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P40009

- YND1_YEAST

UniProt

P40009 - YND1_YEAST

Protein

Golgi apyrase

Gene

YND1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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 acceptorBy 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

    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 2 Publications. Membrane Curated; Single-pass membrane protein Curated

    GO - Cellular componenti

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

    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 apyrasePRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 500500LumenalSequence AnalysisAdd
    BLAST
    Topological domaini518 – 630113CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei501 – 51717HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GDA1/CD39 NTPase family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti498 – 4981S → P in AAT92897. (PubMed:17322287)Curated

    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

    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: October 1, 2014
    This is version 116 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.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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3