Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Apyrase 1

Gene

APY1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates. Substrate preference is ATP > ADP. Functions with APY2 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.5 Publications

Catalytic activityi

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

Cofactori

Ca2+1 Publication

Kineticsi

  1. KM=30 µM for ATP1 Publication

Vmax=26 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei194 – 1941Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi72 – 8211ATP-bindingCuratedAdd
BLAST
Nucleotide bindingi218 – 22811ATP-bindingCuratedAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. guanosine-diphosphatase activity Source: TAIR
  3. inosine-diphosphatase activity Source: TAIR
  4. nucleoside-diphosphatase activity Source: TAIR
  5. uridine-diphosphatase activity Source: TAIR

GO - Biological processi

  1. pollen germination Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Calcium, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT3G04080-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Apyrase 1 (EC:3.6.1.5)
Short name:
AtAPY1
Alternative name(s):
ATP-diphosphatase
ATP-diphosphohydrolase
Adenosine diphosphatase
Short name:
ADPase
NTPDase
Nucleoside triphosphate diphosphohydrolase 1
Gene namesi
Name:APY1
Ordered Locus Names:At3g04080
ORF Names:T6K12.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G04080.

Subcellular locationi

Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Membrane 1 Publication; Single-pass type II membrane protein 1 Publication
Note: As cell membrane protein, the functional domain could be at the extracellular side.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei22 – 4221Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini43 – 471429LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endosome Source: TAIR
  2. Golgi apparatus Source: TAIR
  3. Golgi membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: TAIR
  5. trans-Golgi network Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

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.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Apyrase 1PRO_0000419905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9SQG2.
PRIDEiQ9SQG2.

Expressioni

Tissue specificityi

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.4 Publications

Inductioni

By hypertonic stress.1 Publication

Gene expression databases

GenevestigatoriQ9SQG2.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G04080.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9SQG2.
SMRiQ9SQG2. Positions 70-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi350 – 3556Poly-Gly

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5371.
HOGENOMiHOG000220904.
InParanoidiQ9SQG2.
KOiK14641.
OMAiLAEELCQ.
PhylomeDBiQ9SQG2.

Family and domain databases

InterProiIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERiPTHR11782. PTHR11782. 1 hit.
PfamiPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SQG2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTAKRAIGRH ESLADKVHRH RGLLLVISIP IVLIALVLLL MPGTSTSVSV
60 70 80 90 100
IEYTMKNHEG GSNSRGPKNY AVIFDAGSSG SRVHVYCFDQ NLDLVPLENE
110 120 130 140 150
LELFLQLKPG LSAYPNDPRQ SANSLVTLLD KAEASVPREL RPKTPVRVGA
160 170 180 190 200
TAGLRALGHQ ASENILQAVR ELLKGRSRLK TEANAVTVLD GTQEGSYQWV
210 220 230 240 250
TINYLLRTLG KPYSDTVGVV DLGGGSVQMA YAIPEEDAAT APKPVEGEDS
260 270 280 290 300
YVREMYLKGR KYFLYVHSYL HYGLLAARAE ILKVSEDSNN PCIATGYAGT
310 320 330 340 350
YKYGGKAFKA AASPSGASLD ECRRVAINAL KVNNSLCTHM KCTFGGVWNG
360 370 380 390 400
GGGGGQKKMF VASFFFDRAA EAGFVDPNQP VAEVRPLDFE KAANKACNMR
410 420 430 440 450
MEEGKSKFPR VEEDNLPYLC LDLVYQYTLL VDGFGLKPSQ TITLVKKVKY
460 470
GDYAVEAAWP LGSAIEAVSS P
Length:471
Mass (Da):51,194
Last modified:May 1, 2000 - v1
Checksum:i6EF17A73207ECDA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093604 mRNA. Translation: AAF00071.1.
JQ937231 mRNA. Translation: AFI41199.1.
AC016829 Genomic DNA. Translation: AAF26805.1.
CP002686 Genomic DNA. Translation: AEE74035.1.
BT029157 mRNA. Translation: ABJ17092.1.
RefSeqiNP_187058.1. NM_111279.4.
UniGeneiAt.16940.

Genome annotation databases

EnsemblPlantsiAT3G04080.1; AT3G04080.1; AT3G04080.
GeneIDi819563.
KEGGiath:AT3G04080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093604 mRNA. Translation: AAF00071.1.
JQ937231 mRNA. Translation: AFI41199.1.
AC016829 Genomic DNA. Translation: AAF26805.1.
CP002686 Genomic DNA. Translation: AEE74035.1.
BT029157 mRNA. Translation: ABJ17092.1.
RefSeqiNP_187058.1. NM_111279.4.
UniGeneiAt.16940.

3D structure databases

ProteinModelPortaliQ9SQG2.
SMRiQ9SQG2. Positions 70-462.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G04080.1-P.

Proteomic databases

PaxDbiQ9SQG2.
PRIDEiQ9SQG2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G04080.1; AT3G04080.1; AT3G04080.
GeneIDi819563.
KEGGiath:AT3G04080.

Organism-specific databases

TAIRiAT3G04080.

Phylogenomic databases

eggNOGiCOG5371.
HOGENOMiHOG000220904.
InParanoidiQ9SQG2.
KOiK14641.
OMAiLAEELCQ.
PhylomeDBiQ9SQG2.

Enzyme and pathway databases

BioCyciARA:AT3G04080-MONOMER.

Miscellaneous databases

PROiQ9SQG2.

Gene expression databases

GenevestigatoriQ9SQG2.

Family and domain databases

InterProiIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERiPTHR11782. PTHR11782. 1 hit.
PfamiPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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], COFACTOR, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
  2. "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.
  3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Arabidopsis ORF Clone."
    Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "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.
  7. "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.
  8. "Apyrases (nucleoside triphosphate-diphosphohydrolases) play a key role in growth control in Arabidopsis."
    Wu J., Steinebrunner I., Sun Y., Butterfield T., Torres J., Arnold D., Gonzalez A., Jacob F., Reichler S., Roux S.J.
    Plant Physiol. 144:961-975(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    Strain: cv. Wassilewskija.
  9. "Hypertonic stress increased extracellular ATP levels and the expression of stress-responsive genes in Arabidopsis thaliana seedlings."
    Kim S.H., Yang S.H., Kim T.J., Han J.S., Suh J.W.
    Biosci. Biotechnol. Biochem. 73:1252-1256(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "Extracellular nucleotides and apyrases regulate stomatal aperture in Arabidopsis."
    Clark G., Fraley D., Steinebrunner I., Cervantes A., Onyirimba J., Liu A., Torres J., Tang W., Kim J., Roux S.J.
    Plant Physiol. 156:1740-1753(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: cv. Wassilewskija.

Entry informationi

Entry nameiAPY1_ARATH
AccessioniPrimary (citable) accession number: Q9SQG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: May 1, 2000
Last modified: January 7, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.