GPI1_YEAST
ID GPI1_YEAST Reviewed; 609 AA.
AC P53306; D6VUZ9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1;
DE Short=GPI-GlcNAc transferase complex subunit GPI1;
DE Short=GPI-GnT subunit GPI1;
DE EC=2.4.1.198;
GN Name=GPI1; OrderedLocusNames=YGR216C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8910381; DOI=10.1074/jbc.271.44.27829;
RA Leidich S.D., Orlean P.;
RT "Gpi1, a Saccharomyces cerevisiae protein that participates in the first
RT step in glycosylphosphatidylinositol anchor synthesis.";
RL J. Biol. Chem. 271:27829-27837(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PROBABLE COMPOSITION OF THE COMPLEX.
RX PubMed=15163411; DOI=10.1016/j.cell.2004.05.003;
RA Sobering A.K., Watanabe R., Romeo M.J., Yan B.C., Specht C.A., Orlean P.,
RA Riezman H., Levin D.E.;
RT "Yeast Ras regulates the complex that catalyzes the first step in GPI-
RT anchor biosynthesis at the ER.";
RL Cell 117:637-648(2004).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Part of the complex catalyzing the transfer of N-
CC acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol,
CC the first step of GPI biosynthesis. {ECO:0000269|PubMed:8910381}.
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 -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000305|PubMed:8910381}.
CC -!- SUBUNIT: Component of the phosphatidylinositol N-
CC acetylglucosaminyltransferase (GPI-GlcNAc transferase) complex composed
CC of at least GPI1, GPI2, GPI3, GPI15, GPI19 and ERI1.
CC {ECO:0000305|PubMed:15163411}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PIGQ family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U66864; AAB17870.1; -; Genomic_DNA.
DR EMBL; Z73001; CAA97243.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08310.1; -; Genomic_DNA.
DR PIR; S64539; S64539.
DR RefSeq; NP_011732.1; NM_001181345.1.
DR AlphaFoldDB; P53306; -.
DR BioGRID; 33469; 148.
DR ComplexPortal; CPX-1274; Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex.
DR DIP; DIP-7773N; -.
DR IntAct; P53306; 2.
DR MINT; P53306; -.
DR STRING; 4932.YGR216C; -.
DR MaxQB; P53306; -.
DR PaxDb; P53306; -.
DR PRIDE; P53306; -.
DR EnsemblFungi; YGR216C_mRNA; YGR216C; YGR216C.
DR GeneID; 853130; -.
DR KEGG; sce:YGR216C; -.
DR SGD; S000003448; GPI1.
DR VEuPathDB; FungiDB:YGR216C; -.
DR eggNOG; KOG1183; Eukaryota.
DR GeneTree; ENSGT00390000004994; -.
DR HOGENOM; CLU_007914_3_0_1; -.
DR InParanoid; P53306; -.
DR OMA; NSIWLIF; -.
DR BioCyc; YEAST:G3O-30898-MON; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:P53306; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53306; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IGI:SGD.
DR GO; GO:0016021; C:integral component of membrane; ISM:SGD.
DR GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031505; P:fungal-type cell wall organization; IC:ComplexPortal.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:SGD.
DR InterPro; IPR007720; PigQ/GPI1.
DR PANTHER; PTHR21329; PTHR21329; 1.
DR Pfam; PF05024; Gpi1; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; GPI-anchor biosynthesis; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..609
FT /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT subunit GPI1"
FT /id="PRO_0000215666"
FT TOPO_DOM 1..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..380
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..485
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 609 AA; 70354 MW; 24BE9884EEC0E478 CRC64;
MPNYIFWPYE SLFENSAAQG PQVALAISFE KTHFVVLGVC EPQYLEEVSI RPPYSVVATK
NNGAEGWNYK VADPCNVHFR IPKLKFMQFY SSDPISLIIP EKEVGLHSSV GETLNYSKLE
QHPRYKRDNK KLSETLNIIN LFPAYCKALN ELYPFIQTSQ ENLRGTMLNS VAAWCSSTCI
YKMVAKIGFY LTFVICSIAS LVSSLLNYSH FQLVNYSAFV QQIDLRCQQI CYFPVQYERI
NKKDNIQNVG SMVEKDNSNS QFSHSYMPSK FYPDYILLYN TIWLIINDIS FGLILGAILI
ENRDFLVSAS HRVLKFFLYD SLKTITETLA NNPLGIKLNA ELANFLSELF LWVIEFSYTT
FIKRLIDPKT LSSLLTLTIY MMFLVGFSFA VSLAIDFFAI LSFPIYVFYR ISSKLYHCQL
NIMASLFNLF CGKKRNVLRN RIDHNYFQLD QLLLGTLLFI ILVFLTPTVM AFYMSYTVLR
MLTITIEIFS EAVIALINHF PLFALLLRLK DPKRLPGGIS IELKTTVSNK HTTLELQNNP
IKFKSMFRPY NLLLSQMRTN YFSFATVRKI VRGESIMVNR NKLYYVLYSS LPSKPLSVKD
LYKRLTIQA
