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P78540 (ARGI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

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

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.

Ontologies

Keywords
   Biological processArginine metabolism
Urea cycle
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarginine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

nitric oxide biosynthetic process

Traceable author statement Ref.1. Source: ProtInc

striated muscle contraction

Inferred from electronic annotation. Source: Compara

urea cycle

Traceable author statement. Source: Reactome

ureteric bud development

Inferred from electronic annotation. Source: Compara

   Cellular_componentmitochondrial matrix

Traceable author statement. Source: Reactome

   Molecular_functionarginase activity

Inferred from experiment. Source: Reactome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion Potential
Chain23 – 354332Arginase-2, mitochondrial
PRO_0000002084

Regions

Region145 – 1495Substrate binding By similarity
Region156 – 1583Substrate binding By similarity

Sites

Metal binding1201Manganese 1
Metal binding1431Manganese 1
Metal binding1431Manganese 2
Metal binding1451Manganese 2
Metal binding1471Manganese 1
Metal binding2511Manganese 1
Metal binding2511Manganese 2
Metal binding2531Manganese 2
Binding site2021Substrate By similarity
Binding site2961Substrate By similarity

Natural variations

Natural variant2401G → R.
Corresponds to variant rs17104534 [ dbSNP | Ensembl ].
VAR_033520

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P78540 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Lung, Muscle, Prostate and Testis.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [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.

Web resources

Wikipedia

Arginase entry

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.
IPIIPI00020332.
RefSeqNP_001163.1. NM_001172.3.
UniGeneHs.226007.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PQ3X-ray2.70A/B/C/D/E/F24-329[»]
ProteinModelPortalP78540.
ModBaseSearch...

Protein-protein interaction databases

STRING9606.ENSP00000261783.

PTM databases

PhosphoSiteP78540.

Polymorphism databases

DMDM2492935.

Proteomic databases

PaxDbP78540.
PeptideAtlasP78540.
PRIDEP78540.

Protocols and materials databases

DNASU384.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261783; ENSP00000261783; ENSG00000081181.
GeneID384.
KEGGhsa:384.
UCSCuc001xjs.3. human.

Organism-specific databases

CTD384.
GeneCardsGC14P068086.
HGNCHGNC:664. ARG2.
HPACAB009435.
HPA000663.
MIM107830. gene.
neXtProtNX_P78540.
PharmGKBPA24948.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0010.
HOGENOMHOG000204319.
HOVERGENHBG003030.
InParanoidP78540.
KOK01476.
OMAFLDDRGK.
OrthoDBEOG4FR0S2.
PhylomeDBP78540.

Enzyme and pathway databases

BioCycMetaCyc:HS01388-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP78540.
UniPathwayUPA00158; UER00270.

Gene expression databases

BgeeP78540.
CleanExHS_ARG2.
GenevestigatorP78540.
GermOnlineENSG00000081181. Homo sapiens.

Family and domain databases

Gene3D3.40.800.10. 1 hit.
InterProIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERPTHR11358. PTHR11358. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01229. rocF_arginase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP78540.
ChEMBLCHEMBL1795148.
DrugBankDB00125. L-Arginine.
DB00129. L-Ornithine.
EvolutionaryTraceP78540.
GenomeRNAi384.
NextBio1607.
SOURCESearch...

Entry information

Entry nameARGI2_HUMAN
AccessionPrimary (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: May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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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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

SIMILARITY comments

Index of protein domains and families

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