Reviewed, UniProtKB/Swiss-Prot P62651 (ERI1_YEAST)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit
Alternative name(s):
    Endoplasmic reticulum-associated Ras inhibitor protein 1

Gene names

Name:	ERI1
Synonyms:	RIN1
Ordered Locus Names:	YPL096C-A

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	68 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probable component of the GPI-GlcNAc transferase (GPI-GnT) complex in the endoplasmic reticulum, a complex that catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI-anchors for cell surface proteins. Ras may inhibit the enzyme activity of the GPI-GnT complex via the association between ERI1 and RAS2. Ref.2 Ref.3
Pathway	Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subunit structure	Interacts with GTP-bound RAS2 in an effector loop-dependent manner. Interacts with GPI2, suggesting that it is a component of the GPI-GnT complex, probably composed of GPI1, GPI2, GPI3, GPI15 and ERI1. Ref.2 Ref.3
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Disruption phenotype	Defects cause hyperactive Ras phenotypes, probably due to diminished GPI-anchor protein production. Ref.2

Ontologies

Keywords
Biological process	GPI-anchor biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	GPI anchor biosynthetic process Ref.3 Inferred from mutant phenotype. Source: SGD Ras protein signal transduction Ref.2 Inferred from mutant phenotype. Source: SGD
Cellular component	endoplasmic reticulum membrane Ref.2 Inferred from direct assay. Source: SGD glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Ref.3 Inferred from physical interaction. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTPase inhibitor activity Ref.2 Inferred from physical interaction. Source: SGD protein binding Ref.3 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GPI2	P46961	1	EBI-975247,EBI-7809

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 68	68	Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit		PRO_0000087028
Regions
	Transmembrane	8 – 28	21	Potential
	Transmembrane	34 – 54	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	P62651-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 1F359D0FA63F5F54	FASTA	68	8,039
	10 20 30 40 50 60 MRPRDQGFLV LGFTYSVLLI SLATFYWLRN NDSFLHYWCV LLLCPATLWL WALIAWCDSE MFASSKDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"A novel Ras inhibitor, Eri1, engages yeast Ras at the endoplasmic reticulum." Sobering A.K., Romeo M.J., Vay H.A., Levin D.E. Mol. Cell. Biol. 23:4983-4990(2003) [PubMed: 12832483] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAS2, DISRUPTION PHENOTYPE.
[3]	"Yeast Ras regulates the complex that catalyzes the first step in GPI-anchor biosynthesis at the ER." Sobering A.K., Watanabe R., Romeo M.J., Yan B.C., Specht C.A., Orlean P., Riezman H., Levin D.E. Cell 117:637-648(2004) [PubMed: 15163411] [Abstract] Cited for: FUNCTION, INTERACTION WITH GPI2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U43281 Genomic DNA. No translation available.
RefSeq	NP_690846.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P62651. 2 interactions.
STRING	P62651.
Genome annotation databases
Ensembl	YPL096C-A; YPL096C-A; YPL096C-A; Saccharomyces cerevisiae. [Genome view]
GeneID	856008.
KEGG	sce:YPL096C-A.
NMPDR	fig|4932.3.peg.6361.
Organism-specific databases
CYGD	YPL096c-a.
SGD	S000028423. ERI1.
Phylogenomic databases
HOGENOM	P62651.
OMA	DSEMFAS
OrthoDB	EOG95TF52
Gene expression databases
ArrayExpress	P62651.
Genevestigator	P62651.
GermOnline	YPL096C-A. Saccharomyces cerevisiae.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	980890.

Entry information

Entry name

ERI1_YEAST

Accession

Primary (citable) accession number: P62651

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	November 24, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)