Q9LV77 (ASNS2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Mesangiospermae › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	578 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Biological process	Amino-acid biosynthesis Asparagine biosynthesis
Coding sequence diversity	Alternative splicing
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-asparagine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: UniProtKB-EC
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 578	577	Asparagine synthetase [glutamine-hydrolyzing] 2		PRO_0000420840
Regions
	Domain	2 – 185	184	Glutamine amidotransferase type-2
	Domain	210 – 450	241	Asparagine synthetase
	Nucleotide binding	341 – 342	2	ATP By similarity
	Region	50 – 54	5	Glutamine binding By similarity
	Region	75 – 77	3	Glutamine binding By similarity
	Compositional bias	559 – 565	7	Poly-Ala
Sites
	Active site	2	1	For GATase activity By similarity
	Binding site	98	1	Glutamine By similarity
	Binding site	231	1	ATP; via carbonyl oxygen By similarity
	Binding site	267	1	ATP; via amide nitrogen and carbonyl oxygen By similarity
	Site	343	1	Important for beta-aspartyl-AMP intermediate formation By similarity
Natural variations
	Alternative sequence	508	1	K → KQ in isoform 2.		VSP_044714
Experimental info
	Sequence conflict	484	1	V → F in AAC72837. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: CAEAD8DC90F3A773	FASTA	578	65,030
	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
	Isoform 2 [UniParc]. Checksum: AF6CE3E95A30A9F5	FASTA	579	65,158
	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 IFEKFFPKQS AARATVPGGP SIACSTAKAV EWDATWSKNL 550 560 570 DPSGRAALGV HVAAYEEDKA AAAAKAGSDL VDPLPKNGT

References

	« Hide 'large scale' referencesShow '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. , 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.

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.
RefSeq	NP_201306.2. NM_125900.2. NP_851272.1. NM_180941.2.
UniGene	At.67717. At.7860.
3D structure databases
ProteinModelPortal	Q9LV77.
SMR	Q9LV77. Positions 18-517.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
STRING	3702.AT5G65010.2-P.
Protein family/group databases
MEROPS	C44.976.
Proteomic databases
PRIDE	Q9LV77.
ProMEX	Q9LV77.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G65010.1; AT5G65010.1; AT5G65010.
GeneID	836625.
KEGG	ath:AT5G65010.
Organism-specific databases
TAIR	AT5G65010.
Phylogenomic databases
HOGENOM	HOG000027493.
InParanoid	Q9LV77.
KO	K01953.
OMA	CERFITF.
PhylomeDB	Q9LV77.
ProtClustDB	PLN02549.
Enzyme and pathway databases
BioCyc	ARA:GQT-858-MONOMER.
UniPathway	UPA00134.
Gene expression databases
Genevestigator	Q9LV77.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
InterPro	IPR006426. Asn_synth_AEB. IPR001962. Asn_synthase. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF00733. Asn_synthase. 1 hit. PF13537. GATase_7. 1 hit. [Graphical view]
PIRSF	PIRSF001589. Asn_synthetase_glu-h. 1 hit.
TIGRFAMs	TIGR01536. asn_synth_AEB. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASNS2_ARATH

Accession

Primary (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:	February 19, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program