Reviewed, UniProtKB/Swiss-Prot P46961 (GPI2_YEAST)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit
    EC=2.4.1.198

Gene names

Name:	GPI2
Synonyms:	GCR4
Ordered Locus Names:	YPL076W
ORF Names:	LPF9W

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

General annotation (Comments)

Function	Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Catalytic activity	UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol.
Pathway	Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subunit structure	Component of a complex with GPI1, GPI2, GPI3, GPI15 and ERI1 Probable. Interacts with ERI1.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Sequence similarities	Belongs to the PIGC family.

Ontologies

Keywords
Biological process	GPI-anchor biosynthesis
Cellular component	Membrane
Domain	Transmembrane
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	GPI anchor biosynthetic process Ref.1 Inferred from direct assay. Source: SGD
Cellular component	glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Ref.5 Inferred from physical interaction. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	phosphatidylinositol N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC protein binding Ref.5 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERI1	P62651	1	EBI-7809,EBI-975247
GPI19	Q04082	1	EBI-7809,EBI-36611
RAS2	P01120	1	EBI-7809,EBI-14838

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 280	280	Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit		PRO_0000087558
Regions
	Topological domain	1 – 53	53	Cytoplasmic Potential
	Transmembrane	54 – 74	21	Potential
	Topological domain	75	1	Extracellular Potential
	Transmembrane	76 – 96	21	Potential
	Topological domain	97 – 108	12	Cytoplasmic Potential
	Transmembrane	109 – 129	21	Potential
	Topological domain	130 – 135	6	Extracellular Potential
	Transmembrane	136 – 156	21	Potential
	Topological domain	157 – 189	33	Cytoplasmic Potential
	Transmembrane	190 – 210	21	Potential
	Topological domain	211 – 220	10	Extracellular Potential
	Transmembrane	221 – 241	21	Potential
	Topological domain	242 – 280	39	Cytoplasmic Potential
Experimental info
	Sequence conflict	48	1	A → R in AAA79518. Ref.1
	Sequence conflict	239 – 280	42	IFFAS…TPILD → FSLLQYFILQFYLSGSSTGK SIIINGITIY Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P46961-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 2BFEE04E913918DB	FASTA	280	32,577
	10 20 30 40 50 60 MTRSPWKRLL WLKQEYPDNY TDPSFIELRA RQKAESNQKS DRKLSEAARA QIRLDFISFY 70 80 90 100 110 120 QTILNTSFIY ITFTYIYYYG FDPIPPTIFL SFITLIISRT KVDPLLSSFM DVKSSLIITF 130 140 150 160 170 180 AMLTLSPVLK SLSKTTASDS IWTLSFWLTL WYIFVISSTK SKDKPSNLST NILVALVAVL 190 200 210 220 230 240 SSRLSTTIDV FCFLLICIQL NIILPTYLSV TNKVVPIISN IIVYSFLNVA LGWIYMLLIF 250 260 270 280 FASVFYITVL PKWFIYWKIN YHKRDNDLLS TWDARTPILD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Temperature-sensitive yeast GPI anchoring mutants gpi2 and gpi3 are defective in the synthesis of N-acetylglucosaminyl phosphatidylinositol. Cloning of the GPI2 gene." Leidich S.D., Kostova Z., Latek R.R., Costello L.C., Drapp D.A., Gray W., Fassler J.S., Orlean P. J. Biol. Chem. 270:13029-13035(1995) [PubMed: 7768896] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A new essential gene GCR4 located in the upstream region of GCR1." Uemura H., Jigami Y. Yeast 11:1093-1101(1995) [PubMed: 7502585] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88.
[3]	"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.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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: INTERACTION WITH ERI1.
[6]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U23788 Genomic DNA. Translation: AAA79518.1. D29645 Genomic DNA. Translation: BAA06128.1. U41849 Genomic DNA. Translation: AAB68262.1. AY692961 Genomic DNA. Translation: AAT92980.1.
PIR	S61111.
RefSeq	NP_015249.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4023N.
IntAct	P46961. 7 interactions.
STRING	P46961.
Genome annotation databases
Ensembl	YPL076W; YPL076W; YPL076W; Saccharomyces cerevisiae. [Genome view]
GeneID	856029.
GenomeReviews	Gene locus YPL076W in contig U00094_GR.
KEGG	sce:YPL076W.
NMPDR	fig|4932.3.peg.6382.
Organism-specific databases
CYGD	YPL076w.
SGD	S000005997. GPI2.
Phylogenomic databases
HOGENOM	P46961.
OMA	FCFLLIC.
Enzyme and pathway databases
BRENDA	2.4.1.198. 250.
Gene expression databases
ArrayExpress	P46961.
Genevestigator	P46961.
GermOnline	YPL076W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR009450. Plno_GlcNAc_GPI2. [Graphical view]
PANTHER	PTHR12982. GPI2. 1 hit.
Pfam	PF06432. GPI2. 1 hit. [Graphical view]
PIRSF	PIRSF016104. GPI2. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	980950.

Entry information

Entry name

GPI2_YEAST

Accession

Primary (citable) accession number: P46961
Secondary accession number(s): P48014

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	February 1, 1996
Last modified:	November 3, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)