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Reviewed, UniProtKB/Swiss-Prot P78540 (ARGI2_HUMAN)

Last modified July 22, 2008. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Arginase-2, mitochondrial
      Short name(s)=Arginase II
    EC=3.5.3.1
Alternative name(s):
    Non-hepatic arginase
    Kidney-type arginase
Gene names
Name: ARG2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Catalytic activity

L-arginine + H(2)O = L-ornithine + urea.

Cofactor

Manganese.

Pathway

Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.

Subunit structure

Homohexamer.

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 processArginine metabolism
Urea cycle
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure

Gene Ontology (GO)

   Biological processnitric oxide biosynthetic process Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentmitochondrion Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionarginase activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – 2222Mitochondrion Potential
Chain23 – 354332Arginase-2, mitochondrial

Sites

Metal binding1201Manganese 1 By similarity
Metal binding1431Manganese 1 By similarity
Metal binding1431Manganese 2 By similarity
Metal binding1451Manganese 2 By similarity
Metal binding1471Manganese 1 By similarity
Metal binding2511Manganese 1 By similarity
Metal binding2511Manganese 2 By similarity
Metal binding2531Manganese 2 By similarity

Natural variations

Natural variant2401G → R: dbSNP rs17104534.

Secondary structure

1 ........................................................ 354
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P78540-1 [UniParc].

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

FASTA35438,578
        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

« Hide

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References

« Hide '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]"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.
[7]"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.

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Web resources

Wikipedia

Arginase entry

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Cross-references

Sequence databases

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.
BC001350 mRNA. Translation: AAH01350.1.
BC008464 mRNA. Translation: AAH08464.1.
BC029050 mRNA. Translation: AAH29050.1.
RefSeqNP_001163.1.
UniGeneHs.705408

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1PQ3X-ray2.70A/B/C/D/E/F24-329[»]
ModBaseSearch...

Proteomic databases

PeptideAtlasP78540.

Genome annotation databases

EnsemblENSG00000081181. Homo sapiens. [Contig view]
GeneID384.
KEGGhsa:384.

Organism-specific databases

H-InvDBHIX0011752.
HGNCHGNC:664. ARG2.
HPACAB009435.
HPA000663.
MIM107830. gene.
PharmGKBPA24948.
GenAtlasSearch...
GeneCardsSearch...
GeneLynxSearch...

Phylogenomic databases

HOGENOMP78540.
HOVERGENP78540.

Enzyme and pathway databases

BioCycMetaCyc:MON-11285.

Gene expression databases

ArrayExpressP78540.
CleanExHS_ARG2.
GermOnlineENSG00000081181. Homo sapiens.

Family and domain databases

InterProIPR005924. Arginase.
IPR014033. Arginase_sub.
IPR006035. Ureohydrolase.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHERPTHR11358:SF2. Arginase_sub. 1 hit.
PTHR11358. Ureohydrolase. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01229. rocF_arginase. 1 hit.
PROSITEPS00147. ARGINASE_1. 1 hit.
PS00148. ARGINASE_2. 1 hit.
PS01053. ARGINASE_3. 1 hit.
[Graphical view]
ProDomP78540.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

DrugBankDB00125. L-Arginine.
DB00129. L-Ornithine.
LinkHubP78540.
SOURCESearch...
ProtoNetSearch...

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Entry information

Entry nameARGI2_HUMAN
AccessionPrimary (citable) accession number: P78540
Secondary accession number(s): Q6FHY8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: July 22, 2008
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

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Human chromosome 14: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents