ERI1_YEAST
ID ERI1_YEAST Reviewed; 68 AA.
AC P62651; D6W3S0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit;
DE Short=GPI-GlcNAc transferase complex subunit ERI1;
DE Short=GPI-GnT subunit ERI1;
DE AltName: Full=Endoplasmic reticulum-associated Ras inhibitor protein 1;
GN Name=ERI1; Synonyms=RIN1; OrderedLocusNames=YPL096C-A;
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 [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 [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAS2, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12832483; DOI=10.1128/mcb.23.14.4983-4990.2003;
RA Sobering A.K., Romeo M.J., Vay H.A., Levin D.E.;
RT "A novel Ras inhibitor, Eri1, engages yeast Ras at the endoplasmic
RT reticulum.";
RL Mol. Cell. Biol. 23:4983-4990(2003).
RN [4]
RP FUNCTION, AND INTERACTION WITH GPI2.
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).
CC -!- FUNCTION: Probable component of the GPI-GlcNAc transferase (GPI-GnT)
CC complex in the endoplasmic reticulum, a complex that catalyzes transfer
CC of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the
CC first step in the production of GPI-anchors for cell surface proteins.
CC Ras may inhibit the enzyme activity of the GPI-GnT complex via the
CC association between ERI1 and RAS2. {ECO:0000269|PubMed:12832483,
CC ECO:0000269|PubMed:15163411}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000305|PubMed:12832483}.
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 GPI2 (PubMed:15163411). Interacts with GTP-bound RAS2 in
CC an effector loop-dependent manner (PubMed:12832483).
CC {ECO:0000269|PubMed:12832483, ECO:0000269|PubMed:15163411,
CC ECO:0000305|PubMed:12832483}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12832483}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12832483}.
CC -!- DISRUPTION PHENOTYPE: Defects cause hyperactive Ras phenotypes,
CC probably due to diminished GPI-anchor protein production.
CC {ECO:0000269|PubMed:12832483}.
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DR EMBL; U43281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006949; DAA11336.1; -; Genomic_DNA.
DR RefSeq; NP_690846.1; NM_001184515.1.
DR AlphaFoldDB; P62651; -.
DR BioGRID; 36084; 185.
DR ComplexPortal; CPX-1274; Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex.
DR IntAct; P62651; 1.
DR STRING; 4932.YPL096C-A; -.
DR PaxDb; P62651; -.
DR EnsemblFungi; YPL096C-A_mRNA; YPL096C-A; YPL096C-A.
DR GeneID; 856008; -.
DR KEGG; sce:YPL096C-A; -.
DR SGD; S000028423; ERI1.
DR VEuPathDB; FungiDB:YPL096C-A; -.
DR eggNOG; ENOG502SXJV; Eukaryota.
DR HOGENOM; CLU_190860_0_0_1; -.
DR InParanoid; P62651; -.
DR OMA; WALIAWC; -.
DR BioCyc; YEAST:G3O-34360-MON; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:P62651; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P62651; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IPI:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005095; F:GTPase inhibitor activity; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IC:ComplexPortal.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR GO; GO:0007265; P:Ras protein signal transduction; IMP:SGD.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..68
FT /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT ERI1 subunit"
FT /id="PRO_0000087028"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 68 AA; 8039 MW; 1F359D0FA63F5F54 CRC64;
MRPRDQGFLV LGFTYSVLLI SLATFYWLRN NDSFLHYWCV LLLCPATLWL WALIAWCDSE
MFASSKDE
