ID   ERI1_ASHGO              Reviewed;          71 AA.
AC   Q75D30;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit;
DE   AltName: Full=Endoplasmic reticulum-associated Ras inhibitor protein 1;
GN   Name=ERI1; OrderedLocusNames=ABR192C-A;
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: Probable component of the GPI-GlcNAc transferase (GPI-GnT)
CC       complex in the endoplasmic reticulum, a complex that catalyzes transfer
CC       of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the
CC       first step in the production of GPI-anchors for cell surface proteins.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBUNIT: Interacts with GPI2, suggesting that it is a component of the
CC       GPI-GnT complex, probably composed of GPI1, GPI2, GPI3, GPI15, and
CC       ERI1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
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DR   EMBL; AE016815; AAS50965.1; -; Genomic_DNA.
DR   RefSeq; NP_983141.1; NM_208494.1.
DR   AlphaFoldDB; Q75D30; -.
DR   STRING; 33169.AAS50965; -.
DR   EnsemblFungi; AAS50965; AAS50965; AGOS_ABR192CA.
DR   GeneID; 4619251; -.
DR   KEGG; ago:AGOS_ABR192CA; -.
DR   HOGENOM; CLU_190860_0_0_1; -.
DR   InParanoid; Q75D30; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000591; Chromosome II.
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:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; GPI-anchor biosynthesis; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..71
FT                   /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT                   ERI1 subunit"
FT                   /id="PRO_0000087027"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   71 AA;  8163 MW;  ACAFE89716EE0025 CRC64;
     MNDKVAATLV LVVTYSIVGA SLWCLTYAWH DETKLYYWCI VQLLPVMLWV WCVISWCGAQ
     LFGYAKRGKA D