Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q

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Q9QYT7 (PIGQ_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 79. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	581 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	GPI-anchor biosynthesis
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	GPI anchor biosynthetic process Inferred from mutant phenotype Ref.2. Source: MGI
Cellular component	glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Inferred from direct assay Ref.2. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phosphatidylinositol N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 581

580

Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q

PRO_0000215665

Regions

Transmembrane

276 – 298

Helical; Potential

Transmembrane

344 – 366

Helical; Potential

Transmembrane

381 – 403

Helical; Potential

Transmembrane

446 – 468

Helical; Potential

Transmembrane

478 – 500

Helical; Potential

Experimental info

Sequence conflict

V → A in AAC79574. Ref.1

Sequence conflict

S → N in AAC79574. Ref.1

Sequence conflict

59 – 61

PVA → QVT in AAC79574. Ref.1

Sequence conflict

Q → E in AAC79574. Ref.1

Sequence conflict

N → K in AAC79574. Ref.1

Sequence conflict

T → A in AAC79574. Ref.1

Sequence conflict

D → N in AAC79574. Ref.1

Sequence conflict

100

R → K in AAC79574. Ref.1

Sequence conflict

104

L → F in AAC79574. Ref.1

Sequence conflict

112

P → H in AAC79574. Ref.1

Sequence conflict

116 – 124

NPLDMHPEE → STLDTPTED in AAC79574. Ref.1

Sequence conflict

149

A → D in AAC79574. Ref.1

Sequence conflict

152

M → I in AAC79574. Ref.1

Sequence conflict

155

T → S in AAC79574. Ref.1

Sequence conflict

184

R → G in AAC79574. Ref.1

Sequence conflict

235

W → G in AAC79574. Ref.1

Sequence conflict

238

S → A in AAC79574. Ref.1

Sequence conflict

251

H → Q in AAC79574. Ref.1

Sequence conflict

268

N → S in AAC79574. Ref.1

Sequence conflict

467

Y → C in BAA23615. Ref.2

Sequence conflict

536 – 543

SYNHVMHI → PYSHVVHT in AAC79574. Ref.1

Sequence conflict

548

R → S in AAC79574. Ref.1

Sequence conflict

565

V → F in AAC79574. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9QYT7 [UniParc].

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

FASTA

581

66,264

        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' referencesShow '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: 9729469] [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: 10373468] [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: 15489334] [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.
IPI	IPI00270003.
RefSeq	NP_035952.2. NM_011822.3.
UniGene	Mm.362054.
3D structure databases
ProteinModelPortal	Q9QYT7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9QYT7.
Proteomic databases
PRIDE	Q9QYT7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026823; ENSMUSP00000026823; ENSMUSG00000025728.
GeneID	14755.
KEGG	mmu:14755.
Organism-specific databases
CTD	9091.
MGI	MGI:1333114. Pigq.
Phylogenomic databases
eggNOG	roNOG08937.
GeneTree	ENSGT00390000004994.
HOVERGEN	HBG036559.
OrthoDB	EOG4VQ9P1.
Enzyme and pathway databases
BRENDA	2.4.1.198. 3474.
Gene expression databases
ArrayExpress	Q9QYT7.
Bgee	Q9QYT7.
Genevestigator	Q9QYT7.
GermOnline	ENSMUSG00000025728. Mus musculus.
Family and domain databases
InterPro	IPR007720. GlcNAc_Gpi1. [Graphical view]
KO	K03860.
Pfam	PF05024. Gpi1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	286819.
SOURCE	Search...

Entry information

Entry name

PIGQ_MOUSE

Accession

Primary (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:	November 16, 2011
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents