ID   PIGY_XENTR              Reviewed;          71 AA.
AC   P0C1P1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 49.
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   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) 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.
CC       {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.
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; BC087772; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001258944.1; NM_001272015.1.
DR   RefSeq; NP_001258945.1; NM_001272016.1.
DR   AlphaFoldDB; P0C1P1; -.
DR   DNASU; 496649; -.
DR   Ensembl; ENSXETT00000054548; ENSXETP00000054548; ENSXETG00000025641.
DR   GeneID; 496649; -.
DR   KEGG; xtr:496649; -.
DR   CTD; 84992; -.
DR   Xenbase; XB-GENE-5783232; pigy.
DR   InParanoid; P0C1P1; -.
DR   Reactome; R-XTR-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; 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_0000246313"
FT   TOPO_DOM        1
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        22..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;  8073 MW;  704F834868F76A59 CRC64;
     MFFSLPVLTV LIPLVSLTGL LYSASVEEDF PNGCTSTASL CFYSLLLPIT LPVYVFFHLW
     TWMGLKLFRH N