ID   GPI14_DEBHA             Reviewed;         414 AA.
AC   Q6BHI9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=GPI mannosyltransferase 1;
DE            EC=2.4.1.-;
DE   AltName: Full=GPI mannosyltransferase I;
DE            Short=GPI-MT-I;
DE   AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 14;
GN   Name=GPI14; OrderedLocusNames=DEHA2G18216g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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 first alpha-1,4-mannose to GlcN-
CC       acyl-PI during GPI precursor assembly. Required for cell wall integrity
CC       (By 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 PIGM family. {ECO:0000305}.
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DR   EMBL; CR382139; CAG90838.2; -; Genomic_DNA.
DR   RefSeq; XP_462332.2; XM_462332.2.
DR   AlphaFoldDB; Q6BHI9; -.
DR   STRING; 4959.XP_462332.2; -.
DR   CAZy; GT50; Glycosyltransferase Family 50.
DR   EnsemblFungi; CAG90838; CAG90838; DEHA2G18216g.
DR   GeneID; 2905271; -.
DR   KEGG; dha:DEHA2G18216g; -.
DR   VEuPathDB; FungiDB:DEHA2G18216g; -.
DR   eggNOG; KOG3893; Eukaryota.
DR   HOGENOM; CLU_024220_1_0_1; -.
DR   InParanoid; Q6BHI9; -.
DR   OMA; VTSQYFI; -.
DR   OrthoDB; 1003258at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000599; Chromosome G.
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:0051751; F:alpha-1,4-mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR007704; PIG-M.
DR   PANTHER; PTHR12886; PTHR12886; 1.
DR   Pfam; PF05007; Mannosyl_trans; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Endoplasmic reticulum;
KW   Glycosyltransferase; GPI-anchor biosynthesis; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..414
FT                   /note="GPI mannosyltransferase 1"
FT                   /id="PRO_0000246228"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   414 AA;  47873 MW;  D7CF6E0E5003D2B1 CRC64;
     MLQLSISHII VLSLLIRIGF FLFGLYQDKY MTVKYTDIDY VVFSDAANYV YNGYSPYSRE
     TYRYTPLLAW MLIPNCWGGQ WSNFGKYIFM ISDLITGIII LKLLSGISIA GKKLSTNKII
     MLSSIWLLNP MVITISTRGS SESVLTVMIM LSLYYLINKK SIIASGFWLG LSIHFKIYPV
     IYLPSIMLYL STSGTPFIDV PIVRWVNRTN IKFLITTLIT IGAFNGIMYS IYGYEFLYNS
     YLYHLIRIDH RHNFSVYNVA LYYKSALSEI AEASLGFFTG NMEKFVMLPQ LSISALILPL
     LFARRDLISC IFIQTFAFVT FNKVITSQYF IWFLIFLPHY LAQSKLYSNK HMMKGIVALL
     LWIVSQGSWL YFAYQLEFLG ISTFDNGLLF SSFFFYISNC WILSVFIDDL NNDL