ID   GPI18_CRYNJ             Reviewed;         423 AA.
AC   P0CP62; Q55WA5; Q5KJZ2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 42.
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=CNC04850;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017343; AAW42711.1; -; Genomic_DNA.
DR   RefSeq; XP_570018.1; XM_570018.1.
DR   AlphaFoldDB; P0CP62; -.
DR   STRING; 5207.AAW42711; -.
DR   CAZy; GT76; Glycosyltransferase Family 76.
DR   PaxDb; P0CP62; -.
DR   EnsemblFungi; AAW42711; AAW42711; CNC04850.
DR   VEuPathDB; FungiDB:CNC04850; -.
DR   eggNOG; KOG2647; Eukaryota.
DR   HOGENOM; CLU_029048_1_0_1; -.
DR   InParanoid; P0CP62; -.
DR   OMA; EYFLHIA; -.
DR   OrthoDB; 960696at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000002149; Chromosome 3.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031501; C:mannosyltransferase complex; IBA:GO_Central.
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:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
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..423
FT                   /note="GPI mannosyltransferase 2"
FT                   /id="PRO_0000246245"
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;  46878 MW;  1F583BE0EEC7E196 CRC64;
     MAKLSPLTLI FIAACLSRIL QLTILSGLSK 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
     PILFFSLAGV VKFFSHLVSS SQVLNHGTEE IPPPPILFEL YSVHVLTMAL LLFTSHTQIT
     LRVCLGDPVV WWNAVKLGFD NVQIGEAPTG QVKVNKFGRY WIGWTVVWGA VAAVLWAGHY
     PPA