PIGQ_MOUSE
ID PIGQ_MOUSE Reviewed; 581 AA.
AC Q9QYT7; O35120; O35456; Q99L11;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q {ECO:0000305};
DE AltName: Full=MGpi1p;
DE AltName: Full=N-acetylglucosamyl transferase component GPI1;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class Q protein;
DE Short=PIG-Q;
GN Name=Pigq {ECO:0000312|MGI:MGI:1333114}; Synonyms=Gpi1h, Mgpi1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=9729469; DOI=10.1042/bj3340609;
RA Tiede A., Schubert J., Nischan C., Jensen I., Westfall B., Taron C.H.,
RA Orlean P., Schmidt R.E.;
RT "Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol
RT membrane anchor biosynthesis in yeast mutants.";
RL Biochem. J. 334:609-616(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129; TISSUE=Liver;
RX PubMed=10373468; DOI=10.1074/jbc.274.26.18582;
RA Hong Y., Ohishi K., Watanabe R., Endo Y., Maeda Y., Kinoshita T.;
RT "GPI1 stabilizes an enzyme essential in the first step of
RT glycosylphosphatidylinositol biosynthesis.";
RL J. Biol. Chem. 274:18582-18588(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor, and Salivary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000250|UniProtKB:Q9BRB3}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000250|UniProtKB:Q9BRB3}.
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 with PIGA, PIGH
CC and PIGC. {ECO:0000250|UniProtKB:Q9BRB3}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PIGQ family. {ECO:0000305}.
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DR EMBL; AF030178; AAC79574.1; -; mRNA.
DR EMBL; AB008895; BAA23615.1; -; mRNA.
DR EMBL; AB008921; BAA84658.1; -; Genomic_DNA.
DR EMBL; BC014287; AAH14287.1; -; mRNA.
DR EMBL; BC003917; AAH03917.1; -; mRNA.
DR CCDS; CCDS28538.1; -.
DR RefSeq; NP_035952.2; NM_011822.4.
DR AlphaFoldDB; Q9QYT7; -.
DR BioGRID; 200022; 1.
DR STRING; 10090.ENSMUSP00000026823; -.
DR iPTMnet; Q9QYT7; -.
DR PhosphoSitePlus; Q9QYT7; -.
DR SwissPalm; Q9QYT7; -.
DR EPD; Q9QYT7; -.
DR MaxQB; Q9QYT7; -.
DR PaxDb; Q9QYT7; -.
DR PRIDE; Q9QYT7; -.
DR ProteomicsDB; 287725; -.
DR Antibodypedia; 22728; 86 antibodies from 22 providers.
DR DNASU; 14755; -.
DR Ensembl; ENSMUST00000026823; ENSMUSP00000026823; ENSMUSG00000025728.
DR Ensembl; ENSMUST00000208043; ENSMUSP00000146704; ENSMUSG00000025728.
DR GeneID; 14755; -.
DR KEGG; mmu:14755; -.
DR UCSC; uc008bcp.2; mouse.
DR CTD; 9091; -.
DR MGI; MGI:1333114; Pigq.
DR VEuPathDB; HostDB:ENSMUSG00000025728; -.
DR eggNOG; KOG1183; Eukaryota.
DR GeneTree; ENSGT00390000004994; -.
DR HOGENOM; CLU_021157_2_0_1; -.
DR InParanoid; Q9QYT7; -.
DR OMA; GICRSRV; -.
DR PhylomeDB; Q9QYT7; -.
DR TreeFam; TF321258; -.
DR Reactome; R-MMU-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 14755; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Pigq; mouse.
DR PRO; PR:Q9QYT7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9QYT7; protein.
DR Bgee; ENSMUSG00000025728; Expressed in fetal liver hematopoietic progenitor cell and 263 other tissues.
DR ExpressionAtlas; Q9QYT7; baseline and differential.
DR Genevisible; Q9QYT7; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
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:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IMP:MGI.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:MGI.
DR InterPro; IPR007720; PigQ/GPI1.
DR PANTHER; PTHR21329; PTHR21329; 1.
DR Pfam; PF05024; Gpi1; 1.
PE 1: Evidence at protein level;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..581
FT /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT subunit Q"
FT /id="PRO_0000215665"
FT TRANSMEM 276..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 5
FT /note="V -> A (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="S -> N (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 59..61
FT /note="PVA -> QVT (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="Q -> E (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="N -> K (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="T -> A (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="D -> N (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="R -> K (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="L -> F (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="P -> H (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 116..124
FT /note="NPLDMHPEE -> STLDTPTED (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="A -> D (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="M -> I (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="T -> S (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="R -> G (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="W -> G (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="S -> A (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="H -> Q (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="N -> S (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="Y -> C (in Ref. 2; BAA23615)"
FT /evidence="ECO:0000305"
FT CONFLICT 536..543
FT /note="SYNHVMHI -> PYSHVVHT (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="R -> S (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="V -> F (in Ref. 1; AAC79574)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 66264 MW; 081084B32D09D7E6 CRC64;
MVLKVFFPTC CASADSGLLV GRWVPGQSSA VILAVVHFPF IPIQVKELLA QVQKASQVPV
AVLGTWCHRQ QEPQESLGNF LEGLGTIFSH DPWLQLCRER GTRLWSCKAT YPQMSNPLDM
HPEEQVMLIF YDQRKLLLSW LHPPPVLPAC QMGDTTASTG GLADIFDTVA RSEVLFRNDQ
FDERPVRLSH WQSEGVEASI LVELAKRASG PVCLLLASLL SLISAASACR LWKLWPLSFI
RSKLSTCEQL HHRLKHLSFI FSTEKAQNPM QLMRKANMLV SVLLDVALGL LLLSWLHSNN
RIGQLANALV PVADRVAEEL QHLLQWLMGA PAGLKMNRAL DQVLGRFFLY HIHLWISYIH
LMSPFIEHIL WHVGLSACLG LTVALSIFSD IIALLTFHIY CFYVYGARLY CLKIYGLSSL
WRLFRGKKWN VLRQRVDSCS YDLDQLFIGT LLFTILVFLL PTTALYYLVF TLLRLLVITV
QGLIHLLVDL INSLPLYSLG LRLCRPYRLA AGVKFRVLEK EAGRPLRLLM QINPLSYNHV
MHIYRLPRCG CHPKHSWGTL CRKLVFGELI YPWRQREDKQ D
