ID   PIGY_BOVIN              Reviewed;          71 AA.
AC   P0C1N9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y {ECO:0000250|UniProtKB:Q3MUY2};
DE   AltName: Full=Phosphatidylinositol-glycan biosynthesis class Y protein;
DE            Short=PIG-Y;
GN   Name=PIGY {ECO:0000250|UniProtKB:Q3MUY2};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the glycosylphosphatidylinositol-N-
CC       acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the
CC       transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to
CC       phosphatidylinositol and participates in the first step of GPI
CC       biosynthesis. May act by regulating the catalytic subunit PIGA.
CC       {ECO:0000250|UniProtKB:Q3MUY2}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000250|UniProtKB:Q3MUY2}.
CC   -!- SUBUNIT: Component of the glycosylphosphatidylinositol-N-
CC       acetylglucosaminyltransferase (GPI-GnT) complex composed at least by
CC       PIGA, PIGC, PIGH, PIGP, PIGQ, PIGY and DPM2. Interacts directly with
CC       PIGA; this interaction regulates glycosylphosphatidylinositol-N-
CC       acetylglucosaminyltransferase activity. Does not interact with Ras
CC       proteins. {ECO:0000250|UniProtKB:Q3MUY2}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q3MUY2}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q3MUY2}.
CC   -!- MISCELLANEOUS: PREY is derived from the same bicistronic transcript
CC       that encodes these 2 different proteins.
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DR   EMBL; BC111246; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001257875.1; NM_001270946.1.
DR   AlphaFoldDB; P0C1N9; -.
DR   GeneID; 514374; -.
DR   KEGG; bta:514374; -.
DR   CTD; 84992; -.
DR   InParanoid; P0C1N9; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR029164; PIG-Y.
DR   InterPro; IPR033535; PIGY_chordates.
DR   PANTHER; PTHR39235; PTHR39235; 1.
DR   Pfam; PF15159; PIG-Y; 1.
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                   subunit Y"
FT                   /id="PRO_0000246310"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..44
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..71
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   71 AA;  8105 MW;  0303FB3D681BF834 CRC64;
     MFLSLPMLTV LIPLVSLAGL FYSASVEDDF PQGCTSTTSL CFYSLLLPIT IPVYVFFHLW
     TWMGIKLFRH N