[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1111/j.1432-1033.1993.tb17622.x; PubMed=7916684 [NCBI, ExPASy, EBI, Israel, Japan] Xu Q., Baker B.S., Tata J.R.; "Developmental and hormonal regulation of the Xenopus liver-type arginase gene."; Eur. J. Biochem. 211:891-898(1993).
[2]	DEVELOPMENTAL STAGE. PubMed=7929226 [NCBI, ExPASy, EBI, Israel, Japan] Patterton D., Shi Y.-B.; "Thyroid hormone-dependent differential regulation of multiple arginase genes during amphibian metamorphosis."; J. Biol. Chem. 269:25328-25334(1994).

Comments

CATALYTIC ACTIVITY: L-arginine + H₂O = L-ornithine + urea.
COFACTOR: Manganese.
PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1 .
SUBUNIT: Homotrimer.
TISSUE SPECIFICITY: Strongest expression in liver.
DEVELOPMENTAL STAGE: First expressed at stage 10/11 of gastrulation. Higher levels found at stages 23/24 and 60-62. In the intestine, expression increased during metamorphosis (stage 62/64) and then, decreased. In the tail region, highest levels were found at the time of tail resorption. Activated, but at low levels, at stages 56-58 of hindlimb development.
INDUCTION: Slow-response activation by thyroid hormone (T3).
SIMILARITY: Belongs to the arginase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X69820; CAA49474.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

S29394; S29394.

NP_001095269.1; -.

3D structure databases

HSSP

P07824; 1RLA. [HSSP ENTRY / PDB]

ModBase

P30759.

Ontologies

GO:0004053;	Molecular function: arginase activity (inferred from electronic annotation from InterPro).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006525;	Biological process: arginine metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0000050;	Biological process: urea cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005924; Arginase.
IPR014033; Arginase_sub.
IPR006035; Ureohydrolase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.800.10; Ureohydrolase; 1.

PANTHER

PTHR11358:SF2; Arginase_sub; 1.
PTHR11358; Ureohydrolase; 1.

Pfam

PF00491; Arginase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00116; ARGINASE.

TIGRFAMs

TIGR01229; rocF_arginase; 1.

PROSITE

PS00147; ARGINASE_1; 1.
PS00148; ARGINASE_2; 1.
PS01053; ARGINASE_3; 1.

Genome annotation databases

GeneID

779061; -.

KEGG

xla:779061; -.

Phylogenomic databases

HOVERGEN

P30759; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Arginine metabolism; Hydrolase; Manganese; Metal-binding; Urea cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 316`	`316`	`Arginase-1.`	`PRO_0000173698`
`METAL`	`101 101`		`Manganese 1 (By similarity).`
`METAL`	`124 124`		`Manganese 1 (By similarity).`
`METAL`	`124 124`		`Manganese 2 (By similarity).`
`METAL`	`126 126`		`Manganese 2 (By similarity).`
`METAL`	`128 128`		`Manganese 1 (By similarity).`
`METAL`	`232 232`		`Manganese 1 (By similarity).`
`METAL`	`232 232`		`Manganese 2 (By similarity).`
`METAL`	`234 234`		`Manganese 2 (By similarity).`

Sequence information

Length: 316 AA [This is the length of the unprocessed precursor]

Molecular weight: 34566 Da [This is the MW of the unprocessed precursor]

CRC64: 8E6D08B20BF915ED [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKERHSVGV IGAPFSKGQP RRGVEEGPKY LREAGLIEKL REFGNDVRDC GDLDFPDVPN 

        70         80         90        100        110        120 
DTPFNNVKNP RTVGKATEIL ANAVTAVKKA DKTCQSIGGD HSLAVGTIAG HAAVHPNLCV 

       130        140        150        160        170        180 
VWVDAHADIN TPSTSPCGNL HGQPLSFLMK ELKAKMPAVP GFEWVKPCLR SKDIVYIGLR 

       190        200        210        220        230        240 
DVDPGEHYIL KTLGIKYLSM IEVDYLKDDK VMEETLEYLV GKHKRPIHLS FDIDGLDPSI 

       250        260        270        280        290        300 
APATGTPCPG GRTYREGRIL HEQLHKTGLL SGVDTIWMES TSRGETKRDV EVTVKTALDM 

       310 
TLSCFGKARE GFHAST

P30759 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools