PIGY_HUMAN
ID PIGY_HUMAN Reviewed; 71 AA.
AC Q3MUY2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y {ECO:0000305};
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class Y protein;
DE Short=PIG-Y;
GN Name=PIGY {ECO:0000312|HGNC:HGNC:28213};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-10, FUNCTION, SUBCELLULAR
RP LOCATION, TOPOLOGY, INTERACTION WITH PIGA, AND COMPONENT OF GPI-GNT
RP COMPLEX.
RX PubMed=16162815; DOI=10.1091/mbc.e05-08-0743;
RA Murakami Y., Siripanyaphinyo U., Hong Y., Tashima Y., Maeda Y.,
RA Kinoshita T.;
RT "The initial enzyme for glycosylphosphatidylinositol biosynthesis requires
RT PIG-Y, a seventh component.";
RL Mol. Biol. Cell 16:5236-5246(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INVOLVEMENT IN HPMRS6, AND VARIANT HPMRS6 PRO-46.
RX PubMed=26293662; DOI=10.1093/hmg/ddv331;
RA Ilkovski B., Pagnamenta A.T., O'Grady G.L., Kinoshita T., Howard M.F.,
RA Lek M., Thomas B., Turner A., Christodoulou J., Sillence D., Knight S.J.,
RA Popitsch N., Keays D.A., Anzilotti C., Goriely A., Waddell L.B., Brilot F.,
RA North K.N., Kanzawa N., Macarthur D.G., Taylor J.C., Kini U., Murakami Y.,
RA Clarke N.F.;
RT "Mutations in PIGY: expanding the phenotype of inherited
RT glycosylphosphatidylinositol deficiencies.";
RL Hum. Mol. Genet. 24:6146-6159(2015).
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 (PubMed:16162815). May act by regulating the catalytic
CC subunit PIGA (PubMed:16162815). {ECO:0000269|PubMed:16162815}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000269|PubMed:16162815}.
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 (PubMed:16162815).
CC Interacts directly with PIGA; this interaction regulates
CC glycosylphosphatidylinositol-N-acetylglucosaminyltransferase activity
CC (PubMed:16162815). Does not interact with Ras proteins
CC (PubMed:16162815). {ECO:0000269|PubMed:16162815}.
CC -!- INTERACTION:
CC Q3MUY2; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-3920125, EBI-711490;
CC Q3MUY2; P37287: PIGA; NbExp=6; IntAct=EBI-3920125, EBI-26643054;
CC Q3MUY2; A0PK05: TMEM72; NbExp=3; IntAct=EBI-3920125, EBI-12878352;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16162815}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16162815}.
CC -!- DISEASE: Hyperphosphatasia with intellectual disability syndrome 6
CC (HPMRS6) [MIM:616809]: An autosomal recessive, multisystem disorder
CC characterized by severe developmental delay, dysmorphism, seizures,
CC cataracts, and early death in some patients.
CC {ECO:0000269|PubMed:26293662}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: PREY and PIGY, 2 apparently unrelated proteins, are
CC respectively the product of an upstream and a downstream ORF contained
CC in a single bicistronic transcript.
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; AB206972; BAE44507.1; -; mRNA.
DR EMBL; BC007876; AAH07876.2; -; mRNA.
DR CCDS; CCDS54778.1; -.
DR RefSeq; NP_001036081.1; NM_001042616.2.
DR AlphaFoldDB; Q3MUY2; -.
DR BioGRID; 124417; 5.
DR ComplexPortal; CPX-6502; Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex.
DR IntAct; Q3MUY2; 4.
DR STRING; 9606.ENSP00000432688; -.
DR iPTMnet; Q3MUY2; -.
DR PhosphoSitePlus; Q3MUY2; -.
DR BioMuta; PIGY; -.
DR PaxDb; Q3MUY2; -.
DR PeptideAtlas; Q3MUY2; -.
DR PRIDE; Q3MUY2; -.
DR Antibodypedia; 58497; 80 antibodies from 21 providers.
DR DNASU; 84992; -.
DR Ensembl; ENST00000527353.2; ENSP00000432688.1; ENSG00000255072.2.
DR GeneID; 84992; -.
DR KEGG; hsa:84992; -.
DR MANE-Select; ENST00000527353.2; ENSP00000432688.1; NM_001042616.3; NP_001036081.1.
DR UCSC; uc062ydg.1; human.
DR CTD; 84992; -.
DR DisGeNET; 84992; -.
DR GeneCards; PIGY; -.
DR HGNC; HGNC:28213; PIGY.
DR HPA; ENSG00000255072; Low tissue specificity.
DR MalaCards; PIGY; -.
DR MIM; 610662; gene.
DR MIM; 616809; phenotype.
DR neXtProt; NX_Q3MUY2; -.
DR OpenTargets; ENSG00000255072; -.
DR Orphanet; 247262; Hyperphosphatasia-intellectual disability syndrome.
DR PharmGKB; PA143485576; -.
DR VEuPathDB; HostDB:ENSG00000255072; -.
DR eggNOG; ENOG502S4A7; Eukaryota.
DR GeneTree; ENSGT00610000087446; -.
DR HOGENOM; CLU_2978556_0_0_1; -.
DR InParanoid; Q3MUY2; -.
DR OMA; DETFPQG; -.
DR PhylomeDB; Q3MUY2; -.
DR BRENDA; 2.4.1.198; 2681.
DR PathwayCommons; Q3MUY2; -.
DR Reactome; R-HSA-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR SignaLink; Q3MUY2; -.
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 84992; 114 hits in 985 CRISPR screens.
DR ChiTaRS; PIGY; human.
DR GenomeRNAi; 84992; -.
DR Pharos; Q3MUY2; Tbio.
DR PRO; PR:Q3MUY2; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q3MUY2; protein.
DR Bgee; ENSG00000255072; Expressed in islet of Langerhans and 95 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:MGI.
DR InterPro; IPR029164; PIG-Y.
DR InterPro; IPR033535; PIGY_chordates.
DR PANTHER; PTHR39235; PTHR39235; 1.
DR Pfam; PF15159; PIG-Y; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disease variant; Endoplasmic reticulum;
KW GPI-anchor biosynthesis; Intellectual disability; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..71
FT /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT subunit Y"
FT /id="PRO_0000246311"
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"
FT VARIANT 46
FT /note="L -> P (in HPMRS6; may diminish protein expression
FT and/or stability; decreases cell surface expression of GPI-
FT anchored proteins, including CD55 and CD59, in skin
FT fibroblasts from affected individual; dbSNP:rs869025322)"
FT /evidence="ECO:0000269|PubMed:26293662"
FT /id="VAR_076351"
SQ SEQUENCE 71 AA; 8058 MW; 143975D8CCECED34 CRC64;
MFLSLPTLTV LIPLVSLAGL FYSASVEENF PQGCTSTASL CFYSLLLPIT IPVYVFFHLW
TWMGIKLFRH N
