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P40009 (YND1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:YND1
Ordered Locus Names:YER005W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length630 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8 Ref.9

Catalytic activity

A nucleoside 5'-triphosphate + 2 H2O = a nucleoside 5'-phosphate + 2 phosphate. Ref.5 Ref.8

Cofactor

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

Enzyme regulation

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. Ref.5

Pathway

Protein modification; protein glycosylation.

Subunit structure

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. Ref.5 Ref.8

Subcellular location

Golgi apparatus. Membrane; Single-pass membrane protein Potential Ref.1 Ref.6.

Disruption phenotype

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. Ref.8 Ref.9

Miscellaneous

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

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 630630Golgi apyrase
PRO_0000209920

Regions

Topological domain1 – 500500Lumenal Potential
Transmembrane501 – 51717Helical; Potential
Topological domain518 – 630113Cytoplasmic Potential

Sites

Active site1521Proton acceptor By similarity

Experimental info

Mutagenesis1521E → Q: Expressed at lower levels. GTPase activity reduced. Ref.8
Mutagenesis1891S → 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. Ref.8
Sequence conflict4981S → P in AAT92897. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P40009 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 02F8D24A78212544

FASTA63071,852
        10         20         30         40         50         60 
MLIENTNDRF GIVIDAGSSG SRIHVFKWQD TESLLHATNQ DSQSILQSVP HIHQEKDWTF 

        70         80         90        100        110        120 
KLNPGLSSFE KKPQDAYKSH IKPLLDFAKN IIPESHWSSC PVFIQATAGM RLLPQDIQSS 

       130        140        150        160        170        180 
ILDGLCQGLK HPAEFLVEDC SAQIQVIDGE TEGLYGWLGL NYLYGHFNDY NPEVSDHFTF 

       190        200        210        220        230        240 
GFMDMGGAST QIAFAPHDSG EIARHRDDIA TIFLRSVNGD LQKWDVFVST WLGFGANQAR 

       250        260        270        280        290        300 
RRYLAQLINT LPENTNDYEN DDFSTRNLND PCMPRGSSTD FEFKDTIFHI AGSGNYEQCT 

       310        320        330        340        350        360 
KSIYPLLLKN MPCDDEPCLF NGVHAPRIDF ANDKFIGTSE YWYTANDVFK LGGEYNFDKF 

       370        380        390        400        410        420 
SKSLREFCNS NWTQILANSD KGVYNSIPEN FLKDACFKGN WVLNILHEGF DMPRIDVDAE 

       430        440        450        460        470        480 
NVNDRPLFQS VEKVEERELS WTLGRILLYA SGSILAGNDD FMVGIAPSER RTKLTGKKFI 

       490        500        510        520        530        540 
PGKLLESDQL RKQSSSLSNK GFLMWFAIIC CIFYLIFHRS HIIRRRFSGL YNITKDFKTG 

       550        560        570        580        590        600 
IRRRLKFLRR SDPFSRLEEG ELGTDVDGFK DVYRMKSSSM FDLGKSSATM QREHEPQRTA 

       610        620        630 
SQSANLAPSN LRPAFSMADF SKFKDSRLYD 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF203695 Genomic DNA. Translation: AAF17573.1.
U18778 Genomic DNA. Translation: AAB64538.1.
AY692878 Genomic DNA. Translation: AAT92897.1.
BK006939 Genomic DNA. Translation: DAA07655.1.
PIRS50463.
RefSeqNP_010920.3. NM_001178896.3.

3D structure databases

ProteinModelPortalP40009.
SMRP40009. Positions 7-447.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36735. 62 interactions.
DIPDIP-7607N.
IntActP40009. 7 interactions.
MINTMINT-1354523.
STRING4932.YER005W.

Proteomic databases

MaxQBP40009.
PaxDbP40009.
PeptideAtlasP40009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER005W; YER005W; YER005W.
GeneID856722.
KEGGsce:YER005W.

Organism-specific databases

CYGDYER005w.
SGDS000000807. YND1.

Phylogenomic databases

eggNOGCOG5371.
GeneTreeENSGT00550000074435.
HOGENOMHOG000246725.
KOK14642.
OMAIGTSEYW.
OrthoDBEOG7QK0PD.

Enzyme and pathway databases

BioCycMetaCyc:G3O-30192-MONOMER.
YEAST:G3O-30192-MONOMER.
UniPathwayUPA00378.

Gene expression databases

GenevestigatorP40009.

Family and domain databases

InterProIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERPTHR11782. PTHR11782. 1 hit.
PfamPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982817.
PROP40009.

Entry information

Entry nameYND1_YEAST
AccessionPrimary (citable) accession number: P40009
Secondary accession number(s): D3DLQ1, Q6B252
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways