P50287 (ASPGA_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Isoaspartyl peptidase/L-asparaginase 1
EC=3.4.19.5

Alternative name(s):
L-asparagine amidohydrolase 1

Cleaved into the following 2 chains:

1. Isoaspartyl peptidase/L-asparaginase 1 subunit alpha
2. Isoaspartyl peptidase/L-asparaginase 1 subunit beta

Gene names

Ordered Locus Names:	At5g08100
ORF Names:	T22D6_40

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 › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	315 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	Acts in asparagine catabolism but also in the final steps of protein and degradation via hydrolysis of a range of isoaspartyl dipeptides. The affinity for Asn and at least 4 isoaspartyl dipeptides (L-beta-Asp-Ala, L-beta-Asp-Gly, L-beta-Asp-Leu, L-beta-Asp-Phe) is quite low, KM being greater than 4.0 mM. The enzyme is inactive on alpha-aspartyl dipeptides. Ref.5
Catalytic activity	Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.
Subunit structure	Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers Probable. Ref.5
Post-translational modification	Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.
Sequence similarities	Belongs to the Ntn-hydrolase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protease
PTM	Autocatalytic cleavage Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	asparagine catabolic process via L-aspartate Inferred from Biological aspect of Ancestor. Source: RefGenome protein maturation Inferred from Biological aspect of Ancestor. Source: RefGenome proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR
Molecular_function	asparaginase activity Inferred from direct assay PubMed 16705405. Source: TAIR beta-aspartyl-peptidase activity Inferred from electronic annotation. Source: EC
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: P50287-1)

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 182	182	Isoaspartyl peptidase/L-asparaginase 1 subunit alpha		PRO_0000045442
	Chain	183 – 315	133	Isoaspartyl peptidase/L-asparaginase 1 subunit beta		PRO_0000045443
Regions
	Region	211 – 214	4	Substrate binding By similarity
	Region	233 – 236	4	Substrate binding By similarity
Sites
	Active site	183	1	Nucleophile
	Site	182 – 183	2	Cleavage; by autolysis
Amino acid modifications
	Modified residue	169	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	139	1	D → Y in CAA84367. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 15, 2002. Version 2. Checksum: B6D3202B42F94712	FASTA	315	33,027
	10 20 30 40 50 60 MVGWAIALHG GAGDIPIDLP DERRIPRESA LRHCLDLGIS ALKSGKPPLD VAELVVRELE 70 80 90 100 110 120 NHPDFNAGKG SVLTAQGTVE MEASIMDGKT KRCGAVSGLT TVVNPISLAR LVMEKTPHIY 130 140 150 160 170 180 LAFDAAEAFA RAHGVETVDS SHFITPENIA RLKQAKEFNR VQLDYTVPSP KVPDNCGDSQ 190 200 210 220 230 240 IGTVGCVAVD SAGNLASATS TGGYVNKMVG RIGDTPVIGA GTYANHLCAI SATGKGEDII 250 260 270 280 290 300 RGTVARDVAA LMEYKGLSLT EAAAYVVDQS VPRGSCGLVA VSANGEVTMP FNTTGMFRAC 310 ASEDGYSEIA IWPNN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the gene encoding the L-asparaginase gene of Arabidopsis thaliana." Casado A., Caballero J.L., Franco A.R., Cardenas J., Grant M.R., Munoz-Blanco J. Plant Physiol. 108:1321-1322(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta.
[2]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(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]. Strain: cv. Columbia.
[5]	"Isoaspartyl dipeptidase activity of plant-type asparaginases." Hejazi M., Piotukh K., Mattow J., Deutzmann R., Volkmer-Engert R., Lockau W. Biochem. J. 364:129-136(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 183-191, FUNCTION, SUBUNIT, AUTOCATALYTIC CLEAVAGE.
[6]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z34884 Genomic DNA. Translation: CAA84367.1. AL357612 Genomic DNA. Translation: CAB93711.1. CP002688 Genomic DNA. Translation: AED91247.1. AY039555 mRNA. Translation: AAK62610.1. AY093755 mRNA. Translation: AAM10379.1.
IPI	IPI00546750.
PIR	S53127. T50495.
RefSeq	NP_196427.1. NM_120892.3.
UniGene	At.5449. At.54776.
3D structure databases
ProteinModelPortal	P50287.
SMR	P50287. Positions 3-166, 183-313.
ModBase	Search...
Protein family/group databases
MEROPS	T02.A01.
Proteomic databases
PaxDb	P50287.
PRIDE	P50287.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G08100.1; AT5G08100.1; AT5G08100.
GeneID	830704.
KEGG	ath:AT5G08100.
Organism-specific databases
GeneFarm	1951. 188.
TAIR	At5g08100.
Phylogenomic databases
eggNOG	COG1446.
HOGENOM	HOG000174613.
InParanoid	P50287.
KO	K13051.
OMA	IRYQVAG.
PhylomeDB	P50287.
ProtClustDB	PLN02689.
Gene expression databases
ArrayExpress	P50287.
Genevestigator	P50287.
Family and domain databases
InterPro	IPR000246. Peptidase_T2. [Graphical view]
PANTHER	PTHR10188. PTHR10188. 1 hit.
Pfam	PF01112. Asparaginase_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASPGA_ARATH

Accession

Primary (citable) accession number: P50287
Secondary accession number(s): Q9LEZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 15, 2002
Last modified:	May 1, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program