PIGA_MOUSE
ID PIGA_MOUSE Reviewed; 485 AA.
AC Q64323; Q6LD71; Q8CCQ6;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit A {ECO:0000305};
DE EC=2.4.1.198 {ECO:0000250|UniProtKB:P37287};
DE AltName: Full=GlcNAc-PI synthesis protein;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class A protein;
DE Short=PIG-A;
GN Name=Piga {ECO:0000312|MGI:MGI:99461};
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 [GENOMIC DNA / MRNA].
RC STRAIN=129S/V;
RX PubMed=7851884; DOI=10.1006/geno.1994.1544;
RA Kawagoe K., Takeda J., Endo Y., Kinoshita T.;
RT "Molecular cloning of murine pig-a, a gene for GPI-anchor biosynthesis, and
RT demonstration of interspecies conservation of its structure, function, and
RT genetic locus.";
RL Genomics 23:566-574(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7734452; DOI=10.1016/0005-2760(95)00015-5;
RA Yu J., Nagarajan S., Liu J., Young N., Medof M.E.;
RT "Cloning and characterization of the mouse PIG-A gene.";
RL Biochim. Biophys. Acta 1255:344-350(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Catalytic subunit 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:P37287}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + UDP-N-
CC acetyl-alpha-D-glucosamine = a 6-(N-acetyl-alpha-D-glucosaminyl)-1-
CC phosphatidyl-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:14789,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57265, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58223; EC=2.4.1.198;
CC Evidence={ECO:0000250|UniProtKB:P37287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14790;
CC Evidence={ECO:0000250|UniProtKB:P37287};
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000250|UniProtKB:P37287}.
CC -!- SUBUNIT: Component of the glycosylphosphatidylinositol-N-
CC acetylglucosaminyltransferase (GPI-GnT) complex composed at least by
CC PIGA, PIGC, PIGH, PIGP and PIGQ, DPM2. Interacts with PIGC, PIGH, PIGP,
CC PIGQ and DPM2. The latter is not essential for activity. Interacts
CC directly with PIGY; this interaction regulates
CC glycosylphosphatidylinositol-N-acetylglucosaminyltransferase activity.
CC Interacts with PIGQ. {ECO:0000250|UniProtKB:P37287}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; D31863; BAA06663.1; -; Genomic_DNA.
DR EMBL; D26047; BAA05047.1; -; mRNA.
DR EMBL; S78188; AAP32009.1; -; mRNA.
DR EMBL; AK032283; BAC27792.1; -; mRNA.
DR CCDS; CCDS30522.1; -.
DR PIR; A55731; A55731.
DR PIR; I52484; I52484.
DR RefSeq; NP_035211.2; NM_011081.2.
DR RefSeq; XP_017173917.1; XM_017318428.1.
DR AlphaFoldDB; Q64323; -.
DR SMR; Q64323; -.
DR ELM; Q64323; -.
DR STRING; 10090.ENSMUSP00000033754; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; Q64323; -.
DR PhosphoSitePlus; Q64323; -.
DR PaxDb; Q64323; -.
DR PRIDE; Q64323; -.
DR ProteomicsDB; 287718; -.
DR Antibodypedia; 23929; 214 antibodies from 29 providers.
DR DNASU; 18700; -.
DR Ensembl; ENSMUST00000033754; ENSMUSP00000033754; ENSMUSG00000031381.
DR Ensembl; ENSMUST00000112255; ENSMUSP00000107874; ENSMUSG00000031381.
DR GeneID; 18700; -.
DR KEGG; mmu:18700; -.
DR UCSC; uc009uvo.1; mouse.
DR CTD; 5277; -.
DR MGI; MGI:99461; Piga.
DR VEuPathDB; HostDB:ENSMUSG00000031381; -.
DR eggNOG; KOG1111; Eukaryota.
DR GeneTree; ENSGT00390000014405; -.
DR HOGENOM; CLU_009583_19_0_1; -.
DR InParanoid; Q64323; -.
DR OMA; FFCPNAG; -.
DR OrthoDB; 719531at2759; -.
DR PhylomeDB; Q64323; -.
DR TreeFam; TF105675; -.
DR BRENDA; 2.4.1.198; 3474.
DR Reactome; R-MMU-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 18700; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Piga; mouse.
DR PRO; PR:Q64323; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q64323; protein.
DR Bgee; ENSMUSG00000031381; Expressed in substantia propria of cornea and 233 other tissues.
DR ExpressionAtlas; Q64323; baseline and differential.
DR Genevisible; Q64323; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:HGNC-UCL.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; ISS:HGNC-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:MGI.
DR CDD; cd03796; GT4_PIG-A-like; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR039507; PIG-A/GPI3.
DR InterPro; IPR013234; PIGA_GPI_anchor_biosynthesis.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF08288; PIGA; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..485
FT /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT subunit A"
FT /id="PRO_0000080327"
FT TOPO_DOM 1..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..485
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37287"
FT CONFLICT 107
FT /note="F -> I (in Ref. 3; BAC27792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 54469 MW; 12141BB48A71A03A CRC64;
MANRRGGGQG QPPSVSPSPG SSGNLSDDRT CTHNICMVSD FFYPNMGGVE SHIYQLSQCL
IERGHKVITV THAYGNRKGV RYLTNGLKVY YLPLRVMYNQ STATTLFHSL PLLRYIFVRE
RITIIHSHSS FSAMAHDALF HAKTMGLQTV FTDHSLFGFA DVSSVLTNKL LTVSLCDTNH
IICVSYTSKE NTVLRAALNP EIVSVIPNAV DPTDFTPDPF RRHDSVITVV VVSRLVYRKG
TDLLSGIIPE LCQKYQELHF LIGGEGPKRI ILEEVRERYQ LHDRVQLLGA LEHKDVRNVL
VQGHIFLNTS LTEAFCMAIV EAASCGLQVV STKVGGIPEV LPESLIILCE PSVKSLCDGL
EKAIFQVKSG TLPAPENIHN VVKTFYTWRN VAERTEKVYE RVSKETVLPM HKRLDRLISH
CGPVTGYMFA LLAVLSYLFL IFLQWMTPDS FIDVAIDATG PRRAWTHQWP RDKKRDENDK
ISQSR
