ID   GPI18_YARLI             Reviewed;         357 AA.
AC   Q6C216;
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 mannosyltransferase 2;
DE            EC=2.4.1.-;
DE   AltName: Full=GPI mannosyltransferase II;
DE            Short=GPI-MT-II;
DE   AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 18;
GN   Name=GPI18; OrderedLocusNames=YALI0F11649g;
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: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC       anchor biosynthesis. Transfers the second mannose to the
CC       glycosylphosphatidylinositol during GPI precursor assembly (By
CC       similarity). {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 PIGV family. {ECO:0000305}.
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DR   EMBL; CR382132; CAG78103.1; -; Genomic_DNA.
DR   RefSeq; XP_505296.1; XM_505296.1.
DR   AlphaFoldDB; Q6C216; -.
DR   STRING; 4952.CAG78103; -.
DR   CAZy; GT76; Glycosyltransferase Family 76.
DR   EnsemblFungi; CAG78103; CAG78103; YALI0_F11649g.
DR   GeneID; 2908624; -.
DR   KEGG; yli:YALI0F11649g; -.
DR   VEuPathDB; FungiDB:YALI0_F11649g; -.
DR   HOGENOM; CLU_029048_0_0_1; -.
DR   InParanoid; Q6C216; -.
DR   OMA; EYFLHIA; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031501; C:mannosyltransferase complex; IBA:GO_Central.
DR   GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR007315; PIG-V/Gpi18.
DR   PANTHER; PTHR12468; PTHR12468; 1.
DR   Pfam; PF04188; Mannosyl_trans2; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..357
FT                   /note="GPI mannosyltransferase 2"
FT                   /id="PRO_0000246249"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   357 AA;  40723 MW;  AB80630B687BFEAD CRC64;
     MKHFTTLIVV FVAIKAYLVA LALVVPRQYD TSSTLLFPNN RFLSRLVIWD SVFFVSSAER
     SHLYEHEWAF SWMWSRALGL AGSRDAIAYT AIAVSSLSHL LAALMLRKLT ESVFHNKRFA
     ETTALMYILS PAGIFLVAGY TESLFALLSF TGLYLRQRGQ YPLAGAVLGA SCLLRGNGLL
     WGIPFLFDLA SAIKHNQFNR GVSVVIGGSL VGAVFLYTQY LPWSIFCPER DEWCNYYIPS
     IYGYVQQRYW NVGFLRYWTA NNIPNFLFAA PVLYLMYQSM STNPSLVPFY TVHAIMGLAC
     VFMWHVQIIT RISTCLPTLY WYMAKLAQGY NGHYVVRYIF VWITFQVVMW GAYLPPA