Reviewed, UniProtKB/Swiss-Prot Q9ZPF5 (ARGI2_ARATH)

Names and origin

Protein names

Recommended name:
    Probable arginase
    EC=3.5.3.1

Gene names

Ordered Locus Names:	At4g08870
ORF Names:	T3H13.10

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-arginine + H2O = L-ornithine + urea.
Cofactor	Binds 2 manganese ions per subunit By similarity.
Pathway	Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
Sequence similarities	Belongs to the arginase family.

Ontologies

Keywords
Biological process	Arginine metabolism
Coding sequence diversity	Alternative splicing
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from direct assay. Source: TAIR mitochondrion Inferred from direct assay. Source: TAIR
Molecular function	arginase activity Inferred from genetic interaction. Source: TAIR manganese ion binding 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: Q9ZPF5-1)

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 – 344	344	Probable arginase		PRO_0000173704
Regions
	Region	189 – 193	5	Substrate binding Potential
	Region	197 – 199	3	Substrate binding Potential
Sites
	Metal binding	163	1	Manganese 1 By similarity
	Metal binding	185	1	Manganese 1 By similarity
	Metal binding	185	1	Manganese 2 By similarity
	Metal binding	187	1	Manganese 2 By similarity
	Metal binding	189	1	Manganese 1 By similarity
	Metal binding	272	1	Manganese 1 By similarity
	Metal binding	272	1	Manganese 2 By similarity
	Metal binding	274	1	Manganese 2 By similarity
	Binding site	228	1	Substrate Potential
	Binding site	315	1	Substrate Potential

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: FED95D31B1A2FEBE	FASTA	344	37,980
	10 20 30 40 50 60 MWKIGQRGVP YFQRLIAAPF TTLRSLPTSL VETGQNRVID ASLTLIRERA KLKGELVRLI 70 80 90 100 110 120 GGAKATTALL GVPLGHNSSF LEGPALAPPH VREAIWCGST NSTTEEGKEL KDPRVLSDVG 130 140 150 160 170 180 DIPVQEIREM GVDDDRLMKV VSESVKLVME EEPLRPLVIG GDHSISYPVV RAVSEKLGGP 190 200 210 220 230 240 VDILHLDAHP DIYDRFEGNY YSHASSFARI MEGGYARRLL QVGIRSINKE GREQGKRFGV 250 260 270 280 290 300 EQYEMRTFSK DRQMLENLKL GEGVKGVYIS IDVDCLDPGF AHGVSHFEPG GLSFRDVLNI 310 320 330 340 LHNLQGDLVG ADVVEYNPQR DTADDMTAMV AAKFVRELAA KMSK

References

[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF128396 Genomic DNA. Translation: AAD17371.1. AL161513 Genomic DNA. Translation: CAB78011.1. BT003815 mRNA. Translation: AAO41868.1.
IPI	IPI00521796.
PIR	C85089.
RefSeq	NP_192626.1.
UniGene	At.4188
3D structure databases
HSSP	HSSP built from PDB template 1GQ6 based on UniProtKB P37819.
ModBase	Search...
2-D gel databases
SWISS-2DPAGE	Q9ZPF5.
Proteomic databases
PRIDE	Q9ZPF5.
ProMEX	Q9ZPF5.
Genome annotation databases
GeneID	826458.
GenomeReviews	Gene locus AT4G08870 in contig CT486007_GR.
NMPDR	fig|3702.1.peg.18540.
Organism-specific databases
TAIR	At4g08870.
Phylogenomic databases
OMA	SSCLETY.
Enzyme and pathway databases
BRENDA	3.5.3.1. 302.
Gene expression databases
ArrayExpress	Q9ZPF5.
Genevestigator	Q9ZPF5.
Family and domain databases
InterPro	IPR006035. Ureohydrolase. [Graphical view]
Gene3D	G3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHER	PTHR11358. Ureohydrolase. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
PROSITE	PS01053. ARGINASE_1. False negative. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGI2_ARATH

Accession

Primary (citable) accession number: Q9ZPF5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)