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Q9SPM5 (APY2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apyrase 2

Short name=AtAPY2
EC=3.6.1.5
Alternative name(s):
ATP-diphosphatase
ATP-diphosphohydrolase
Adenosine diphosphatase
Short name=ADPase
NTPDase
Nucleoside triphosphate diphosphohydrolase 2
Gene names
Name:APY2
Ordered Locus Names:At5g18280
ORF Names:MRG7.24
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates. Substrate preference is ATP > ADP. Functions with APY1 to reduce extracellular ATP level which is essential for pollen germination and normal plant development. Plays a role in the regulation of stomatal function by modulating extracellular ATP levels in guard cells. Ref.2 Ref.7 Ref.8

Catalytic activity

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

Cofactor

Calcium By similarity.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein. Membrane Probable; Single-pass type II membrane protein Probable. Note: As cell membrane protein, the functional domain could be at the extracellular side. Ref.3

Tissue specificity

Expressed in roots, root hairs, root cap, leaves, stems, trichomes, phloem throughout the plant, guard cells, filaments of young stamens, stipules, papillae of stigmas, pollen, pollen tubes and the abscission zone of siliques. Ref.2 Ref.7 Ref.8

Induction

By hypertonic stress.

Disruption phenotype

No visible phenotype under normal growth conditions. Apy1 and apy2 double mutant displays developmental defects including the lack of functional root and shoot meristems, and morphogenetic and patterning abnormalities of the cotyledons. Double mutant exhibits a complete inhibition of pollen germination. Ref.7 Ref.8

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Biophysicochemical properties

Kinetic parameters:

KM=30 µM for ATP Ref.2

Vmax=26 µmol/min/mg enzyme

Sequence caution

The sequence AED92532.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Nucleotide-binding
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9SPM5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain48 – 472425Apyrase 2
PRO_0000419906

Regions

Topological domain1 – 2121Cytoplasmic Potential
Transmembrane22 – 4221Helical; Signal-anchor for type II membrane protein; Potential
Topological domain43 – 472430Lumenal Potential
Nucleotide binding73 – 8311ATP-binding Probable
Nucleotide binding219 – 22911ATP-binding Probable

Sites

Active site1951Proton acceptor By similarity

Amino acid modifications

Glycosylation3341N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict201H → N in AFI41206. Ref.3
Sequence conflict1511A → V in AAF66599. Ref.2
Sequence conflict2611R → Q in AAM98186. Ref.6
Sequence conflict3011M → T in AAF66599. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FA0C280456D51224

FASTA47251,599
        10         20         30         40         50         60 
MTAKRGIGRH ESLADKIQRH RGIILVISVP IVLIGLVLLL MPGRSISDSV VEEYSVHNRK 

        70         80         90        100        110        120 
GGPNSRGPKN YAVIFDAGSS GSRVHVYCFD QNLDLIPLGN ELELFLQLKP GLSAYPTDPR 

       130        140        150        160        170        180 
QAANSLVSLL DKAEASVPRE LRPKTHVRVG ATAGLRTLGH DASENILQAV RELLRDRSML 

       190        200        210        220        230        240 
KTEANAVTVL DGTQEGSYQW VTINYLLRNL GKPYSDTVGV VDLGGGSVQM AYAISEEDAA 

       250        260        270        280        290        300 
SAPKPLEGED SYVREMYLKG RKYFLYVHSY LHYGLLAARA EILKVSEDSE NPCIVAGYDG 

       310        320        330        340        350        360 
MYKYGGKEFK APASQSGASL DECRRITINA LKVNDTLCTH MKCTFGGVWN GGRGGGQKNM 

       370        380        390        400        410        420 
FVASFFFDRA AEAGFVDPKQ PVATVRPMDF EKAAKKACSM KLEEGKSTFP LVEEENLPYL 

       430        440        450        460        470 
CMDLVYQYTL LIDGFGLEPS QTITLVKKVK YGDQAVEAAW PLGSAIEAVS SP 

« Hide

References

« Hide 'large scale' references
[1]"A Nod factor-binding lectin is a member of a distinct class of apyrases that may be unique to the legumes."
Roberts N.J., Brigham J., Wu B., Murphy J.B., Volpin H., Phillips D.A., Etzler M.E.
Mol. Gen. Genet. 262:261-267(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. No-0.
[2]"Molecular and biochemical comparison of two different apyrases from Arabidopsis thaliana."
Steinebrunner I.A., Jeter C.R., Song C., Roux S.J.
Plant Physiol. Biochem. 38:913-922(2000)
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[3]"Isolation and proteomic characterization of the Arabidopsis Golgi defines functional and novel components involved in plant cell wall biosynthesis."
Parsons H.T., Christiansen K., Knierim B., Carroll A., Ito J., Batth T.S., Smith-Moritz A.M., Morrison S., McInerney P., Hadi M.Z., Auer M., Mukhopadhyay A., Petzold C.J., Scheller H.V., Loque D., Heazlewood J.L.
Plant Physiol. 159:12-26(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Strain: cv. Landsberg erecta.
[4]"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
DNA Res. 5:203-216(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[6]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[7]"Disruption of apyrases inhibits pollen germination in Arabidopsis."
Steinebrunner I., Wu J., Sun Y., Corbett A., Roux S.J.
Plant Physiol. 131:1638-1647(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
Strain: cv. Wassilewskija.
[8]"Developmental defects and seedling lethality in apyrase AtAPY1 and AtAPY2 double knockout mutants."
Wolf C., Hennig M., Romanovicz D., Steinebrunner I.
Plant Mol. Biol. 64:657-672(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
Strain: cv. Wassilewskija.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF156783 mRNA. Translation: AAF00612.1.
AF141671 mRNA. Translation: AAF66599.1.
JQ937238 mRNA. Translation: AFI41206.1.
AB012246 Genomic DNA. Translation: BAB09486.1.
CP002688 Genomic DNA. Translation: AED92532.1. Sequence problems.
AY099866 mRNA. Translation: AAM20717.1.
AY140045 mRNA. Translation: AAM98186.1.
BT000329 mRNA. Translation: AAN15648.1.
RefSeqNP_197329.4. NM_121833.6.
UniGeneAt.19874.

3D structure databases

ProteinModelPortalQ9SPM5.
SMRQ9SPM5. Positions 71-463.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9SPM5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G18280.1; AT5G18280.1; AT5G18280.
GeneID831946.
KEGGath:AT5G18280.

Organism-specific databases

TAIRAT5G18280.

Phylogenomic databases

InParanoidQ9SPM5.
KOK14641.
PhylomeDBQ9SPM5.

Enzyme and pathway databases

BioCycARA:AT5G18280-MONOMER.
ARA:GQT-2442-MONOMER.

Gene expression databases

GenevestigatorQ9SPM5.

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...

Entry information

Entry nameAPY2_ARATH
AccessionPrimary (citable) accession number: Q9SPM5
Secondary accession number(s): F4JWK7 expand/collapse secondary AC list , I1VCB1, Q8L704, Q9M7B3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names