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P78540

- ARGI2_HUMAN

UniProt

P78540 - ARGI2_HUMAN

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Protein

Arginase-2, mitochondrial

Gene
ARG2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

L-arginine + H2O = L-ornithine + urea.

Cofactori

Binds 2 manganese ions per subunit.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi120 – 1201Manganese 1
Metal bindingi143 – 1431Manganese 1
Metal bindingi143 – 1431Manganese 2
Metal bindingi145 – 1451Manganese 2
Metal bindingi147 – 1471Manganese 1
Binding sitei202 – 2021Substrate By similarity
Metal bindingi251 – 2511Manganese 1
Metal bindingi251 – 2511Manganese 2
Metal bindingi253 – 2531Manganese 2
Binding sitei296 – 2961Substrate By similarity

GO - Molecular functioni

  1. arginase activity Source: Reactome
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine metabolic process Source: UniProtKB-KW
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. nitric oxide biosynthetic process Source: ProtInc
  4. small molecule metabolic process Source: Reactome
  5. striated muscle contraction Source: Ensembl
  6. urea cycle Source: Reactome
  7. ureteric bud development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arginine metabolism, Urea cycle

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS01388-MONOMER.
ReactomeiREACT_847. Urea cycle.
SABIO-RKP78540.
UniPathwayiUPA00158; UER00270.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginase-2, mitochondrial (EC:3.5.3.1)
Alternative name(s):
Kidney-type arginase
Non-hepatic arginase
Type II arginase
Gene namesi
Name:ARG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:664. ARG2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24948.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2222Mitochondrion Reviewed predictionAdd
BLAST
Chaini23 – 354332Arginase-2, mitochondrialPRO_0000002084Add
BLAST

Proteomic databases

MaxQBiP78540.
PaxDbiP78540.
PeptideAtlasiP78540.
PRIDEiP78540.

PTM databases

PhosphoSiteiP78540.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiP78540.
CleanExiHS_ARG2.
GenevestigatoriP78540.

Organism-specific databases

HPAiCAB009435.
HPA000663.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi106879. 1 interaction.
STRINGi9606.ENSP00000261783.

Structurei

Secondary structure

1
354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 306
Helixi42 – 443
Helixi45 – 517
Helixi54 – 607
Beta strandi64 – 707
Turni83 – 853
Helixi89 – 10820
Beta strandi112 – 1165
Helixi120 – 1223
Helixi123 – 13311
Beta strandi138 – 1458
Turni151 – 1533
Helixi159 – 1613
Helixi163 – 1664
Helixi169 – 1746
Helixi190 – 1923
Beta strandi193 – 1986
Helixi203 – 2119
Beta strandi215 – 2184
Helixi219 – 2257
Helixi227 – 23913
Beta strandi240 – 2423
Beta strandi246 – 2516
Helixi252 – 2543
Turni257 – 2593
Beta strandi262 – 2654
Helixi273 – 28513
Beta strandi289 – 2957
Helixi299 – 3013
Beta strandi302 – 3043
Helixi305 – 32218

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PQ3X-ray2.70A/B/C/D/E/F24-329[»]
4HZEX-ray1.60A/B/C24-329[»]
4I06X-ray1.80A/B/C24-329[»]
4IE2X-ray2.21A/B/C24-329[»]
4IE3X-ray2.35A/B/C24-329[»]
4IXUX-ray1.90A/B/C24-329[»]
4IXVX-ray2.30A/B/C24-329[»]
ProteinModelPortaliP78540.
SMRiP78540. Positions 24-329.

Miscellaneous databases

EvolutionaryTraceiP78540.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni145 – 1495Substrate binding By similarity
Regioni156 – 1583Substrate binding By similarity

Sequence similaritiesi

Belongs to the arginase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0010.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
InParanoidiP78540.
KOiK01476.
OMAiRNMKNPR.
OrthoDBiEOG747PJ5.
PhylomeDBiP78540.
TreeFamiTF300034.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P78540-1 [UniParc]FASTAAdd to Basket

« Hide

MSLRGSLSRL LQTRVHSILK KSVHSVAVIG APFSQGQKRK GVEHGPAAIR    50
EAGLMKRLSS LGCHLKDFGD LSFTPVPKDD LYNNLIVNPR SVGLANQELA 100
EVVSRAVSDG YSCVTLGGDH SLAIGTISGH ARHCPDLCVV WVDAHADINT 150
PLTTSSGNLH GQPVSFLLRE LQDKVPQLPG FSWIKPCISS ASIVYIGLRD 200
VDPPEHFILK NYDIQYFSMR DIDRLGIQKV MERTFDLLIG KRQRPIHLSF 250
DIDAFDPTLA PATGTPVVGG LTYREGMYIA EEIHNTGLLS ALDLVEVNPQ 300
LATSEEEAKT TANLAVDVIA SSFGQTREGG HIVYDQLPTP SSPDESENQA 350
RVRI 354
Length:354
Mass (Da):38,578
Last modified:May 1, 1997 - v1
Checksum:i1624FAC7D515C68B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti240 – 2401G → R.
Corresponds to variant rs17104534 [ dbSNP | Ensembl ].
VAR_033520

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS9785.1.
RefSeqiNP_001163.1. NM_001172.3.
UniGeneiHs.226007.

Genome annotation databases

EnsembliENST00000261783; ENSP00000261783; ENSG00000081181.
GeneIDi384.
KEGGihsa:384.
UCSCiuc001xjs.3. human.

Polymorphism databases

DMDMi2492935.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Arginase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS9785.1.
RefSeqi NP_001163.1. NM_001172.3.
UniGenei Hs.226007.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PQ3 X-ray 2.70 A/B/C/D/E/F 24-329 [» ]
4HZE X-ray 1.60 A/B/C 24-329 [» ]
4I06 X-ray 1.80 A/B/C 24-329 [» ]
4IE2 X-ray 2.21 A/B/C 24-329 [» ]
4IE3 X-ray 2.35 A/B/C 24-329 [» ]
4IXU X-ray 1.90 A/B/C 24-329 [» ]
4IXV X-ray 2.30 A/B/C 24-329 [» ]
ProteinModelPortali P78540.
SMRi P78540. Positions 24-329.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106879. 1 interaction.
STRINGi 9606.ENSP00000261783.

Chemistry

BindingDBi P78540.
ChEMBLi CHEMBL1795148.
DrugBanki DB00125. L-Arginine.
DB00129. L-Ornithine.

PTM databases

PhosphoSitei P78540.

Polymorphism databases

DMDMi 2492935.

Proteomic databases

MaxQBi P78540.
PaxDbi P78540.
PeptideAtlasi P78540.
PRIDEi P78540.

Protocols and materials databases

DNASUi 384.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261783 ; ENSP00000261783 ; ENSG00000081181 .
GeneIDi 384.
KEGGi hsa:384.
UCSCi uc001xjs.3. human.

Organism-specific databases

CTDi 384.
GeneCardsi GC14P068086.
HGNCi HGNC:664. ARG2.
HPAi CAB009435.
HPA000663.
MIMi 107830. gene.
neXtProti NX_P78540.
PharmGKBi PA24948.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0010.
HOGENOMi HOG000204319.
HOVERGENi HBG003030.
InParanoidi P78540.
KOi K01476.
OMAi RNMKNPR.
OrthoDBi EOG747PJ5.
PhylomeDBi P78540.
TreeFami TF300034.

Enzyme and pathway databases

UniPathwayi UPA00158 ; UER00270 .
BioCyci MetaCyc:HS01388-MONOMER.
Reactomei REACT_847. Urea cycle.
SABIO-RK P78540.

Miscellaneous databases

EvolutionaryTracei P78540.
GenomeRNAii 384.
NextBioi 1607.
PROi P78540.
SOURCEi Search...

Gene expression databases

Bgeei P78540.
CleanExi HS_ARG2.
Genevestigatori P78540.

Family and domain databases

Gene3Di 3.40.800.10. 1 hit.
InterProi IPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view ]
PANTHERi PTHR11358. PTHR11358. 1 hit.
Pfami PF00491. Arginase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036979. Arginase. 1 hit.
PRINTSi PR00116. ARGINASE.
TIGRFAMsi TIGR01229. rocF_arginase. 1 hit.
PROSITEi PS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiARGI2_HUMAN
AccessioniPrimary (citable) accession number: P78540
Secondary accession number(s): B2R690, Q6FHY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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