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Q9USP2 (YND1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:ynd1
ORF Names:SPCC11E10.05c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates. Required for Golgi glycosylation and cell wall integrity. Involved in N-mannosylation of proteins in Golgi. Ref.2 UniProtKB P40009

Catalytic activity

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

Cofactor

Divalent metal cations. Ca2+, Mg2+ or Mn2+. Ref.2

Pathway

Protein modification; protein glycosylation. Ref.2

Subcellular location

Golgi apparatus. Membrane; Single-pass membrane protein Potential Ref.2 Ref.3.

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processADP catabolic process

Inferred from direct assay Ref.2. Source: PomBase

ATP catabolic process

Inferred from direct assay Ref.2. Source: PomBase

CDP catabolic process

Inferred from direct assay Ref.2. Source: PomBase

GDP catabolic process

Inferred from direct assay Ref.2. Source: PomBase

GTP catabolic process

Inferred from direct assay Ref.2. Source: PomBase

UDP catabolic process

Inferred from direct assay Ref.2. Source: PomBase

protein glycosylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.2Ref.3. Source: PomBase

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from direct assay Ref.2. Source: PomBase

GTPase activity

Inferred from direct assay Ref.2. Source: PomBase

adenosine-diphosphatase activity

Inferred from direct assay Ref.2. Source: PomBase

cytidine diphosphatase activity

Inferred from direct assay Ref.2. Source: PomBase

guanosine-diphosphatase activity

Inferred from direct assay Ref.2. Source: PomBase

nucleoside-triphosphate diphosphatase activity

Inferred from genetic interaction. Source: PomBase

uridine-diphosphatase activity

Inferred from direct assay Ref.2. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Golgi apyrase
PRO_0000347282

Regions

Topological domain1 – 470470Lumenal Potential UniProtKB P40009
Transmembrane471 – 49121Helical; Potential
Topological domain492 – 57281Cytoplasmic Potential UniProtKB P40009

Sites

Active site1451Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9USP2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 8E039FBFA0D3B482

FASTA57264,680
        10         20         30         40         50         60 
MVRKYGIFID AGSSGSRLLI YSWDYDTDSS LSDKVKKLPL IETGIGDGGK WSLKVQPGIS 

        70         80         90        100        110        120 
SFANNPKHVG KKHLKELLDF AAHAIPKDVH KETPVFLSAT AGMRLLGVDA QNKILSHACR 

       130        140        150        160        170        180 
YIKKNYDFDI PNCSNSIRVI DGKAEGMYGW LATNYLLKTL EEKDTSTVGF LDMGGASVQI 

       190        200        210        220        230        240 
AFELPPSQLK NYKDSISTVH IGLQNGQQLE YPLFVTTWLG FGANEAYRRY LGLLIESENG 

       250        260        270        280        290        300 
KVGNTLSDPC SLRGRTYDID GIEFAGTGDL KQCLKLTYNL LNKDKPCSMD PCNFDGISIP 

       310        320        330        340        350        360 
PVDFANTEFV GVSEFWYTTN DVFDMGGSYH FPNFYKKVDE YCGTEWETML SRLYNKELTP 

       370        380        390        400        410        420 
STDENKLEKL CFKASWALNV LHEGFDVPKS NTSSNDAKDG LSVIPAYHSP FTSLEKIERT 

       430        440        450        460        470        480 
EVSWTLGQVL LYASNQQLLA KPEYANYYMD PYGKLIASPS KHWMRLFPNK LFFILSFIFC 

       490        500        510        520        530        540 
LFFLFSLVLF GYDPKRRQRF KKFLLRLQRR KAPYIMSANG SYEDIADFSD DLEMSSPSKW 

       550        560        570 
HGPPIRTTSS HVLADRLSFT ASRERTPRSP FP 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Nucleoside diphosphatase and glycosyltransferase activities can localize to different subcellular compartments in Schizosaccharomyces pombe."
D'Alessio C., Trombetta E.S., Parodi A.J.
J. Biol. Chem. 278:22379-22387(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
[3]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAB57847.1.
PIRT40856.
RefSeqNP_588201.1. NM_001023191.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid275324. 11 interactions.
MINTMINT-4708352.
STRING4896.SPCC11E10.05c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC11E10.05c.1; SPCC11E10.05c.1:pep; SPCC11E10.05c.
GeneID2538741.
KEGGspo:SPCC11E10.05c.

Organism-specific databases

PomBaseSPCC11E10.05c.

Phylogenomic databases

eggNOGCOG5371.
HOGENOMHOG000246725.
OMALVCAKEH.
OrthoDBEOG7QK0PD.
PhylomeDBQ9USP2.

Enzyme and pathway databases

UniPathwayUPA00378.

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

NextBio20799925.

Entry information

Entry nameYND1_SCHPO
AccessionPrimary (citable) accession number: Q9USP2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways