ID   GPI3_YEAS7              Reviewed;         452 AA.
AC   A6ZW78;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit;
DE            EC=2.4.1.198;
DE   AltName: Full=GlcNAc-PI synthesis protein;
GN   Name=SPT14; ORFNames=SCY_5555;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Catalytic subunit in the complex catalyzing the transfer of
CC       N-acetylglucosamine from UDP-N-acetylglucosamine to
CC       phosphatidylinositol, the first step of GPI biosynthesis.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + UDP-N-
CC         acetyl-alpha-D-glucosamine = a 6-(N-acetyl-alpha-D-glucosaminyl)-1-
CC         phosphatidyl-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:14789,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57265, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58223; EC=2.4.1.198;
CC   -!- ACTIVITY REGULATION: Inhibited by Ras, probably via the interaction
CC       between RAS2 and ERI1. {ECO:0000250}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBUNIT: Component of the phosphatidylinositol N-
CC       acetylglucosaminyltransferase complex composed of at least GPI1, GPI2,
CC       GPI3, GPI15, GPI19 and ERI1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {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; AAFW02000135; EDN60970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZW78; -.
DR   SMR; A6ZW78; -.
DR   PRIDE; A6ZW78; -.
DR   EnsemblFungi; EDN60970; EDN60970; SCY_5555.
DR   HOGENOM; CLU_009583_19_0_1; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03796; GT4_PIG-A-like; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR039507; PIG-A/GPI3.
DR   InterPro; IPR013234; PIGA_GPI_anchor_biosynthesis.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF08288; PIGA; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW   Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..452
FT                   /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT                   GPI3 subunit"
FT                   /id="PRO_0000377639"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  51316 MW;  AAEB6D80967A7C7F CRC64;
     MGFNIAMLCD FFYPQLGGVE FHIYHLSQKL IDLGHSVVII THAYKDRVGV RHLTNGLKVY
     HVPFFVIFRE TTFPTVFSTF PIIRNILLRE QIQIVHSHGS ASTFAHEGIL HANTMGLRTV
     FTDHSLYGFN NLTSIWVNKL LTFTLTNIDR VICVSNTCKE NMIVRTELSP DIISVIPNAV
     VSEDFKPRDP TDSTKRKQSR DKIVIVVIGR LFPNKGSDLL TRIIPKVCSS HEDVEFIVAG
     DGPKFIDFQQ MIESHRLQKR VQLLGSVPHE KVRDVLCQGD IYLHASLTEA FGTILVEAAS
     CNLLIVTTQV GGIPEVLPNE MTVYAEQTSV SDLVQATNKA INIIRSKALD TSSFHDSVSK
     MYDWMDVAKR TVEIYTNISS TSSADDKDWM KMVANLYKRD GIWAKHLYLL CGIVEYMLFF
     LLEWLYPRDE IDLAPKWPKK SVSNETKEAR ET