GPI18_CRYNB
ID GPI18_CRYNB Reviewed; 423 AA.
AC P0CP63; Q55WA5; Q5KJZ2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 34.
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=CNBC2320;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AAEY01000013; EAL22094.1; -; Genomic_DNA.
DR RefSeq; XP_776741.1; XM_771648.1.
DR AlphaFoldDB; P0CP63; -.
DR CAZy; GT76; Glycosyltransferase Family 76.
DR EnsemblFungi; EAL22094; EAL22094; CNBC2320.
DR GeneID; 4934897; -.
DR KEGG; cnb:CNBC2320; -.
DR VEuPathDB; FungiDB:CNBC2320; -.
DR HOGENOM; CLU_029048_1_0_1; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000001435; Chromosome 3.
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; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..423
FT /note="GPI mannosyltransferase 2"
FT /id="PRO_0000410189"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 423 AA; 46857 MW; 273877D4B40C93C9 CRC64;
MAKLSPLTLI FIAACLSRIL HLTILSGLSK ALPLFDTSPS LLLSSPPPAL RWDAIHFASV
AYNGYEYEQQ VAFQPGWLAV MRLAGEGVRF IRAASVVELK DVILGGTIVA NVAFVAATLV
LYKLTKHIFN PTFAFLTSLL YLLPPTATPS APYTEPIYSL LTFSGIYLLS IKRQMVLAGL
CFAGATTIRS TGIFNSITLM CFAVFGDAHI FDLDPKDYCK IRKKLKPFLS AILVVAPFFM
FQHYTETVFC TRELKRASTA RPWCSNSPPV SYGFVQKLYW NVGPFEYWTV SQLPNFALAM
PILFSSLAGV VKFFSHLVSS SQVLNHGTEE IPPPPILFEL YSVHVLTMAL LLFTSHTQIT
LRVCLGDPVV WWNAVKLGFD NVQIGEAPMG QVKVNKFGRY WIGWTVVWGA VAAVLWAGHY
PPA