Arginase-2, mitochondrial precursor

Names and origin

Protein names

Recommended name:
    Arginase-2, mitochondrial
    EC=3.5.3.1
Alternative name(s):
    Type II arginase
    Non-hepatic arginase
    Kidney-type arginase

Gene names

Name:

ARG2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase. Since NO synthase is found in the penile corpus cavernosum smooth muscle, the clitoral corpus cavernosum and the vagina, arginase II plays a role in both male and female sexual arousal. It is therefore a potential target for the treatment of male and female sexual arousal disorders. Ref.10
Catalytic activity	L-arginine + H₂O = L-ornithine + urea.
Cofactor	Binds 2 manganese ions per subunit. Ref.10
Pathway	Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
Subunit structure	Homotrimer. Ref.10
Subcellular location	Mitochondrion.
Tissue specificity	Expressed most strongly in kidney and prostate, much less strongly in the brain, skeletal muscle, placenta, lung, mammary gland, macrophage, uterus, testis and gut, but apparently not in the liver, heart and pancreas.
Sequence similarities	Belongs to the arginase family.

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Ontologies

Keywords
Biological process	Arginine metabolism Urea cycle
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	arginine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW nitric oxide biosynthetic process Ref.1 Traceable author statement. Source: ProtInc urea cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Ref.1 Traceable author statement. Source: ProtInc
Molecular function	arginase activity Traceable author statement. Source: ProtInc manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 22

22

Mitochondrion Potential

Chain

23 – 354

332

Arginase-2, mitochondrial

PRO_0000002084

Regions

Region

145 – 149

5

Substrate binding By similarity

Region

156 – 158

3

Substrate binding By similarity

Sites

Metal binding

120

1

Manganese 1

Metal binding

143

1

Manganese 1

Metal binding

143

1

Manganese 2

Metal binding

145

1

Manganese 2

Metal binding

147

1

Manganese 1

Metal binding

251

1

Manganese 1

Metal binding

251

1

Manganese 2

Metal binding

253

1

Manganese 2

Binding site

202

1

Substrate By similarity

Binding site

296

1

Substrate By similarity

Natural variations

Natural variant

240

1

G → R: dbSNP rs17104534.

VAR_033520

Secondary structure

1

.

354

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P78540-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 1624FAC7D515C68B
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FASTA

354

38,578

        10         20         30         40         50         60 
MSLRGSLSRL LQTRVHSILK KSVHSVAVIG APFSQGQKRK GVEHGPAAIR EAGLMKRLSS 

        70         80         90        100        110        120 
LGCHLKDFGD LSFTPVPKDD LYNNLIVNPR SVGLANQELA EVVSRAVSDG YSCVTLGGDH 

       130        140        150        160        170        180 
SLAIGTISGH ARHCPDLCVV WVDAHADINT PLTTSSGNLH GQPVSFLLRE LQDKVPQLPG 

       190        200        210        220        230        240 
FSWIKPCISS ASIVYIGLRD VDPPEHFILK NYDIQYFSMR DIDRLGIQKV MERTFDLLIG 

       250        260        270        280        290        300 
KRQRPIHLSF DIDAFDPTLA PATGTPVVGG LTYREGMYIA EEIHNTGLLS ALDLVEVNPQ 

       310        320        330        340        350 
LATSEEEAKT TANLAVDVIA SSFGQTREGG HIVYDQLPTP SSPDESENQA RVRI

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage-like cell line." Gotoh T., Sonoki T., Nagasaki A., Terada K., Takiguchi M., Mori M. FEBS Lett. 395:119-122(1996) [PubMed: 8898077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning and characterization of the human type II arginase gene." Vockley J.G., Jenkinson C.P., Shukla H., Kern R.M., Grody W.W., Cederbaum S.D. Genomics 38:118-123(1996) [PubMed: 8954792] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Human type II arginase: sequence analysis and tissue-specific expression." Morris S.M. Jr., Bhamidipati D., Kepka-Lenhart D. Gene 193:157-161(1997) [PubMed: 9256072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[4]	Lee Y.T., Miller J.L. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Erythroblast.
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Hippocampus.
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Lung, Muscle, Prostate and Testis.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"Human arginase II: crystal structure and physiological role in male and female sexual arousal." Cama E., Colleluori D.M., Emig F.A., Shin H., Kim S.W., Kim N.N., Traish A.M., Ash D.E., Christianson D.W. Biochemistry 42:8445-8451(2003) [PubMed: 12859189] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-329 IN COMPLEX WITH MANGANESE IONS AND S-2-(BORONOETHYL)-L-CYSTEINE, COFACTOR, SUBUNIT, FUNCTION.
+	Additional computationally mapped references.

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Web resources

Wikipedia

Arginase entry

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D86724 mRNA. Translation: BAA13158.1.
U75667 mRNA. Translation: AAB39855.1.
U82256 mRNA. Translation: AAC51664.1.
AY074489 mRNA. Translation: AAL71548.1.
CR536550 mRNA. Translation: CAG38787.1.
AK312484 mRNA. Translation: BAG35387.1.
CH471061 Genomic DNA. Translation: EAW80943.1.
BC001350 mRNA. Translation: AAH01350.1.
BC008464 mRNA. Translation: AAH08464.1.
BC029050 mRNA. Translation: AAH29050.1.

IPI

IPI00020332.

RefSeq

NP_001163.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PQ3	X-ray	2.70	A/B/C/D/E/F	24-329	[»]

ModBase

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Protein-protein interaction databases

STRING

P78540.

Proteomic databases

PeptideAtlas

P78540.

PRIDE

P78540.

Genome annotation databases

Ensembl

ENST00000261783; ENSP00000261783; ENSG00000081181; Homo sapiens. [Genome view]

GeneID

384.

KEGG

hsa:384.

UCSC

uc001xjs.1. human.

Organism-specific databases

CTD

384.

GeneCards

GC14P067156.

H-InvDB

HIX0011752.

HGNC

HGNC:664. ARG2.

HPA

CAB009435.
HPA000663.

MIM

107830. gene.

PharmGKB

PA24948.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12844.

HOGENOM

HBG391953.

HOVERGEN

P78540.

InParanoid

P78540.

OMA

TYREAQL.

OrthoDB

EOG9T4GF6.

PhylomeDB

P78540.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-11285.

BRENDA

3.5.3.1. 247.

Gene expression databases

ArrayExpress

P78540.

Bgee

P78540.

CleanEx

HS_ARG2.

Genevestigator

P78540.

GermOnline

ENSG00000081181. Homo sapiens.

Family and domain databases

InterPro

IPR005924. Arginase.
IPR014033. Arginase_sub.
IPR006035. Ureohydrolase.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]

Gene3D

G3DSA:3.40.800.10. Ureohydrolase. 1 hit.

PANTHER

PTHR11358:SF2. Arginase_sub. 1 hit.
PTHR11358. Ureohydrolase. 1 hit.

Pfam

PF00491. Arginase. 1 hit.
[Graphical view]

PRINTS

PR00116. ARGINASE.

TIGRFAMs

TIGR01229. rocF_arginase. 1 hit.

PROSITE

PS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00125. L-Arginine.
DB00129. L-Ornithine.

NextBio

1607.

SOURCE

Search...

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Entry information

Entry name

ARGI2_HUMAN

Accession

Primary (citable) accession number: P78540
Secondary accession number(s): B2R690, Q6FHY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	February 9, 2010
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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