GPI18_DEBHA
ID GPI18_DEBHA Reviewed; 428 AA.
AC Q6BRZ9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=DEHA2D12628g;
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 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; CR382136; CAG87189.1; -; Genomic_DNA.
DR RefSeq; XP_459021.1; XM_459021.1.
DR AlphaFoldDB; Q6BRZ9; -.
DR STRING; 4959.XP_459021.1; -.
DR CAZy; GT76; Glycosyltransferase Family 76.
DR EnsemblFungi; CAG87189; CAG87189; DEHA2D12628g.
DR GeneID; 2901205; -.
DR KEGG; dha:DEHA2D12628g; -.
DR VEuPathDB; FungiDB:DEHA2D12628g; -.
DR eggNOG; KOG2647; Eukaryota.
DR HOGENOM; CLU_029048_0_0_1; -.
DR InParanoid; Q6BRZ9; -.
DR OMA; RWDSIYY; -.
DR OrthoDB; 960696at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000599; Chromosome D.
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:0000009; F:alpha-1,6-mannosyltransferase activity; IEA:InterPro.
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; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..428
FT /note="GPI mannosyltransferase 2"
FT /id="PRO_0000246246"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 428 AA; 49934 MW; EB375D8977371FF9 CRC64;
MKDISVIVKY FVLFKSIQLI IVYFTPVQFD TSSQLIIEKY RNDKLQVLSD WKLPFQISDS
ILSNIIDKFI TWDAVYFSDL FLNDIKYEHQ FVFCPLWWRI IKWIPIGEGN YYKKLMLGML
CSNICHLGTC IILYYLTFEM FKTSSLFTKT LREFSLISSI IYIISPAGIF LTASYSESPC
ALFSMASIYL REISINRENF NHLNSKNSLK THWIYKVTYL LSGTMVSIAY GIRGNCLLLG
AMFLFDLYEF GIRNRDITDS ILSLVSGGQI FVSIIALNWY TYAIFCPARG EWCQSWIPSL
FSYAQSHYWN VGFFNYWSLA NIPNFLFALP TIVLTLQSFK HFTEEKPVKN LLPVMIVNGM
LLVGAVFWWH VQILTRISSF LPLMYWFVAS MWISDSPTYK RYSENTMKFM IGWNLIQTSM
FAAFLPPA
