ID   GPI18_KLULA             Reviewed;         417 AA.
AC   Q6CMW6;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=KLLA0E17215g;
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: 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; CR382125; CAG99810.1; -; Genomic_DNA.
DR   RefSeq; XP_454723.1; XM_454723.1.
DR   AlphaFoldDB; Q6CMW6; -.
DR   STRING; 28985.XP_454723.1; -.
DR   CAZy; GT76; Glycosyltransferase Family 76.
DR   EnsemblFungi; CAG99810; CAG99810; KLLA0_E17161g.
DR   GeneID; 2893770; -.
DR   KEGG; kla:KLLA0_E17161g; -.
DR   eggNOG; KOG2647; Eukaryota.
DR   HOGENOM; CLU_029048_0_0_1; -.
DR   InParanoid; Q6CMW6; -.
DR   OMA; RWDSIYY; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0120097; C:glycosylphosphatidylinositol-mannosyltransferase II complex; IEA:EnsemblFungi.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR   GO; GO:0031501; C:mannosyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
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..417
FT                   /note="GPI mannosyltransferase 2"
FT                   /id="PRO_0000246248"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   417 AA;  49001 MW;  6BF6E4008150D5ED CRC64;
     MFIDSEYSSF LIINVTFFAV KLLQFGLVWL APRTFDTSTH LFLEHYGITS NPWWGKLLSW
     DSIFFLKTSL WMRNSGYSAP QYEHEWAFSP IWSIIIQSSD LQHIVLKAVS FNLLLHYLST
     WIVYALTKLT FPPFGQNVQT KLALTTSVLF ILSSAAGFLI SVYSEPIAFT FSLLGMLFRQ
     WSISFDVYGN LHMDKLKWIS YLLSSFCFAF AFLNRSNCLL LGLFYVHDCL NLFKQKKWIT
     SIFYPILSGT ILFGVFVYFH YYFPYAALCP ERGEWCNSKI YGLPIPYQSL YSYIQSKHWN
     VGFLKYWTPN NIPNFLFGLP NIVITWNAIT YFSYQYPSRN MKPYIWIARI FLFIMVFLAN
     VQIINRVSSF LPLSLWYISD SLIKNPHEMR IVKYYVMWLL IWIPTQTALF ACFLPPA