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P78540

- ARGI2_HUMAN

UniProt

P78540 - ARGI2_HUMAN

Protein

Arginase-2, mitochondrial

Gene

ARG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    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 PublicationPROSITE-ProRule annotation

    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 – 2021SubstrateBy similarity
    Metal bindingi251 – 2511Manganese 1
    Metal bindingi251 – 2511Manganese 2
    Metal bindingi253 – 2531Manganese 2
    Binding sitei296 – 2961SubstrateBy 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

    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

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24948.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2222MitochondrionSequence AnalysisAdd
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP78540.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the arginase family.PROSITE-ProRule annotation

    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

    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: October 1, 2014
    This is version 142 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