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Protein

Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit

Gene

SPT14

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.2 Publications

Catalytic activityi

UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol.

Enzyme regulationi

Inhibited by Ras, probably via the interaction between RAS2 and ERI1.1 Publication

Pathwayi

GO - Molecular functioni

  1. phosphatidylinositol N-acetylglucosaminyltransferase activity Source: SGD

GO - Biological processi

  1. GPI anchor biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

GPI-anchor biosynthesis

Enzyme and pathway databases

BioCyciYEAST:G3O-34070-MONOMER.
UniPathwayiUPA00196.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit (EC:2.4.1.198)
Alternative name(s):
GlcNAc-PI synthesis protein
Gene namesi
Name:SPT14
Synonyms:CWH6, GPI3
Ordered Locus Names:YPL175W
ORF Names:P2269
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

SGDiS000006096. SPT14.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei407 – 42721HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: SGD
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Source: SGD
  4. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi289 – 2891E → A: Severe growth defect. 1 Publication
Mutagenesisi289 – 2891E → D: Reduces the transferase reaction 12-fold. 1 Publication
Mutagenesisi289 – 2891E → G: Lethal. 1 Publication
Mutagenesisi297 – 2971E → A or G: Lethal. 1 Publication
Mutagenesisi297 – 2971E → D: No transferase activity. 1 Publication
Mutagenesisi301 – 3011C → A: Reduces the transferase reaction 5-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 452452Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunitPRO_0000080325Add
BLAST

Proteomic databases

MaxQBiP32363.
PaxDbiP32363.
PeptideAtlasiP32363.
PRIDEiP32363.

Expressioni

Gene expression databases

GenevestigatoriP32363.

Interactioni

Subunit structurei

Component of the phosphatidylinositol N-acetylglucosaminyltransferase complex composed of at least GPI1, GPI2, GPI3, GPI15, GPI19 and ERI1.

Protein-protein interaction databases

BioGridi36008. 62 interactions.
DIPiDIP-1834N.
IntActiP32363. 1 interaction.
MINTiMINT-385729.
STRINGi4932.YPL175W.

Structurei

3D structure databases

ProteinModelPortaliP32363.
SMRiP32363. Positions 17-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0438.
GeneTreeiENSGT00390000014405.
HOGENOMiHOG000203293.
InParanoidiP32363.
KOiK03857.
OMAiREKYQLH.
OrthoDBiEOG7ZGXCR.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
IPR013234. PIGA_GPI_anchor_biosynthesis.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 1 hit.
PF08288. PIGA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32363-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFNIAMLCD FFYPQLGGVE FHIYHLSQKL IDLGHSVVII THAYKDRVGV
60 70 80 90 100
RHLTNGLKVY HVPFFVIFRE TTFPTVFSTF PIIRNILLRE QIQIVHSHGS
110 120 130 140 150
ASTFAHEGIL HANTMGLRTV FTDHSLYGFN NLTSIWVNKL LTFTLTNIDR
160 170 180 190 200
VICVSNTCKE NMIVRTELSP DIISVIPNAV VSEDFKPRDP TGGTKRKQSR
210 220 230 240 250
DKIVIVVIGR LFPNKGSDLL TRIIPKVCSS HEDVEFIVAG DGPKFIDFQQ
260 270 280 290 300
MIESHRLQKR VQLLGSVPHE KVRDVLCQGD IYLHASLTEA FGTILVEAAS
310 320 330 340 350
CNLLIVTTQV GGIPEVLPNE MTVYAEQTSV SDLVQATNKA INIIRSKALD
360 370 380 390 400
TSSFHDSVSK MYDWMDVAKR TVEIYTNISS TSSADDKDWM KMVANLYKRD
410 420 430 440 450
GIWAKHLYLL CGIVEYMLFF LLEWLYPRDE IDLAPKWPKK TVSNETKEAR

ET
Length:452
Mass (Da):51,242
Last modified:June 16, 2009 - v4
Checksum:i7589FD815707EC73
GO

Sequence cautioni

The sequence CAA97882.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63290 Genomic DNA. Translation: CAA44924.1.
Z73531 Genomic DNA. Translation: CAA97882.1. Sequence problems.
BK006949 Genomic DNA. Translation: DAA11259.1.
PIRiS65187.
RefSeqiNP_015150.2. NM_001183989.1.

Genome annotation databases

EnsemblFungiiYPL175W; YPL175W; YPL175W.
GeneIDi855928.
KEGGisce:YPL175W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63290 Genomic DNA. Translation: CAA44924.1.
Z73531 Genomic DNA. Translation: CAA97882.1. Sequence problems.
BK006949 Genomic DNA. Translation: DAA11259.1.
PIRiS65187.
RefSeqiNP_015150.2. NM_001183989.1.

3D structure databases

ProteinModelPortaliP32363.
SMRiP32363. Positions 17-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36008. 62 interactions.
DIPiDIP-1834N.
IntActiP32363. 1 interaction.
MINTiMINT-385729.
STRINGi4932.YPL175W.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Proteomic databases

MaxQBiP32363.
PaxDbiP32363.
PeptideAtlasiP32363.
PRIDEiP32363.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL175W; YPL175W; YPL175W.
GeneIDi855928.
KEGGisce:YPL175W.

Organism-specific databases

SGDiS000006096. SPT14.

Phylogenomic databases

eggNOGiCOG0438.
GeneTreeiENSGT00390000014405.
HOGENOMiHOG000203293.
InParanoidiP32363.
KOiK03857.
OMAiREKYQLH.
OrthoDBiEOG7ZGXCR.

Enzyme and pathway databases

UniPathwayiUPA00196.
BioCyciYEAST:G3O-34070-MONOMER.

Miscellaneous databases

NextBioi980663.
PROiP32363.

Gene expression databases

GenevestigatoriP32363.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
IPR013234. PIGA_GPI_anchor_biosynthesis.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 1 hit.
PF08288. PIGA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "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] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE BINDING.
  8. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF INTRON.
  9. "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] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-289; GLU-297 AND CYS-301.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "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] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.

Entry informationi

Entry nameiGPI3_YEAST
AccessioniPrimary (citable) accession number: P32363
Secondary accession number(s): D6W3J3, Q08918
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: June 16, 2009
Last modified: February 4, 2015
This is version 126 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1480 molecules/cell in log phase SD medium.1 Publication

Caution

Was originally thought to be involved in transcription.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.