[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Intestine; 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).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-360. TISSUE=Eye; NIH - Xenopus Gene Collection (XGC) project; Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: As well as its role in the urea cycle, may be involved in tissue remodeling.
CATALYTIC ACTIVITY: L-arginine + H₂O = L-ornithine + urea.
COFACTOR: Manganese (By similarity).
PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1 .
SUBUNIT: Homotrimer (By similarity).
TISSUE SPECIFICITY: Expressed at differing tadpole stages in tail, intestine, hindlimb and trunk region. Strongest in tadpole tail.
DEVELOPMENTAL STAGE: First detected in early tailbud (stage 23/24). Highest levels in whole tadpole found around stage 47/48. In the intestine, increased levels are found during metamorphosis (stages 58-64) and in the hindlimb, expressed at low levels during metamorphosis until stage 66 when levels dramatically increase. In the tail, a constant high level of expression is found throughout metamorphosis.
INDUCTION: 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

U08408; AAA56893.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC094076; AAH94076.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I51665; I51665.

UniGene

Xl.893

3D structure databases

HSSP

P78540; 1PQ3. [HSSP ENTRY / PDB]

SMR

Q91555; 26-331.

ModBase

Q91555.

Organism-specific databases

Xenbase

XB-FEAT-482623; arg2.

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.

ProtoNet

Q91555.

Phylogenomic databases

HOVERGEN

Q91555; -.

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`	`1 360`	`360`	`Arginase, non-hepatic 3.`	`PRO_0000173701`
`METAL`	`122 122`		`Manganese 1 (By similarity).`
`METAL`	`145 145`		`Manganese 1 (By similarity).`
`METAL`	`145 145`		`Manganese 2 (By similarity).`
`METAL`	`147 147`		`Manganese 2 (By similarity).`
`METAL`	`149 149`		`Manganese 1 (By similarity).`
`METAL`	`253 253`		`Manganese 1 (By similarity).`
`METAL`	`253 253`		`Manganese 2 (By similarity).`
`METAL`	`255 255`		`Manganese 2 (By similarity).`

Sequence information

Length: 360 AA [This is the length of the unprocessed precursor]

Molecular weight: 39238 Da [This is the MW of the unprocessed precursor]

CRC64: F1515DED32514662 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSIRSNFVRL LKKQVNIIKL QKKCSHSVAV IGAPFSKGQK RRGVEHGPAA IRSAGLIDRL 

        70         80         90        100        110        120 
SNLGCNVCDF GDLHFSQVPN DEQYNSIVKH PRTVGLACKV LAKEVGKAVG AGHTCVTLGG 

       130        140        150        160        170        180 
DHSLAFGSIT GHAQQCPDLC VIWVDAHADI NTPLTTPSGN LHGQPVSFLL RELQDKIPPI 

       190        200        210        220        230        240 
PGFSWAKPCL SKSDIVYIGL RDLDPAEQFI LKNYNISYYS MRHIDCMGIR KVMEKTFDQL 

       250        260        270        280        290        300 
LGRRDRPIHL SFDIDAFDPA LAPATGTPVI GGLTYREGVY ITEEIHNTGM LSALDLVEVN 

       310        320        330        340        350        360 
PVLATTSEEV KATANLAVDV IASCFGQTRE GAHTRADTII DVLPTPSTSY ESDNEEQVRI

Q91555 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