GPI14_CANGA
ID GPI14_CANGA Reviewed; 431 AA.
AC Q6FXQ5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=CAGL0B03905g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380948; CAG58040.1; -; Genomic_DNA.
DR RefSeq; XP_445140.1; XM_445140.1.
DR AlphaFoldDB; Q6FXQ5; -.
DR STRING; 5478.XP_445140.1; -.
DR CAZy; GT50; Glycosyltransferase Family 50.
DR EnsemblFungi; CAG58040; CAG58040; CAGL0B03905g.
DR GeneID; 2886715; -.
DR KEGG; cgr:CAGL0B03905g; -.
DR CGD; CAL0127722; CAGL0B03905g.
DR VEuPathDB; FungiDB:CAGL0B03905g; -.
DR eggNOG; KOG3893; Eukaryota.
DR HOGENOM; CLU_024220_1_0_1; -.
DR InParanoid; Q6FXQ5; -.
DR OMA; VTSQYFI; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002428; Chromosome B.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IEA:EnsemblFungi.
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:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
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..431
FT /note="GPI mannosyltransferase 1"
FT /id="PRO_0000246227"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 410..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 50244 MW; 41CD6DAA67BF7C0B CRC64;
MFKLGTIGLL SLAVLLRIAF FLFGVYQDEH FTVKYTDIDY QVFNDAAWFV AHRKSPYNRD
TYRYTPLLSW LLLPNHMIPW FHFGKLIFVL CDLATGVLIL QMLKKLKSKY RYGTDRMTIM
AAIWLLNPMV ITISTRGNAE SVLCFLILSF LYCFLCEQYL LGGLLFGLSI HFKIYPIIYA
LPIAIYVAAA HYNKTQSVFK SSFKLFLVGF STLIVLILLT VFMYMLYGDK FIDQTYLYHI
YRTDHRHNFS VWNMLLYFNS ALPKTSELSK FVFLPQMIIV LAISLTQLRR PSSFPLLCNV
LFLETFAFVT FNKVCTSQYF IWYLIFLPFV LYNTRISMRR GIVMLVVWVA TQALWLRQGY
LLEFEGQNVF YPGLFCASVG FFVSNAWILG QFIEDTIIQN DYVYRIEPSE SRSKDSAVID
KPAIAKTEKA E
