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P40009

- YND1_YEAST

UniProt

P40009 - YND1_YEAST

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Protein
Golgi apyrase
Gene
YND1, YER005W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates. Has equal high activity toward ADP/ATP, GDP/GTP, and UDP/UTP and approximately 50% less toward CDP/CTP and thiamine pyrophosphate. Has no activity toward GMP. Required for Golgi glycosylation and cell wall integrity. Together with CDC55, required for adenovirus E4orf4 (early region 4 open reading frame 4) induced toxicity, the apyrase activity is not required for this function. Plays a role in sphingolipid synthesis.3 Publications

Catalytic activityi

A nucleoside 5'-triphosphate + 2 H2O = a nucleoside 5'-phosphate + 2 phosphate.2 Publications

Cofactori

A divalent cation Ca2+, Mg2+ or Mn2+ By similarity.

Enzyme regulationi

Activity is inhibited both by interaction with VMA13 and by V-ATPase acidification of the lumen. The activity of VMA13 is not required for YND1 inhibition.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei152 – 1521Proton acceptor By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. nucleoside-diphosphatase activity Source: SGD
  3. nucleoside-triphosphatase activity Source: SGD

GO - Biological processi

  1. protein glycosylation Source: SGD
  2. sphingolipid metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:G3O-30192-MONOMER.
YEAST:G3O-30192-MONOMER.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Golgi apyrase (EC:3.6.1.5)
Alternative name(s):
ATP-diphosphatase
ATP-diphosphohydrolase
Adenosine diphosphatase
Short name:
ADPase
Golgi nucleoside diphosphatase
Yeast nucleoside diphosphatase 1
Gene namesi
Name:YND1
Ordered Locus Names:YER005W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome V

Organism-specific databases

CYGDiYER005w.
SGDiS000000807. YND1.

Subcellular locationi

Golgi apparatus. Membrane; Single-pass membrane protein Reviewed prediction 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 500500Lumenal Reviewed prediction
Add
BLAST
Transmembranei501 – 51717Helical; Reviewed prediction
Add
BLAST
Topological domaini518 – 630113Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: SGD
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells are partially resistant to E4orf4 and can partially suppress the spindle checkpoint defect in CDC55 deletion mutant. Does not suppress the rapamycin-resistance of CDC55 deletion mutant. YND1 and CDC55 double mutant is fully resistant to E4orf4. Deletion mutant suppresses the synthetic lethality of triple mutants, where UPC2 and ECM22 are knocked out along with either HAP1, ERG6 or ERG28.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi152 – 1521E → Q: Expressed at lower levels. GTPase activity reduced. 1 Publication
Mutagenesisi189 – 1891S → A: Expressed at the same level as wild-type. GTPase and GDPase activities decreased more than 20-fold toward GTP and 3-fold for GDP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 630630Golgi apyrase
PRO_0000209920Add
BLAST

Proteomic databases

MaxQBiP40009.
PaxDbiP40009.
PeptideAtlasiP40009.

Expressioni

Gene expression databases

GenevestigatoriP40009.

Interactioni

Subunit structurei

Interacts with activator subunit VMA13 of vacuolar H+-ATPase. Interacts with CDC55; this interaction is disrupted by adenovirus E4orf4, which remains associated with both YND1 and CDC55.2 Publications

Protein-protein interaction databases

BioGridi36735. 62 interactions.
DIPiDIP-7607N.
IntActiP40009. 7 interactions.
MINTiMINT-1354523.
STRINGi4932.YER005W.

Structurei

3D structure databases

ProteinModelPortaliP40009.
SMRiP40009. Positions 7-447.

Family & Domainsi

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5371.
GeneTreeiENSGT00550000074435.
HOGENOMiHOG000246725.
KOiK14642.
OMAiIGTSEYW.
OrthoDBiEOG7QK0PD.

Family and domain databases

InterProiIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERiPTHR11782. PTHR11782. 1 hit.
PfamiPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40009-1 [UniParc]FASTAAdd to Basket

« Hide

MLIENTNDRF GIVIDAGSSG SRIHVFKWQD TESLLHATNQ DSQSILQSVP    50
HIHQEKDWTF KLNPGLSSFE KKPQDAYKSH IKPLLDFAKN IIPESHWSSC 100
PVFIQATAGM RLLPQDIQSS ILDGLCQGLK HPAEFLVEDC SAQIQVIDGE 150
TEGLYGWLGL NYLYGHFNDY NPEVSDHFTF GFMDMGGAST QIAFAPHDSG 200
EIARHRDDIA TIFLRSVNGD LQKWDVFVST WLGFGANQAR RRYLAQLINT 250
LPENTNDYEN DDFSTRNLND PCMPRGSSTD FEFKDTIFHI AGSGNYEQCT 300
KSIYPLLLKN MPCDDEPCLF NGVHAPRIDF ANDKFIGTSE YWYTANDVFK 350
LGGEYNFDKF SKSLREFCNS NWTQILANSD KGVYNSIPEN FLKDACFKGN 400
WVLNILHEGF DMPRIDVDAE NVNDRPLFQS VEKVEERELS WTLGRILLYA 450
SGSILAGNDD FMVGIAPSER RTKLTGKKFI PGKLLESDQL RKQSSSLSNK 500
GFLMWFAIIC CIFYLIFHRS HIIRRRFSGL YNITKDFKTG IRRRLKFLRR 550
SDPFSRLEEG ELGTDVDGFK DVYRMKSSSM FDLGKSSATM QREHEPQRTA 600
SQSANLAPSN LRPAFSMADF SKFKDSRLYD 630
Length:630
Mass (Da):71,852
Last modified:February 1, 1995 - v1
Checksum:i02F8D24A78212544
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti498 – 4981S → P in AAT92897. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF203695 Genomic DNA. Translation: AAF17573.1.
U18778 Genomic DNA. Translation: AAB64538.1.
AY692878 Genomic DNA. Translation: AAT92897.1.
BK006939 Genomic DNA. Translation: DAA07655.1.
PIRiS50463.
RefSeqiNP_010920.3. NM_001178896.3.

Genome annotation databases

EnsemblFungiiYER005W; YER005W; YER005W.
GeneIDi856722.
KEGGisce:YER005W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF203695 Genomic DNA. Translation: AAF17573.1 .
U18778 Genomic DNA. Translation: AAB64538.1 .
AY692878 Genomic DNA. Translation: AAT92897.1 .
BK006939 Genomic DNA. Translation: DAA07655.1 .
PIRi S50463.
RefSeqi NP_010920.3. NM_001178896.3.

3D structure databases

ProteinModelPortali P40009.
SMRi P40009. Positions 7-447.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36735. 62 interactions.
DIPi DIP-7607N.
IntActi P40009. 7 interactions.
MINTi MINT-1354523.
STRINGi 4932.YER005W.

Proteomic databases

MaxQBi P40009.
PaxDbi P40009.
PeptideAtlasi P40009.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YER005W ; YER005W ; YER005W .
GeneIDi 856722.
KEGGi sce:YER005W.

Organism-specific databases

CYGDi YER005w.
SGDi S000000807. YND1.

Phylogenomic databases

eggNOGi COG5371.
GeneTreei ENSGT00550000074435.
HOGENOMi HOG000246725.
KOi K14642.
OMAi IGTSEYW.
OrthoDBi EOG7QK0PD.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci MetaCyc:G3O-30192-MONOMER.
YEAST:G3O-30192-MONOMER.

Miscellaneous databases

NextBioi 982817.
PROi P40009.

Gene expression databases

Genevestigatori P40009.

Family and domain databases

InterProi IPR000407. GDA1_CD39_NTPase.
[Graphical view ]
PANTHERi PTHR11782. PTHR11782. 1 hit.
Pfami PF01150. GDA1_CD39. 1 hit.
[Graphical view ]
PROSITEi PS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "YND1, a homologue of GDA1, encodes membrane-bound apyrase required for Golgi N- and O-glycosylation in Saccharomyces cerevisiae."
    Gao X.D., Kaigorodov V., Jigami Y.
    J. Biol. Chem. 274:21450-21456(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
    Strain: ATCC 204508 / S288c.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Regulation of yeast ectoapyrase ynd1p activity by activator subunit Vma13p of vacuolar H+-ATPase."
    Zhong X., Malhotra R., Guidotti G.
    J. Biol. Chem. 275:35592-35599(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYMATIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH VMA13.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "YND1 interacts with CDC55 and is a novel mediator of E4orf4-induced toxicity."
    Maoz T., Koren R., Ben-Ari I., Kleinberger T.
    J. Biol. Chem. 280:41270-41277(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYMATIC ACTIVITY, INTERACTION WITH CDC55, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-152 AND SER-189.
  9. "Cumulative mutations affecting sterol biosynthesis in the yeast Saccharomyces cerevisiae result in synthetic lethality that is suppressed by alterations in sphingolipid profiles."
    Valachovic M., Bareither B.M., Bhuiyan M.S.A., Eckstein J., Barbuch R., Balderes D., Wilcox L., Sturley S.L., Dickson R.C., Bard M.
    Genetics 173:1893-1908(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiYND1_YEAST
AccessioniPrimary (citable) accession number: P40009
Secondary accession number(s): D3DLQ1, Q6B252
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 14, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 450 molecules/cell in log phase SD medium.

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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

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