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Golgi apyrase (EC 3.6.1.5) (ATP-diphosphatase) (ATP-diphosphohydrolase) (Adenosine diphosphatase) (ADPase) (Golgi nucleoside diphosphatase) (Yeast nucleoside diphosphatase 1)

 YND1_YEAST              Reviewed;         630 AA.
P40009; D3DLQ1; Q6B252;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
22-NOV-2017, entry version 142.
RecName: Full=Golgi apyrase;
EC=3.6.1.5;
AltName: Full=ATP-diphosphatase;
AltName: Full=ATP-diphosphohydrolase;
AltName: Full=Adenosine diphosphatase;
Short=ADPase;
AltName: Full=Golgi nucleoside diphosphatase;
AltName: Full=Yeast nucleoside diphosphatase 1;
Name=YND1; OrderedLocusNames=YER005W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 204508 / S288c;
PubMed=10409709; DOI=10.1074/jbc.274.30.21450;
Gao X.D., Kaigorodov V., Jigami Y.;
"YND1, a homologue of GDA1, encodes membrane-bound apyrase required
for Golgi N- and O-glycosylation in Saccharomyces cerevisiae.";
J. Biol. Chem. 274:21450-21456(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
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., 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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
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.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
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., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
ENZYMATIC ACTIVITY, ENZYME REGULATION, AND INTERACTION WITH VMA13.
PubMed=10954728; DOI=10.1074/jbc.M006932200;
Zhong X., Malhotra R., Guidotti G.;
"Regulation of yeast ectoapyrase ynd1p activity by activator subunit
Vma13p of vacuolar H+-ATPase.";
J. Biol. Chem. 275:35592-35599(2000).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
FUNCTION, ENZYMATIC ACTIVITY, INTERACTION WITH CDC55, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF GLU-152 AND SER-189.
PubMed=16227198; DOI=10.1074/jbc.M507281200;
Maoz T., Koren R., Ben-Ari I., Kleinberger T.;
"YND1 interacts with CDC55 and is a novel mediator of E4orf4-induced
toxicity.";
J. Biol. Chem. 280:41270-41277(2005).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16702413; DOI=10.1534/genetics.105.053025;
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.;
"Cumulative mutations affecting sterol biosynthesis in the yeast
Saccharomyces cerevisiae result in synthetic lethality that is
suppressed by alterations in sphingolipid profiles.";
Genetics 173:1893-1908(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- 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. {ECO:0000269|PubMed:10409709,
ECO:0000269|PubMed:16227198, ECO:0000269|PubMed:16702413}.
-!- CATALYTIC ACTIVITY: A nucleoside 5'-triphosphate + 2 H(2)O = a
nucleoside 5'-phosphate + 2 phosphate.
{ECO:0000269|PubMed:10954728, ECO:0000269|PubMed:16227198}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=A divalent cation Ca(2+), Mg(2+) or Mn(2+). {ECO:0000250};
-!- 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.
{ECO:0000269|PubMed:10954728}.
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:10954728, ECO:0000269|PubMed:16227198}.
-!- SUBCELLULAR LOCATION: Golgi apparatus
{ECO:0000269|PubMed:10409709, ECO:0000269|PubMed:14562095}.
Membrane {ECO:0000305}; Single-pass membrane protein
{ECO:0000305}.
-!- 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.
{ECO:0000269|PubMed:16227198, ECO:0000269|PubMed:16702413}.
-!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF203695; AAF17573.1; -; Genomic_DNA.
EMBL; U18778; AAB64538.1; -; Genomic_DNA.
EMBL; AY692878; AAT92897.1; -; Genomic_DNA.
EMBL; BK006939; DAA07655.1; -; Genomic_DNA.
PIR; S50463; S50463.
RefSeq; NP_010920.3; NM_001178896.3.
ProteinModelPortal; P40009; -.
BioGrid; 36735; 81.
DIP; DIP-7607N; -.
IntAct; P40009; 7.
MINT; MINT-1354523; -.
STRING; 4932.YER005W; -.
iPTMnet; P40009; -.
MaxQB; P40009; -.
PRIDE; P40009; -.
EnsemblFungi; YER005W; YER005W; YER005W.
GeneID; 856722; -.
KEGG; sce:YER005W; -.
EuPathDB; FungiDB:YER005W; -.
SGD; S000000807; YND1.
GeneTree; ENSGT00550000074435; -.
HOGENOM; HOG000246725; -.
InParanoid; P40009; -.
KO; K14642; -.
OMA; SEYWYTA; -.
OrthoDB; EOG092C1F34; -.
BioCyc; MetaCyc:G3O-30192-MONOMER; -.
BioCyc; YEAST:G3O-30192-MONOMER; -.
Reactome; R-SCE-8850843; Phosphate bond hydrolysis by NTPDase proteins.
UniPathway; UPA00378; -.
PRO; PR:P40009; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0000139; C:Golgi membrane; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:SGD.
GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0102485; F:dATP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102486; F:dCTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102491; F:dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102488; F:dTTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102487; F:dUTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102489; F:GTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0017110; F:nucleoside-diphosphatase activity; IDA:SGD.
GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:SGD.
GO; GO:0006486; P:protein glycosylation; IMP:SGD.
GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
InterPro; IPR000407; GDA1_CD39_NTPase.
PANTHER; PTHR11782; PTHR11782; 1.
Pfam; PF01150; GDA1_CD39; 1.
PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Golgi apparatus; Hydrolase;
Lipid metabolism; Membrane; Nucleotide-binding; Reference proteome;
Sphingolipid metabolism; Transmembrane; Transmembrane helix.
CHAIN 1 630 Golgi apyrase.
/FTId=PRO_0000209920.
TOPO_DOM 1 500 Lumenal. {ECO:0000255}.
TRANSMEM 501 517 Helical. {ECO:0000255}.
TOPO_DOM 518 630 Cytoplasmic. {ECO:0000255}.
ACT_SITE 152 152 Proton acceptor. {ECO:0000250}.
MUTAGEN 152 152 E->Q: Expressed at lower levels. GTPase
activity reduced.
{ECO:0000269|PubMed:16227198}.
MUTAGEN 189 189 S->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.
{ECO:0000269|PubMed:16227198}.
CONFLICT 498 498 S -> P (in Ref. 4; AAT92897).
{ECO:0000305}.
SEQUENCE 630 AA; 71852 MW; 02F8D24A78212544 CRC64;
MLIENTNDRF GIVIDAGSSG SRIHVFKWQD TESLLHATNQ DSQSILQSVP HIHQEKDWTF
KLNPGLSSFE KKPQDAYKSH IKPLLDFAKN IIPESHWSSC PVFIQATAGM RLLPQDIQSS
ILDGLCQGLK HPAEFLVEDC SAQIQVIDGE TEGLYGWLGL NYLYGHFNDY NPEVSDHFTF
GFMDMGGAST QIAFAPHDSG EIARHRDDIA TIFLRSVNGD LQKWDVFVST WLGFGANQAR
RRYLAQLINT LPENTNDYEN DDFSTRNLND PCMPRGSSTD FEFKDTIFHI AGSGNYEQCT
KSIYPLLLKN MPCDDEPCLF NGVHAPRIDF ANDKFIGTSE YWYTANDVFK LGGEYNFDKF
SKSLREFCNS NWTQILANSD KGVYNSIPEN FLKDACFKGN WVLNILHEGF DMPRIDVDAE
NVNDRPLFQS VEKVEERELS WTLGRILLYA SGSILAGNDD FMVGIAPSER RTKLTGKKFI
PGKLLESDQL RKQSSSLSNK GFLMWFAIIC CIFYLIFHRS HIIRRRFSGL YNITKDFKTG
IRRRLKFLRR SDPFSRLEEG ELGTDVDGFK DVYRMKSSSM FDLGKSSATM QREHEPQRTA
SQSANLAPSN LRPAFSMADF SKFKDSRLYD


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