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Q9QYT7 (PIGQ_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q

EC=2.4.1.198
Alternative name(s):
MGpi1p
N-acetylglucosamyl transferase component GPI1
Phosphatidylinositol-glycan biosynthesis class Q protein
Short name=PIG-Q
Gene names
Name:Pigq
Synonyms:Gpi1h, Mgpi1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.

Catalytic activity

UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol.

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subunit structure

Associates with PIGA, PIGC, PIGH, PIGP and DPM2. The latter is not essential for activity.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the PIGQ family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 581580Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
PRO_0000215665

Regions

Transmembrane276 – 29823Helical; Potential
Transmembrane344 – 36623Helical; Potential
Transmembrane381 – 40323Helical; Potential
Transmembrane446 – 46823Helical; Potential
Transmembrane478 – 50023Helical; Potential

Experimental info

Sequence conflict51V → A in AAC79574. Ref.1
Sequence conflict281S → N in AAC79574. Ref.1
Sequence conflict59 – 613PVA → QVT in AAC79574. Ref.1
Sequence conflict741Q → E in AAC79574. Ref.1
Sequence conflict791N → K in AAC79574. Ref.1
Sequence conflict861T → A in AAC79574. Ref.1
Sequence conflict911D → N in AAC79574. Ref.1
Sequence conflict1001R → K in AAC79574. Ref.1
Sequence conflict1041L → F in AAC79574. Ref.1
Sequence conflict1121P → H in AAC79574. Ref.1
Sequence conflict116 – 1249NPLDMHPEE → STLDTPTED in AAC79574. Ref.1
Sequence conflict1491A → D in AAC79574. Ref.1
Sequence conflict1521M → I in AAC79574. Ref.1
Sequence conflict1551T → S in AAC79574. Ref.1
Sequence conflict1841R → G in AAC79574. Ref.1
Sequence conflict2351W → G in AAC79574. Ref.1
Sequence conflict2381S → A in AAC79574. Ref.1
Sequence conflict2511H → Q in AAC79574. Ref.1
Sequence conflict2681N → S in AAC79574. Ref.1
Sequence conflict4671Y → C in BAA23615. Ref.2
Sequence conflict536 – 5438SYNHVMHI → PYSHVVHT in AAC79574. Ref.1
Sequence conflict5481R → S in AAC79574. Ref.1
Sequence conflict5651V → F in AAC79574. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9QYT7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 081084B32D09D7E6

FASTA58166,264
        10         20         30         40         50         60 
MVLKVFFPTC CASADSGLLV GRWVPGQSSA VILAVVHFPF IPIQVKELLA QVQKASQVPV 

        70         80         90        100        110        120 
AVLGTWCHRQ QEPQESLGNF LEGLGTIFSH DPWLQLCRER GTRLWSCKAT YPQMSNPLDM 

       130        140        150        160        170        180 
HPEEQVMLIF YDQRKLLLSW LHPPPVLPAC QMGDTTASTG GLADIFDTVA RSEVLFRNDQ 

       190        200        210        220        230        240 
FDERPVRLSH WQSEGVEASI LVELAKRASG PVCLLLASLL SLISAASACR LWKLWPLSFI 

       250        260        270        280        290        300 
RSKLSTCEQL HHRLKHLSFI FSTEKAQNPM QLMRKANMLV SVLLDVALGL LLLSWLHSNN 

       310        320        330        340        350        360 
RIGQLANALV PVADRVAEEL QHLLQWLMGA PAGLKMNRAL DQVLGRFFLY HIHLWISYIH 

       370        380        390        400        410        420 
LMSPFIEHIL WHVGLSACLG LTVALSIFSD IIALLTFHIY CFYVYGARLY CLKIYGLSSL 

       430        440        450        460        470        480 
WRLFRGKKWN VLRQRVDSCS YDLDQLFIGT LLFTILVFLL PTTALYYLVF TLLRLLVITV 

       490        500        510        520        530        540 
QGLIHLLVDL INSLPLYSLG LRLCRPYRLA AGVKFRVLEK EAGRPLRLLM QINPLSYNHV 

       550        560        570        580 
MHIYRLPRCG CHPKHSWGTL CRKLVFGELI YPWRQREDKQ D 

« Hide

References

« Hide 'large scale' references
[1]"Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol membrane anchor biosynthesis in yeast mutants."
Tiede A., Schubert J., Nischan C., Jensen I., Westfall B., Taron C.H., Orlean P., Schmidt R.E.
Biochem. J. 334:609-616(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
Tissue: Brain.
[2]"GPI1 stabilizes an enzyme essential in the first step of glycosylphosphatidylinositol biosynthesis."
Hong Y., Ohishi K., Watanabe R., Endo Y., Maeda Y., Kinoshita T.
J. Biol. Chem. 274:18582-18588(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129.
Tissue: Liver.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor and Salivary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF030178 mRNA. Translation: AAC79574.1.
AB008895 mRNA. Translation: BAA23615.1.
AB008921 Genomic DNA. Translation: BAA84658.1.
BC014287 mRNA. Translation: AAH14287.1.
BC003917 mRNA. Translation: AAH03917.1.
CCDSCCDS28538.1.
RefSeqNP_035952.2. NM_011822.4.
UniGeneMm.362054.

3D structure databases

ProteinModelPortalQ9QYT7.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9QYT7.

Proteomic databases

PaxDbQ9QYT7.
PRIDEQ9QYT7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026823; ENSMUSP00000026823; ENSMUSG00000025728.
GeneID14755.
KEGGmmu:14755.
UCSCuc008bcp.1. mouse.

Organism-specific databases

CTD9091.
MGIMGI:1333114. Pigq.

Phylogenomic databases

eggNOGNOG242183.
GeneTreeENSGT00390000004994.
HOGENOMHOG000070446.
HOVERGENHBG036559.
KOK03860.
PhylomeDBQ9QYT7.
TreeFamTF321258.

Enzyme and pathway databases

BRENDA2.4.1.198. 3474.
UniPathwayUPA00196.

Gene expression databases

ArrayExpressQ9QYT7.
BgeeQ9QYT7.
GenevestigatorQ9QYT7.

Family and domain databases

InterProIPR007720. GlcNAc_Gpi1.
[Graphical view]
PfamPF05024. Gpi1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPIGQ. mouse.
NextBio286819.
PROQ9QYT7.
SOURCESearch...

Entry information

Entry namePIGQ_MOUSE
AccessionPrimary (citable) accession number: Q9QYT7
Secondary accession number(s): O35120, O35456, Q99L11
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot