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   27-MAR-2024, entry version 160.
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.ENSMUSP00000107874; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   iPTMnet; Q64323; -.
DR   PhosphoSitePlus; Q64323; -.
DR   PaxDb; 10090-ENSMUSP00000033754; -.
DR   ProteomicsDB; 287718; -.
DR   Antibodypedia; 23929; 235 antibodies from 29 providers.
DR   DNASU; 18700; -.
DR   Ensembl; ENSMUST00000033754.15; ENSMUSP00000033754.8; ENSMUSG00000031381.17.
DR   Ensembl; ENSMUST00000112255.8; ENSMUSP00000107874.2; ENSMUSG00000031381.17.
DR   GeneID; 18700; -.
DR   KEGG; mmu:18700; -.
DR   UCSC; uc009uvo.1; mouse.
DR   AGR; MGI:99461; -.
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; QCVLPTM; -.
DR   OrthoDB; 24420at2759; -.
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 80 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 237 other cell types or tissues.
DR   ExpressionAtlas; Q64323; baseline and differential.
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: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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR039507; PIG-A/GPI3.
DR   InterPro; IPR013234; PIGA_GPI_anchor_biosynthesis.
DR   PANTHER; PTHR45871; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL BIOSYNTHETIC PROTEIN; 1.
DR   PANTHER; PTHR45871:SF1; PHOSPHATIDYLINOSITOL N-ACETYLGLUCOSAMINYLTRANSFERASE SUBUNIT A; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF08288; PIGA; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   Genevisible; Q64323; MM.
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
//