ID   GPI3_YEAS1              Reviewed;         452 AA.
AC   B3LKQ3;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
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=SCRG_02322;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CH408046; EDV11051.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LKQ3; -.
DR   SMR; B3LKQ3; -.
DR   EnsemblFungi; EDV11051; EDV11051; SCRG_02322.
DR   HOGENOM; CLU_009583_19_0_1; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000008335; 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_0000377637"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  51242 MW;  7589FD815707EC73 CRC64;
     MGFNIAMLCD FFYPQLGGVE FHIYHLSQKL IDLGHSVVII THAYKDRVGV RHLTNGLKVY
     HVPFFVIFRE TTFPTVFSTF PIIRNILLRE QIQIVHSHGS ASTFAHEGIL HANTMGLRTV
     FTDHSLYGFN NLTSIWVNKL LTFTLTNIDR VICVSNTCKE NMIVRTELSP DIISVIPNAV
     VSEDFKPRDP TGGTKRKQSR DKIVIVVIGR LFPNKGSDLL TRIIPKVCSS HEDVEFIVAG
     DGPKFIDFQQ MIESHRLQKR VQLLGSVPHE KVRDVLCQGD IYLHASLTEA FGTILVEAAS
     CNLLIVTTQV GGIPEVLPNE MTVYAEQTSV SDLVQATNKA INIIRSKALD TSSFHDSVSK
     MYDWMDVAKR TVEIYTNISS TSSADDKDWM KMVANLYKRD GIWAKHLYLL CGIVEYMLFF
     LLEWLYPRDE IDLAPKWPKK TVSNETKEAR ET