GPI2_YEAST
ID GPI2_YEAST Reviewed; 280 AA.
AC P46961; D6W3U0; P48014;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit;
DE Short=GPI-GlcNAc transferase complex subunit GPI2;
DE Short=GPI-GnT subunit GPI2;
DE EC=2.4.1.198;
GN Name=GPI2; Synonyms=GCR4; OrderedLocusNames=YPL076W; ORFNames=LPF9W;
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=7768896; DOI=10.1074/jbc.270.22.13029;
RA Leidich S.D., Kostova Z., Latek R.R., Costello L.C., Drapp D.A., Gray W.,
RA Fassler J.S., Orlean P.;
RT "Temperature-sensitive yeast GPI anchoring mutants gpi2 and gpi3 are
RT defective in the synthesis of N-acetylglucosaminyl phosphatidylinositol.
RT Cloning of the GPI2 gene.";
RL J. Biol. Chem. 270:13029-13035(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=7502585; DOI=10.1002/yea.320111111;
RA Uemura H., Jigami Y.;
RT "A new essential gene GCR4 located in the upstream region of GCR1.";
RL Yeast 11:1093-1101(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP INTERACTION WITH ERI1.
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 [7]
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:7768896}.
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:7768896}.
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 (Probable).
CC Interacts with ERI1 (PubMed:15163411). {ECO:0000269|PubMed:15163411,
CC ECO:0000305|PubMed:15163411}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PIGC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA79518.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U23788; AAA79518.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D29645; BAA06128.1; -; Genomic_DNA.
DR EMBL; U41849; AAB68262.1; -; Genomic_DNA.
DR EMBL; AY692961; AAT92980.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11356.1; -; Genomic_DNA.
DR PIR; S61111; S61111.
DR RefSeq; NP_015249.1; NM_001183890.1.
DR AlphaFoldDB; P46961; -.
DR BioGRID; 36104; 603.
DR ComplexPortal; CPX-1274; Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex.
DR DIP; DIP-4023N; -.
DR IntAct; P46961; 16.
DR MINT; P46961; -.
DR STRING; 4932.YPL076W; -.
DR MaxQB; P46961; -.
DR PaxDb; P46961; -.
DR PRIDE; P46961; -.
DR EnsemblFungi; YPL076W_mRNA; YPL076W; YPL076W.
DR GeneID; 856029; -.
DR KEGG; sce:YPL076W; -.
DR SGD; S000005997; GPI2.
DR VEuPathDB; FungiDB:YPL076W; -.
DR eggNOG; KOG3059; Eukaryota.
DR GeneTree; ENSGT00390000005496; -.
DR HOGENOM; CLU_024002_2_0_1; -.
DR InParanoid; P46961; -.
DR OMA; HAFVMVT; -.
DR BioCyc; YEAST:G3O-33983-MON; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:P46961; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P46961; 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; IPI:SGD.
DR GO; GO:0016021; C:integral component of membrane; ISM:SGD.
DR GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IC:SGD.
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; IPR009450; Plno_GlcNAc_GPI2.
DR PANTHER; PTHR12982; PTHR12982; 1.
DR Pfam; PF06432; GPI2; 1.
DR PIRSF; PIRSF016104; GPI2; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; GPI-anchor biosynthesis; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..280
FT /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT GPI2 subunit"
FT /id="PRO_0000087558"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..135
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 48
FT /note="A -> R (in Ref. 1; AAA79518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 32577 MW; 2BFEE04E913918DB CRC64;
MTRSPWKRLL WLKQEYPDNY TDPSFIELRA RQKAESNQKS DRKLSEAARA QIRLDFISFY
QTILNTSFIY ITFTYIYYYG FDPIPPTIFL SFITLIISRT KVDPLLSSFM DVKSSLIITF
AMLTLSPVLK SLSKTTASDS IWTLSFWLTL WYIFVISSTK SKDKPSNLST NILVALVAVL
SSRLSTTIDV FCFLLICIQL NIILPTYLSV TNKVVPIISN IIVYSFLNVA LGWIYMLLIF
FASVFYITVL PKWFIYWKIN YHKRDNDLLS TWDARTPILD
