Reviewed, UniProtKB/Swiss-Prot P32363 (GPI3_YEAST)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
    EC=2.4.1.198
Alternative name(s):
    GlcNAc-PI synthesis protein

Gene names

Name:	SPT14
Synonyms:	CWH6, GPI3
Ordered Locus Names:	YPL175W
ORF Names:	P2269

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

General annotation (Comments)

Function	Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis. Ref.5 Ref.6
Catalytic activity	UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol.
Enzyme regulation	Inhibited by Ras, probably via the interaction between RAS2 and ERI1. Ref.10
Pathway	Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subunit structure	Component of the phosphatidylinositol N-acetylglucosaminyltransferase complex composed of at least GPI1, GPI2, GPI3, GPI15, GPI19 and ERI1.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein Potential.
Miscellaneous	Present with 1480 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the glycosyltransferase 1 family.
Caution	Was originally (Ref.1) thought to be involved in transcription.
Sequence caution	The sequence CAA97882.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	GPI-anchor biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	GPI anchor biosynthetic process Traceable author statement. Source: SGD
Cellular component	glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Traceable author statement. 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 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P38800	1	EBI-7815,EBI-24597

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 452	452	Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit		PRO_0000080325
Regions
	Transmembrane	407 – 427	21	Potential
Experimental info
	Mutagenesis	289	1	E → A: Severe growth defect. Ref.8
	Mutagenesis	289	1	E → D: Reduces the transferase reaction 12-fold. Ref.8
	Mutagenesis	289	1	E → G: Lethal. Ref.8
	Mutagenesis	297	1	E → A or G: Lethal. Ref.8
	Mutagenesis	297	1	E → D: No transferase activity. Ref.8
	Mutagenesis	301	1	C → A: Reduces the transferase reaction 5-fold. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P32363-1 [UniParc]. Last modified June 16, 2009. Version 4. Checksum: 7589FD815707EC73	FASTA	452	51,242
	10 20 30 40 50 60 MGFNIAMLCD FFYPQLGGVE FHIYHLSQKL IDLGHSVVII THAYKDRVGV RHLTNGLKVY 70 80 90 100 110 120 HVPFFVIFRE TTFPTVFSTF PIIRNILLRE QIQIVHSHGS ASTFAHEGIL HANTMGLRTV 130 140 150 160 170 180 FTDHSLYGFN NLTSIWVNKL LTFTLTNIDR VICVSNTCKE NMIVRTELSP DIISVIPNAV 190 200 210 220 230 240 VSEDFKPRDP TGGTKRKQSR DKIVIVVIGR LFPNKGSDLL TRIIPKVCSS HEDVEFIVAG 250 260 270 280 290 300 DGPKFIDFQQ MIESHRLQKR VQLLGSVPHE KVRDVLCQGD IYLHASLTEA FGTILVEAAS 310 320 330 340 350 360 CNLLIVTTQV GGIPEVLPNE MTVYAEQTSV SDLVQATNKA INIIRSKALD TSSFHDSVSK 370 380 390 400 410 420 MYDWMDVAKR TVEIYTNISS TSSADDKDWM KMVANLYKRD GIWAKHLYLL CGIVEYMLFF 430 440 450 LLEWLYPRDE IDLAPKWPKK TVSNETKEAR ET

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Saccharomyces cerevisiae SPT14 gene is essential for normal expression of the yeast transposon, Ty, as well as for expression of the HIS4 gene and several genes in the mating pathway." Fassler J.S., Gray W., Lee J.P., Yu G., Gingerich G. Mol. Gen. Genet. 230:310-320(1991) [PubMed: 1660567] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Fassler J.S. Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[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]	"The yeast spt14 gene is homologous to the human PIG-A gene and is required for GPI anchor synthesis." Schoenbaechler M., Horvath A., Fassler J.S., Riezman H. EMBO J. 14:1637-1645(1995) [PubMed: 7737116] [Abstract] Cited for: CHARACTERIZATION.
[5]	"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: FUNCTION.
[6]	"Photoaffinity labelling with P3-(4-azidoanilido)uridine 5'-triphosphate identifies gpi3p as the UDP-GlcNAc-binding subunit of the enzyme that catalyses formation of GlcNAc-phosphatidylinositol, the first glycolipid intermediate in glycosylphosphatidylinositol synthesis." Kostova Z., Rancour D.M., Menon A.K., Orlean P. Biochem. J. 350:815-822(2000) [PubMed: 10970797] [Abstract] Cited for: FUNCTION, SUBSTRATE BINDING.
[7]	"Test of intron predictions reveals novel splice sites, alternatively spliced mRNAs and new introns in meiotically regulated genes of yeast." Davis C.A., Grate L., Spingola M., Ares M. Jr. Nucleic Acids Res. 28:1700-1706(2000) [PubMed: 10734188] [Abstract] Cited for: IDENTIFICATION OF INTRON.
[8]	"Comparative importance in vivo of conserved glutamate residues in the EX7E motif retaining glycosyltransferase Gpi3p, the UDP-GlcNAc-binding subunit of the first enzyme in glycosylphosphatidylinositol assembly." Kostova Z., Yan B.C., Vainauskas S., Schwartz R., Menon A.K., Orlean P. Eur. J. Biochem. 270:4507-4514(2003) [PubMed: 14622279] [Abstract] Cited for: MUTAGENESIS OF GLU-289; GLU-297 AND CYS-301.
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"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: ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X63290 Genomic DNA. Translation: CAA44924.1. Z73531 Genomic DNA. Translation: CAA97882.1. Sequence problems.
PIR	S65187.
RefSeq	NP_015150.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1834N.
IntAct	P32363. 2 interactions.
STRING	P32363.
Protein family/group databases
CAZy	GT4. Glycosyltransferase Family 4.
Proteomic databases
PeptideAtlas	P32363.
Genome annotation databases
Ensembl	YPL175W; YPL175W; YPL175W; Saccharomyces cerevisiae. [Genome view]
GeneID	855928.
GenomeReviews	Gene locus YPL175W in contig U00094_GR.
KEGG	sce:YPL175W.
Organism-specific databases
CYGD	YPL175w.
SGD	S000006096. SPT14.
Phylogenomic databases
HOGENOM	P32363.
Enzyme and pathway databases
BRENDA	2.4.1.198. 250.
Gene expression databases
ArrayExpress	P32363.
Genevestigator	P32363.
GermOnline	YPL175W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001296. Glyco_trans_1. IPR013234. PIGA_GPI_anchor_biosynthesis. [Graphical view]
Pfam	PF00534. Glycos_transf_1. 1 hit. PF08288. PIGA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPI3_YEAST

Accession

Primary (citable) accession number: P32363
Secondary accession number(s): Q08918

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	June 16, 2009
Last modified:	October 13, 2009
This is version 80 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)