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Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q (EC 2.4.1.198) (N-acetylglucosamyl transferase component GPI1) (Phosphatidylinositol-glycan biosynthesis class Q protein) (PIG-Q)

 PIGQ_HUMAN              Reviewed;         760 AA.
Q9BRB3; A2IDE1; D3DU52; O14927; Q96G00; Q96S22; Q9UJH4;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 147.
RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q;
EC=2.4.1.198;
AltName: Full=N-acetylglucosamyl transferase component GPI1;
AltName: Full=Phosphatidylinositol-glycan biosynthesis class Q protein;
Short=PIG-Q;
Name=PIGQ; Synonyms=GPI1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=9729469; DOI=10.1042/bj3340609;
Tiede A., Schubert J., Nischan C., Jensen I., Westfall B., Taron C.H.,
Orlean P., Schmidt R.E.;
"Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol
membrane anchor biosynthesis in yeast mutants.";
Biochem. J. 334:609-616(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=9463366; DOI=10.1093/emboj/17.4.877;
Watanabe R., Inoue N., Westfall B., Taron C.H., Orlean P., Takeda J.,
Kinoshita T.;
"The first step of glycosylphosphatidylinositol biosynthesis is
mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1.";
EMBO J. 17:877-885(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-14.
PubMed=11157797; DOI=10.1093/hmg/10.4.339;
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
Higgs D.R.;
"Sequence, structure and pathology of the fully annotated terminal 2
Mb of the short arm of human chromosome 16.";
Hum. Mol. Genet. 10:339-352(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
ALA-14.
TISSUE=Melanoma, and Retinoblastoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-6.
PubMed=10944123; DOI=10.1093/emboj/19.16.4402;
Watanabe R., Murakami Y., Marmor M.D., Inoue N., Maeda Y., Hino J.,
Kangawa K., Julius M., Kinoshita T.;
"Initial enzyme for glycosylphosphatidylinositol biosynthesis requires
PIG-P and is regulated by DPM2.";
EMBO J. 19:4402-4411(2000).
-!- 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:
Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) +
UDP-N-acetyl-alpha-D-glucosamine = a 6-(N-acetyl-alpha-D-
glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H(+) + UDP;
Xref=Rhea:RHEA:14789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57265,
ChEBI:CHEBI:57705, ChEBI:CHEBI:57880, ChEBI:CHEBI:58223;
EC=2.4.1.198;
-!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-
anchor biosynthesis.
-!- SUBUNIT: Associates with PIGA, PIGC, PIGH, PIGP and DPM2. The
latter is not essential for activity.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9BRB3-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q9BRB3-2; Sequence=VSP_007281, VSP_007282;
Name=3;
IsoId=Q9BRB3-3; Sequence=VSP_007279, VSP_007280;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the PIGQ family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF030177; AAC32661.1; -; mRNA.
EMBL; AB003723; BAA24948.1; -; mRNA.
EMBL; AE006464; AAK61235.1; -; Genomic_DNA.
EMBL; Z98883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85796.1; -; Genomic_DNA.
EMBL; CH471112; EAW85797.1; -; Genomic_DNA.
EMBL; CH471112; EAW85799.1; -; Genomic_DNA.
EMBL; BC006377; AAH06377.1; -; mRNA.
EMBL; BC010094; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS10411.1; -. [Q9BRB3-1]
CCDS; CCDS10412.1; -. [Q9BRB3-2]
RefSeq; NP_004195.2; NM_004204.3. [Q9BRB3-2]
RefSeq; NP_683721.1; NM_148920.2. [Q9BRB3-1]
UniGene; Hs.741878; -.
UniGene; Hs.744949; -.
ProteinModelPortal; Q9BRB3; -.
BioGrid; 114545; 23.
CORUM; Q9BRB3; -.
IntAct; Q9BRB3; 4.
MINT; Q9BRB3; -.
STRING; 9606.ENSP00000026218; -.
iPTMnet; Q9BRB3; -.
PhosphoSitePlus; Q9BRB3; -.
BioMuta; PIGQ; -.
DMDM; 30173119; -.
MaxQB; Q9BRB3; -.
PaxDb; Q9BRB3; -.
PeptideAtlas; Q9BRB3; -.
PRIDE; Q9BRB3; -.
ProteomicsDB; 78753; -.
ProteomicsDB; 78754; -. [Q9BRB3-2]
ProteomicsDB; 78755; -. [Q9BRB3-3]
DNASU; 9091; -.
Ensembl; ENST00000026218; ENSP00000026218; ENSG00000007541. [Q9BRB3-1]
Ensembl; ENST00000321878; ENSP00000326674; ENSG00000007541. [Q9BRB3-2]
Ensembl; ENST00000409527; ENSP00000386760; ENSG00000007541. [Q9BRB3-2]
Ensembl; ENST00000470411; ENSP00000439650; ENSG00000007541. [Q9BRB3-3]
GeneID; 9091; -.
KEGG; hsa:9091; -.
UCSC; uc002chm.4; human. [Q9BRB3-1]
CTD; 9091; -.
DisGeNET; 9091; -.
EuPathDB; HostDB:ENSG00000007541.15; -.
GeneCards; PIGQ; -.
HGNC; HGNC:14135; PIGQ.
HPA; HPA039105; -.
HPA; HPA039828; -.
HPA; HPA061414; -.
MalaCards; PIGQ; -.
MIM; 605754; gene.
neXtProt; NX_Q9BRB3; -.
OpenTargets; ENSG00000007541; -.
Orphanet; 1934; Early infantile epileptic encephalopathy.
PharmGKB; PA33299; -.
eggNOG; KOG1183; Eukaryota.
eggNOG; ENOG410XSXI; LUCA.
GeneTree; ENSGT00390000004994; -.
HOVERGEN; HBG036559; -.
InParanoid; Q9BRB3; -.
KO; K03860; -.
OrthoDB; EOG091G0K98; -.
PhylomeDB; Q9BRB3; -.
TreeFam; TF321258; -.
BRENDA; 2.4.1.198; 2681.
Reactome; R-HSA-162710; Synthesis of glycosylphosphatidylinositol (GPI).
UniPathway; UPA00196; -.
ChiTaRS; PIGQ; human.
GeneWiki; PIGQ; -.
GenomeRNAi; 9091; -.
PRO; PR:Q9BRB3; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000007541; Expressed in 137 organ(s), highest expression level in adult mammalian kidney.
CleanEx; HS_PIGQ; -.
ExpressionAtlas; Q9BRB3; baseline and differential.
Genevisible; Q9BRB3; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
GO; GO:0016254; P:preassembly of GPI anchor in ER membrane; TAS:Reactome.
InterPro; IPR007720; GlcNAc_Gpi1.
PANTHER; PTHR21329; PTHR21329; 1.
Pfam; PF05024; Gpi1; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Glycosyltransferase; GPI-anchor biosynthesis; Membrane; Polymorphism;
Reference proteome; Transferase; Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10944123}.
CHAIN 2 760 Phosphatidylinositol N-
acetylglucosaminyltransferase subunit Q.
/FTId=PRO_0000215664.
TRANSMEM 278 298 Helical. {ECO:0000255}.
TRANSMEM 349 371 Helical. {ECO:0000255}.
TRANSMEM 378 400 Helical. {ECO:0000255}.
TRANSMEM 446 468 Helical. {ECO:0000255}.
TRANSMEM 475 497 Helical. {ECO:0000255}.
COMPBIAS 214 536 Leu-rich.
VAR_SEQ 275 299 KANTVASVLLDVALGLMLLSWLHGR -> CGPALVSAGLGA
CPLAPSPSPSAPR (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_007279.
VAR_SEQ 300 760 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_007280.
VAR_SEQ 511 581 DKPTALQPRGAHLPPPQLWLPPQALLGRPVPQAVPWGAHLP
LEAERGQAGLRELLARLAPPHGHSQPSALP -> AGVKFRV
LRHEAGRPLRLLMQINPLPYSRVVHTYRLPSCGCHPKHSWG
ALCRKLFLGELIYPWRQRGDKQD (in isoform 2).
{ECO:0000303|PubMed:9463366,
ECO:0000303|PubMed:9729469}.
/FTId=VSP_007281.
VAR_SEQ 582 760 Missing (in isoform 2).
{ECO:0000303|PubMed:9463366,
ECO:0000303|PubMed:9729469}.
/FTId=VSP_007282.
VARIANT 14 14 T -> A (in dbSNP:rs2071979).
{ECO:0000269|PubMed:11157797,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_015596.
VARIANT 592 592 C -> R (in dbSNP:rs1045277).
/FTId=VAR_053579.
VARIANT 668 668 C -> R (in dbSNP:rs710924).
/FTId=VAR_053580.
VARIANT 668 668 C -> Y (in dbSNP:rs710925).
/FTId=VAR_053581.
SEQUENCE 760 AA; 84082 MW; DBF900ADCE08DA98 CRC64;
MVLKAFFPTC CVSTDSGLLV GRWVPEQSSA VVLAVLHFPF IPIQVKQLLA QVRQASQVGV
AVLGTWCHCR QEPEESLGRF LESLGAVFPH EPWLRLCRER GGTFWSCEAT HRQAPTAPGA
PGEDQVMLIF YDQRQVLLSQ LHLPTVLPDR QAGATTASTG GLAAVFDTVA RSEVLFRSDR
FDEGPVRLSH WQSEGVEASI LAELARRASG PICLLLASLL SLVSAVSACR VFKLWPLSFL
GSKLSTCEQL RHRLEHLTLI FSTRKAENPA QLMRKANTVA SVLLDVALGL MLLSWLHGRS
RIGHLADALV PVADHVAEEL QHLLQWLMGA PAGLKMNRAL DQVLGRFFLY HIHLWISYIH
LMSPFVEHIL WHVGLSACLG LTVALSLLSD IIALLTFHIY CFYVYGARLY CLKIHGLSSL
WRLFRGKKWN VLRQRVDSCS YDLDQLFIGT LLFTILLFLL PTTALYYLVF TLLRLLVVAV
QGLIHLLVDL INSLPLYSLG LRLCRPYRLA DKPTALQPRG AHLPPPQLWL PPQALLGRPV
PQAVPWGAHL PLEAERGQAG LRELLARLAP PHGHSQPSAL PGWHQLSWRM SCALWTLLCA
PEHGRPCYHT LGLEVIGSEQ MWGWPARLAA LHHWHCLPWD PLPTCCGHHG GEHSNPRCPE
HCPMPTLCTQ VQRVRPPQQP QVEGWSPWGL PSGSALAVGV EGPCQDEPPS PRHPLAPSAE
QHPASGGLKQ SLTPVPSGPG PSLPEPHGVY LRMFPGEVAL


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