GPI18_CANGA
ID GPI18_CANGA Reviewed; 433 AA.
AC Q6FWN4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=CAGL0C04235g;
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 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; CR380949; CAG58266.1; -; Genomic_DNA.
DR RefSeq; XP_445360.1; XM_445360.1.
DR AlphaFoldDB; Q6FWN4; -.
DR STRING; 5478.XP_445360.1; -.
DR CAZy; GT76; Glycosyltransferase Family 76.
DR EnsemblFungi; CAG58266; CAG58266; CAGL0C04235g.
DR GeneID; 2886825; -.
DR KEGG; cgr:CAGL0C04235g; -.
DR CGD; CAL0127622; CAGL0C04235g.
DR VEuPathDB; FungiDB:CAGL0C04235g; -.
DR eggNOG; KOG2647; Eukaryota.
DR HOGENOM; CLU_029048_0_0_1; -.
DR InParanoid; Q6FWN4; -.
DR OMA; RWDSIYY; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002428; Chromosome C.
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..433
FT /note="GPI mannosyltransferase 2"
FT /id="PRO_0000246243"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 433 AA; 51042 MW; E7EA2D034379743A CRC64;
MHSLVKPVLF FVVVRIVQYA IISLSPNKQF DLSTNLLLAK YCSEQETQQF WHRHLFNKLL
SWDSVFFIKT AMTMDGYPEY EHEWAFSVIW SSLIRSVSPS NNFYTVLKTA VILENLIYFM
AMITLFYLTR ITFGKLDKSK THLSDKLATF TAILFSCNSG SGFFTGPYSE PLSFLFSFLG
ILAREFSVTP IIPYGLEFKS SKIFYYTIVS SFCFTIATLN RSNCILLGFY YVFDSIYLIR
RQKYKKALLF PVLAGCIVAL FFVRQQFYIP YKNFCELRGE WCNESLINFK PLHFLTRKSL
YSYIQSEHWN LGLFNYWTPN NIPNFLFGLP TFVILFSSTF YFSRVYPNYK LKPLIFITRA
FTIIILLFAH VQIINRISTF IPLHLWYISD RFVKFEANKK MTGDDWIVKG YIYWLIFWVP
IQTSLFVFFL PPA
