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Protein

Golgi apyrase

Gene

YND1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Miscellaneous

Present with 450 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

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

Cofactori

Ca2+By similarity, Mg2+By similarity, Mn2+By similarityNote: 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: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei152Proton acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

  • protein glycosylation Source: SGD
  • sphingolipid metabolic process Source: UniProtKB-KW

Keywordsi

Molecular functionHydrolase
Biological processLipid metabolism, Sphingolipid metabolism
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:G3O-30192-MONOMER
YEAST:G3O-30192-MONOMER
ReactomeiR-SCE-8850843 Phosphate bond hydrolysis by NTPDase proteins
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
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER005W
SGDiS000000807 YND1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 500LumenalSequence analysisAdd BLAST500
Transmembranei501 – 517HelicalSequence analysisAdd BLAST17
Topological domaini518 – 630CytoplasmicSequence analysisAdd BLAST113

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)DescriptionActionsGraphical viewLength
Mutagenesisi152E → Q: Expressed at lower levels. GTPase activity reduced. 1 Publication1
Mutagenesisi189S → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002099201 – 630Golgi apyraseAdd BLAST630

Proteomic databases

MaxQBiP40009
PaxDbiP40009
PRIDEiP40009

PTM databases

iPTMnetiP40009

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, 98 interactors
DIPiDIP-7607N
IntActiP40009, 7 interactors
MINTiP40009
STRINGi4932.YER005W

Structurei

3D structure databases

ProteinModelPortaliP40009
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00550000074435
HOGENOMiHOG000246725
InParanoidiP40009
KOiK14642
OMAiSEYWYTA
OrthoDBiEOG092C1F34

Family and domain databases

InterProiView protein in InterPro
IPR000407 GDA1_CD39_NTPase
PANTHERiPTHR11782 PTHR11782, 1 hit
PfamiView protein in Pfam
PF01150 GDA1_CD39, 1 hit
PROSITEiView protein in PROSITE
PS01238 GDA1_CD39_NTPASE, 1 hit

Sequencei

Sequence statusi: Complete.

P40009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIENTNDRF GIVIDAGSSG SRIHVFKWQD TESLLHATNQ DSQSILQSVP
60 70 80 90 100
HIHQEKDWTF KLNPGLSSFE KKPQDAYKSH IKPLLDFAKN IIPESHWSSC
110 120 130 140 150
PVFIQATAGM RLLPQDIQSS ILDGLCQGLK HPAEFLVEDC SAQIQVIDGE
160 170 180 190 200
TEGLYGWLGL NYLYGHFNDY NPEVSDHFTF GFMDMGGAST QIAFAPHDSG
210 220 230 240 250
EIARHRDDIA TIFLRSVNGD LQKWDVFVST WLGFGANQAR RRYLAQLINT
260 270 280 290 300
LPENTNDYEN DDFSTRNLND PCMPRGSSTD FEFKDTIFHI AGSGNYEQCT
310 320 330 340 350
KSIYPLLLKN MPCDDEPCLF NGVHAPRIDF ANDKFIGTSE YWYTANDVFK
360 370 380 390 400
LGGEYNFDKF SKSLREFCNS NWTQILANSD KGVYNSIPEN FLKDACFKGN
410 420 430 440 450
WVLNILHEGF DMPRIDVDAE NVNDRPLFQS VEKVEERELS WTLGRILLYA
460 470 480 490 500
SGSILAGNDD FMVGIAPSER RTKLTGKKFI PGKLLESDQL RKQSSSLSNK
510 520 530 540 550
GFLMWFAIIC CIFYLIFHRS HIIRRRFSGL YNITKDFKTG IRRRLKFLRR
560 570 580 590 600
SDPFSRLEEG ELGTDVDGFK DVYRMKSSSM FDLGKSSATM QREHEPQRTA
610 620 630
SQSANLAPSN LRPAFSMADF SKFKDSRLYD
Length:630
Mass (Da):71,852
Last modified:February 1, 1995 - v1
Checksum:i02F8D24A78212544
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti498S → P in AAT92897 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiYND1_YEAST
AccessioniPrimary (citable) accession number: P40009
Secondary accession number(s): D3DLQ1, Q6B252
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 23, 2018
This is version 147 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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