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Protein

Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q

Gene

Pigq

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. phosphatidylinositol N-acetylglucosaminyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. GPI anchor biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

GPI-anchor biosynthesis

Enzyme and pathway databases

BRENDAi2.4.1.198. 3474.
ReactomeiREACT_243945. Synthesis of glycosylphosphatidylinositol (GPI).
UniPathwayiUPA00196.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Pigq
Synonyms:Gpi1h, Mgpi1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1333114. Pigq.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei276 – 29823HelicalSequence AnalysisAdd
BLAST
Transmembranei344 – 36623HelicalSequence AnalysisAdd
BLAST
Transmembranei381 – 40323HelicalSequence AnalysisAdd
BLAST
Transmembranei446 – 46823HelicalSequence AnalysisAdd
BLAST
Transmembranei478 – 50023HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Source: MGI
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 581580Phosphatidylinositol N-acetylglucosaminyltransferase subunit QPRO_0000215665Add
BLAST

Proteomic databases

PaxDbiQ9QYT7.
PRIDEiQ9QYT7.

PTM databases

PhosphoSiteiQ9QYT7.

Expressioni

Gene expression databases

BgeeiQ9QYT7.
ExpressionAtlasiQ9QYT7. baseline and differential.
GenevestigatoriQ9QYT7.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ9QYT7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PIGQ family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG242183.
GeneTreeiENSGT00390000004994.
HOGENOMiHOG000070446.
HOVERGENiHBG036559.
InParanoidiQ9QYT7.
KOiK03860.
PhylomeDBiQ9QYT7.
TreeFamiTF321258.

Family and domain databases

InterProiIPR007720. GlcNAc_Gpi1.
[Graphical view]
PfamiPF05024. Gpi1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QYT7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVLKVFFPTC CASADSGLLV GRWVPGQSSA VILAVVHFPF IPIQVKELLA
60 70 80 90 100
QVQKASQVPV AVLGTWCHRQ QEPQESLGNF LEGLGTIFSH DPWLQLCRER
110 120 130 140 150
GTRLWSCKAT YPQMSNPLDM HPEEQVMLIF YDQRKLLLSW LHPPPVLPAC
160 170 180 190 200
QMGDTTASTG GLADIFDTVA RSEVLFRNDQ FDERPVRLSH WQSEGVEASI
210 220 230 240 250
LVELAKRASG PVCLLLASLL SLISAASACR LWKLWPLSFI RSKLSTCEQL
260 270 280 290 300
HHRLKHLSFI FSTEKAQNPM QLMRKANMLV SVLLDVALGL LLLSWLHSNN
310 320 330 340 350
RIGQLANALV PVADRVAEEL QHLLQWLMGA PAGLKMNRAL DQVLGRFFLY
360 370 380 390 400
HIHLWISYIH LMSPFIEHIL WHVGLSACLG LTVALSIFSD IIALLTFHIY
410 420 430 440 450
CFYVYGARLY CLKIYGLSSL WRLFRGKKWN VLRQRVDSCS YDLDQLFIGT
460 470 480 490 500
LLFTILVFLL PTTALYYLVF TLLRLLVITV QGLIHLLVDL INSLPLYSLG
510 520 530 540 550
LRLCRPYRLA AGVKFRVLEK EAGRPLRLLM QINPLSYNHV MHIYRLPRCG
560 570 580
CHPKHSWGTL CRKLVFGELI YPWRQREDKQ D
Length:581
Mass (Da):66,264
Last modified:January 23, 2007 - v3
Checksum:i081084B32D09D7E6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51V → A in AAC79574. (PubMed:9729469)Curated
Sequence conflicti28 – 281S → N in AAC79574. (PubMed:9729469)Curated
Sequence conflicti59 – 613PVA → QVT in AAC79574. (PubMed:9729469)Curated
Sequence conflicti74 – 741Q → E in AAC79574. (PubMed:9729469)Curated
Sequence conflicti79 – 791N → K in AAC79574. (PubMed:9729469)Curated
Sequence conflicti86 – 861T → A in AAC79574. (PubMed:9729469)Curated
Sequence conflicti91 – 911D → N in AAC79574. (PubMed:9729469)Curated
Sequence conflicti100 – 1001R → K in AAC79574. (PubMed:9729469)Curated
Sequence conflicti104 – 1041L → F in AAC79574. (PubMed:9729469)Curated
Sequence conflicti112 – 1121P → H in AAC79574. (PubMed:9729469)Curated
Sequence conflicti116 – 1249NPLDMHPEE → STLDTPTED in AAC79574. (PubMed:9729469)Curated
Sequence conflicti149 – 1491A → D in AAC79574. (PubMed:9729469)Curated
Sequence conflicti152 – 1521M → I in AAC79574. (PubMed:9729469)Curated
Sequence conflicti155 – 1551T → S in AAC79574. (PubMed:9729469)Curated
Sequence conflicti184 – 1841R → G in AAC79574. (PubMed:9729469)Curated
Sequence conflicti235 – 2351W → G in AAC79574. (PubMed:9729469)Curated
Sequence conflicti238 – 2381S → A in AAC79574. (PubMed:9729469)Curated
Sequence conflicti251 – 2511H → Q in AAC79574. (PubMed:9729469)Curated
Sequence conflicti268 – 2681N → S in AAC79574. (PubMed:9729469)Curated
Sequence conflicti467 – 4671Y → C in BAA23615. (PubMed:10373468)Curated
Sequence conflicti536 – 5438SYNHVMHI → PYSHVVHT in AAC79574. (PubMed:9729469)Curated
Sequence conflicti548 – 5481R → S in AAC79574. (PubMed:9729469)Curated
Sequence conflicti565 – 5651V → F in AAC79574. (PubMed:9729469)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS28538.1.
RefSeqiNP_035952.2. NM_011822.4.
UniGeneiMm.362054.

Genome annotation databases

EnsembliENSMUST00000026823; ENSMUSP00000026823; ENSMUSG00000025728.
GeneIDi14755.
KEGGimmu:14755.
UCSCiuc008bcp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS28538.1.
RefSeqiNP_035952.2. NM_011822.4.
UniGeneiMm.362054.

3D structure databases

ProteinModelPortaliQ9QYT7.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9QYT7.

Proteomic databases

PaxDbiQ9QYT7.
PRIDEiQ9QYT7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026823; ENSMUSP00000026823; ENSMUSG00000025728.
GeneIDi14755.
KEGGimmu:14755.
UCSCiuc008bcp.1. mouse.

Organism-specific databases

CTDi9091.
MGIiMGI:1333114. Pigq.

Phylogenomic databases

eggNOGiNOG242183.
GeneTreeiENSGT00390000004994.
HOGENOMiHOG000070446.
HOVERGENiHBG036559.
InParanoidiQ9QYT7.
KOiK03860.
PhylomeDBiQ9QYT7.
TreeFamiTF321258.

Enzyme and pathway databases

UniPathwayiUPA00196.
BRENDAi2.4.1.198. 3474.
ReactomeiREACT_243945. Synthesis of glycosylphosphatidylinositol (GPI).

Miscellaneous databases

ChiTaRSiPigq. mouse.
NextBioi286819.
PROiQ9QYT7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QYT7.
ExpressionAtlasiQ9QYT7. baseline and differential.
GenevestigatoriQ9QYT7.

Family and domain databases

InterProiIPR007720. GlcNAc_Gpi1.
[Graphical view]
PfamiPF05024. Gpi1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiPIGQ_MOUSE
AccessioniPrimary (citable) accession number: Q9QYT7
Secondary accession number(s): O35120, O35456, Q99L11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.