ID   GPI14_ASHGO             Reviewed;         397 AA.
AC   Q75C82;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=GPI mannosyltransferase 1;
DE            EC=2.4.1.-;
DE   AltName: Full=GPI mannosyltransferase I;
DE            Short=GPI-MT-I;
DE   AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 14;
GN   Name=GPI14; OrderedLocusNames=ACR034W;
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 first alpha-1,4-mannose to GlcN-
CC       acyl-PI during GPI precursor assembly. Required for cell wall integrity
CC       (By 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 PIGM family. {ECO:0000305}.
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DR   EMBL; AE016816; AAS51261.1; -; Genomic_DNA.
DR   RefSeq; NP_983437.1; NM_208790.1.
DR   AlphaFoldDB; Q75C82; -.
DR   STRING; 33169.AAS51261; -.
DR   CAZy; GT50; Glycosyltransferase Family 50.
DR   EnsemblFungi; AAS51261; AAS51261; AGOS_ACR034W.
DR   GeneID; 4619562; -.
DR   KEGG; ago:AGOS_ACR034W; -.
DR   eggNOG; KOG3893; Eukaryota.
DR   HOGENOM; CLU_024220_3_1_1; -.
DR   InParanoid; Q75C82; -.
DR   OMA; VTSQYFI; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051751; F:alpha-1,4-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:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR007704; PIG-M.
DR   PANTHER; PTHR12886; PTHR12886; 1.
DR   Pfam; PF05007; Mannosyl_trans; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Endoplasmic reticulum;
KW   Glycosyltransferase; GPI-anchor biosynthesis; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..397
FT                   /note="GPI mannosyltransferase 1"
FT                   /id="PRO_0000246223"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   397 AA;  46504 MW;  C55C9A28A745CED3 CRC64;
     MKREECLLVL AGLLARVGFF SYGIYQDAHF AVKYTDIDYH VFHDAARYVA QGNSPYLRDT
     YRYTPLLSWM LVPNHWLQWV HFGKFIFVLF DLLAGVMVMN LLGKCGRRRK LILASLWLLN
     PVVITVSTRG NAESVMAFLI MWFLVHLRNR QFALSGFVYG VAIHFKIYPI IYALPISIYI
     RSSEGSRWFL RLLTMGIATL ATLVGCGIGM YYIYGWEFLE HAYIYHFTRT DHRHNFSLWN
     MLLYLDSSGV VPTTINWAEF AFLPQLFICA AVTYVLWEAP TFQNMQCVLF LQTFAFVTYN
     KVCTSQYFIW YLLFLPSFLL DTTLSGAKGI FLIFLWVGTQ AWWLYNGYLL EFEGKNMFYP
     RLFSACVTFF LANVYLLAQF ILDCRRRNYQ TNIKKTN