKSWTLI PFHLLALLYW
     FLKYTDFNLL ALLYIMIPTQ VIYLIFRFNK NTIYGKKRLR LNWLLVFITL GACLLLSIPC
     LAIIVLFGAP FVELLKESWL LALHCCFLTY PAVYDVFNCN FKVGYFKKYF ISVVIGCWIS
     CFVIPLDWDR DWQAWPVPLI VGAYLGSFIG FSIGGYI