Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Arginase-2, mitochondrial

Gene

ARG2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.1 Publication

Cofactori

Mn2+PROSITE-ProRule annotation1 PublicationNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation1 Publication

Pathwayi: urea cycle

This protein is involved in step 1 of the subpathway that synthesizes L-ornithine and urea from L-arginine.By similarity
Proteins known to be involved in this subpathway in this organism are:
  1. Arginase (ARG2), Arginase-2, mitochondrial (ARG2), Arginase-1 (ARG1)
This subpathway is part of the pathway urea cycle, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ornithine and urea from L-arginine, the pathway urea cycle and in Nitrogen metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi120Manganese 1Combined sources1 Publication1
Metal bindingi143Manganese 1Combined sources1 Publication1
Metal bindingi143Manganese 2Combined sources1 Publication1
Metal bindingi145Manganese 2Combined sources1 Publication1
Metal bindingi147Manganese 1Combined sources1 Publication1
Binding sitei202SubstrateCombined sources1 Publication1
Metal bindingi251Manganese 1Combined sources1 Publication1
Metal bindingi251Manganese 2Combined sources1 Publication1
Metal bindingi253Manganese 2Combined sources1 Publication1
Binding sitei265SubstrateBy similarity1
Binding sitei296SubstrateCombined sources1 Publication1

GO - Molecular functioni

  • arginase activity Source: CACAO
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

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.
ZFISH:HS01388-MONOMER.
BRENDAi3.5.3.1. 2681.
ReactomeiR-HSA-70635. Urea cycle.
SABIO-RKP78540.
UniPathwayiUPA00158; UER00270.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginase-2, mitochondrial (EC:3.5.3.11 Publication)
Alternative name(s):
Kidney-type arginase
Non-hepatic arginase
Type II arginase
Gene namesi
Name:ARG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:664. ARG2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

DisGeNETi384.
OpenTargetsiENSG00000081181.
PharmGKBiPA24948.

Chemistry databases

ChEMBLiCHEMBL1795148.
DrugBankiDB00125. L-Arginine.
DB00129. L-Ornithine.
GuidetoPHARMACOLOGYi1245.

Polymorphism and mutation databases

BioMutaiARG2.
DMDMi2492935.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 22MitochondrionSequence analysisAdd BLAST22
ChainiPRO_000000208423 – 354Arginase-2, mitochondrialAdd BLAST332

Proteomic databases

EPDiP78540.
MaxQBiP78540.
PaxDbiP78540.
PeptideAtlasiP78540.
PRIDEiP78540.

PTM databases

iPTMnetiP78540.
PhosphoSitePlusiP78540.

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

BgeeiENSG00000081181.
CleanExiHS_ARG2.
ExpressionAtlasiP78540. baseline and differential.
GenevisibleiP78540. HS.

Organism-specific databases

HPAiCAB009435.
HPA000663.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi106879. 4 interactors.
IntActiP78540. 1 interactor.
STRINGi9606.ENSP00000261783.

Chemistry databases

BindingDBiP78540.

Structurei

Secondary structure

1354
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 30Combined sources6
Helixi42 – 44Combined sources3
Helixi45 – 51Combined sources7
Helixi54 – 60Combined sources7
Beta strandi64 – 70Combined sources7
Turni83 – 85Combined sources3
Helixi89 – 108Combined sources20
Beta strandi112 – 116Combined sources5
Helixi120 – 122Combined sources3
Helixi123 – 133Combined sources11
Beta strandi138 – 145Combined sources8
Turni151 – 153Combined sources3
Helixi159 – 161Combined sources3
Helixi163 – 166Combined sources4
Helixi169 – 174Combined sources6
Helixi190 – 192Combined sources3
Beta strandi193 – 198Combined sources6
Helixi203 – 211Combined sources9
Beta strandi215 – 218Combined sources4
Helixi219 – 225Combined sources7
Helixi227 – 239Combined sources13
Beta strandi240 – 242Combined sources3
Beta strandi246 – 251Combined sources6
Helixi252 – 254Combined sources3
Turni257 – 259Combined sources3
Beta strandi262 – 265Combined sources4
Helixi273 – 285Combined sources13
Beta strandi289 – 295Combined sources7
Helixi299 – 301Combined sources3
Beta strandi302 – 304Combined sources3
Helixi305 – 322Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78540.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni145 – 149Substrate bindingCombined sources1 Publication5
Regioni156 – 158Substrate bindingCombined sources1 Publication3

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2965. Eukaryota.
COG0010. LUCA.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
InParanoidiP78540.
KOiK01476.
OMAiCVTIGGD.
OrthoDBiEOG091G0A38.
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

        10         20         30         40         50
MSLRGSLSRL LQTRVHSILK KSVHSVAVIG APFSQGQKRK GVEHGPAAIR
60 70 80 90 100
EAGLMKRLSS LGCHLKDFGD LSFTPVPKDD LYNNLIVNPR SVGLANQELA
110 120 130 140 150
EVVSRAVSDG YSCVTLGGDH SLAIGTISGH ARHCPDLCVV WVDAHADINT
160 170 180 190 200
PLTTSSGNLH GQPVSFLLRE LQDKVPQLPG FSWIKPCISS ASIVYIGLRD
210 220 230 240 250
VDPPEHFILK NYDIQYFSMR DIDRLGIQKV MERTFDLLIG KRQRPIHLSF
260 270 280 290 300
DIDAFDPTLA PATGTPVVGG LTYREGMYIA EEIHNTGLLS ALDLVEVNPQ
310 320 330 340 350
LATSEEEAKT TANLAVDVIA SSFGQTREGG HIVYDQLPTP SSPDESENQA

RVRI
Length:354
Mass (Da):38,578
Last modified:May 1, 1997 - v1
Checksum:i1624FAC7D515C68B
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033520240G → R.Corresponds to variant rs17104534dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Arginase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106879. 4 interactors.
IntActiP78540. 1 interactor.
STRINGi9606.ENSP00000261783.

Chemistry databases

BindingDBiP78540.
ChEMBLiCHEMBL1795148.
DrugBankiDB00125. L-Arginine.
DB00129. L-Ornithine.
GuidetoPHARMACOLOGYi1245.

PTM databases

iPTMnetiP78540.
PhosphoSitePlusiP78540.

Polymorphism and mutation databases

BioMutaiARG2.
DMDMi2492935.

Proteomic databases

EPDiP78540.
MaxQBiP78540.
PaxDbiP78540.
PeptideAtlasiP78540.
PRIDEiP78540.

Protocols and materials databases

DNASUi384.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261783; ENSP00000261783; ENSG00000081181.
GeneIDi384.
KEGGihsa:384.
UCSCiuc001xjs.4. human.

Organism-specific databases

CTDi384.
DisGeNETi384.
GeneCardsiARG2.
HGNCiHGNC:664. ARG2.
HPAiCAB009435.
HPA000663.
MIMi107830. gene.
neXtProtiNX_P78540.
OpenTargetsiENSG00000081181.
PharmGKBiPA24948.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2965. Eukaryota.
COG0010. LUCA.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
InParanoidiP78540.
KOiK01476.
OMAiCVTIGGD.
OrthoDBiEOG091G0A38.
PhylomeDBiP78540.
TreeFamiTF300034.

Enzyme and pathway databases

UniPathwayiUPA00158; UER00270.
BioCyciMetaCyc:HS01388-MONOMER.
ZFISH:HS01388-MONOMER.
BRENDAi3.5.3.1. 2681.
ReactomeiR-HSA-70635. Urea cycle.
SABIO-RKP78540.

Miscellaneous databases

ChiTaRSiARG2. human.
EvolutionaryTraceiP78540.
GenomeRNAii384.
PROiP78540.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000081181.
CleanExiHS_ARG2.
ExpressionAtlasiP78540. baseline and differential.
GenevisibleiP78540. HS.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 158 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.