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Q9LV77 (ASNS2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 92. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Asparagine synthetase [glutamine-hydrolyzing] 2

EC=6.3.5.4
Alternative name(s):
Glutamine-dependent asparagine synthetase 2
Gene names
Name:ASN2
Ordered Locus Names:At5g65010
ORF Names:MXK3.25
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for nitrogen assimilation, distribution and remobilization within the plant via the phloem. Ref.7

Catalytic activity

ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.

Pathway

Amino-acid biosynthesis; L-asparagine biosynthesis.

Tissue specificity

Expressed in the vascular region adjacent to leaf mesophyll cells in the companion cell-sieve tube element complex. Ref.1 Ref.7

Induction

By light and sucrose. Down-regulated by dark. Ref.1 Ref.5 Ref.7

Disruption phenotype

Pale green leaf phenotype and reduction of biomass in mature plants. Increased levels of asparagine, proline and ammonium in response to salt treatment. Ref.6 Ref.7

Sequence similarities

Contains 1 asparagine synthetase domain.

Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9LV77-1)

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.
Isoform 2 (identifier: Q9LV77-2)

The sequence of this isoform differs from the canonical sequence as follows:
     508-508: K → KQ
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 578577Asparagine synthetase [glutamine-hydrolyzing] 2
PRO_0000420840

Regions

Domain2 – 185184Glutamine amidotransferase type-2
Domain210 – 450241Asparagine synthetase
Nucleotide binding341 – 3422ATP By similarity
Region50 – 545Glutamine binding By similarity
Region75 – 773Glutamine binding By similarity
Compositional bias559 – 5657Poly-Ala

Sites

Active site21For GATase activity By similarity
Binding site981Glutamine By similarity
Binding site2311ATP; via carbonyl oxygen By similarity
Binding site2671ATP; via amide nitrogen and carbonyl oxygen By similarity
Site3431Important for beta-aspartyl-AMP intermediate formation By similarity

Natural variations

Alternative sequence5081K → KQ in isoform 2.
VSP_044714

Experimental info

Sequence conflict4841V → F in AAC72837. Ref.1

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: CAEAD8DC90F3A773

FASTA57865,030
        10         20         30         40         50         60 
MCGILAVLGC IDNSQAKRSR IIELSRRLRH RGPDWSGLHC YEDCYLAHER LAIIDPTSGD 

        70         80         90        100        110        120 
QPLYNEDKTV AVTVNGEIYN HKILREKLKS HQFRTGSDCE VIAHLYEEHG EEFIDMLDGM 

       130        140        150        160        170        180 
FAFVLLDTRD KSFIAARDAI GITPLYIGWG LDGSVWFASE MKALSDDCEQ FMSFPPGHIY 

       190        200        210        220        230        240 
SSKQGGLRRW YNPPWYNEQV PSTPYDPLVL RNAFEKAVIK RLMTDVPFGV LLSGGLDSSL 

       250        260        270        280        290        300 
VAAVALRHLE KSEAARQWGS QLHTFCIGLQ GSPDLKAGRE VADYLGTRHH EFQFTVQDGI 

       310        320        330        340        350        360 
DAIEEVIYHI ETYDVTTIRA STPMFLMSRK IKSLGVKMVL SGEGSDEILG GYLYFHKAPN 

       370        380        390        400        410        420 
KKEFHEETCR KIKALHQFDC LRANKSTSAW GVEARVPFLD KEFLNVAMSI DPEWKLIKPD 

       430        440        450        460        470        480 
LGRIEKWVLR NAFDDEERPY LPKHILYRQK EQFSDGVGYS WIDGLKDHAN KHVSDTMLSN 

       490        500        510        520        530        540 
ASFVFPDNTP LTKEAYYYRT IFEKFFPKSA ARATVPGGPS IACSTAKAVE WDATWSKNLD 

       550        560        570 
PSGRAALGVH VAAYEEDKAA AAAKAGSDLV DPLPKNGT 

« Hide

Isoform 2 [UniParc].

Checksum: AF6CE3E95A30A9F5
Show »

FASTA57965,158

References

« Hide 'large scale' references
[1]"Reciprocal regulation of distinct asparagine synthetase genes by light and metabolites in Arabidopsis thaliana."
Lam H.M., Hsieh M.H., Coruzzi G.
Plant J. 16:345-353(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
DNA Res. 7:31-63(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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] (ISOFORM 1).
Strain: cv. Columbia.
[5]"Correlation of ASN2 gene expression with ammonium metabolism in Arabidopsis."
Wong H.K., Chan H.K., Coruzzi G.M., Lam H.M.
Plant Physiol. 134:332-338(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[6]"An Arabidopsis mutant disrupted in ASN2 encoding asparagine synthetase 2 exhibits low salt stress tolerance."
Maaroufi-Dguimi H., Debouba M., Gaufichon L., Clement G., Gouia H., Hajjaji A., Suzuki A.
Plant Physiol. Biochem. 49:623-628(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[7]"Arabidopsis thaliana ASN2 encoding asparagine synthetase is involved in the control of nitrogen assimilation and export during vegetative growth."
Gaufichon L., Masclaux-Daubresse C., Tcherkez G., Reisdorf-Cren M., Sakakibara Y., Hase T., Clement G., Avice J.C., Grandjean O., Marmagne A., Boutet-Mercey S., Azzopardi M., Soulay F., Suzuki A.
Plant Cell Environ. 36:328-342(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF095453 mRNA. Translation: AAC72837.1.
AB019236 Genomic DNA. Translation: BAA97313.1.
CP002688 Genomic DNA. Translation: AED97984.1.
CP002688 Genomic DNA. Translation: AED97985.1.
AF367340 mRNA. Translation: AAK32927.1.
AY124866 mRNA. Translation: AAM70575.1.
RefSeqNP_201306.2. NM_125900.2. [Q9LV77-2]
NP_851272.1. NM_180941.2. [Q9LV77-1]
UniGeneAt.67717.
At.7860.

3D structure databases

ProteinModelPortalQ9LV77.
SMRQ9LV77. Positions 18-517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT5G65010.2-P.

Protein family/group databases

MEROPSC44.976.

Proteomic databases

PRIDEQ9LV77.
ProMEXQ9LV77.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G65010.1; AT5G65010.1; AT5G65010. [Q9LV77-1]
GeneID836625.
KEGGath:AT5G65010.

Organism-specific databases

TAIRAT5G65010.

Phylogenomic databases

HOGENOMHOG000027493.
InParanoidQ9LV77.
KOK01953.
OMAICGELRF.
PhylomeDBQ9LV77.

Enzyme and pathway databases

BioCycARA:GQT-858-MONOMER.
UniPathwayUPA00134.

Gene expression databases

GenevestigatorQ9LV77.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProIPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
PIRSFPIRSF001589. Asn_synthetase_glu-h. 1 hit.
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR01536. asn_synth_AEB. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASNS2_ARATH
AccessionPrimary (citable) accession number: Q9LV77
Secondary accession number(s): F4KGG8, Q9ZST6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2013
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 92 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names