ID   GPI18_ASHGO             Reviewed;         427 AA.
AC   Q757K7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=AER005C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS52689.1; -; Genomic_DNA.
DR   RefSeq; NP_984865.1; NM_210219.1.
DR   AlphaFoldDB; Q757K7; -.
DR   STRING; 33169.AAS52689; -.
DR   CAZy; GT76; Glycosyltransferase Family 76.
DR   EnsemblFungi; AAS52689; AAS52689; AGOS_AER005C.
DR   GeneID; 4621064; -.
DR   KEGG; ago:AGOS_AER005C; -.
DR   eggNOG; KOG2647; Eukaryota.
DR   HOGENOM; CLU_029048_0_0_1; -.
DR   InParanoid; Q757K7; -.
DR   OMA; RWDSIYY; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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; IBA:GO_Central.
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: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..427
FT                   /note="GPI mannosyltransferase 2"
FT                   /id="PRO_0000246239"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   427 AA;  50042 MW;  7303E7717E84D48A CRC64;
     MECFKRLTTV FFTVKLVQYL LVYFAPGQFD TSTPLFLEKY QPLQPEKWYH KLLSWDSVYF
     VKNGLQAVTH TNAYGYVSLP EYEHEWMFSP FVWSQTLKTA GGATLRNWAA PIDTLLVRAT
     LLNLVLHYVS VWLLYALTLR TFPKNRELAY KTSLLFILSS AAGFLLAPYS EPLSFAFSFL
     GMLLRMLAVE HNVYGGITLA WYNWLPYTLS GICFSVAAAN RPNCVLLGVY YIYDVLKLVR
     QRNWVRAVLF PCIAGSMMLG IFAYMHYYLP SVVFCPERES WCKHSLPWIH IPYKSFYSFV
     QGYYWRNGFL NYWTWNNVPN FLFALPNLVI LWYSTVYFSY QYPLESIRPL VYITRALLLI
     ITFFAHVQII NRISSFIPLH LWYLSDRMIK TTGEAKGDDR LVYLYVNWLI LWIPLQTVLF
     ACFLPPA