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P07824

- ARGI1_RAT

UniProt

P07824 - ARGI1_RAT

Protein

Arginase-1

Gene

Arg1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.2 PublicationsPROSITE-ProRule annotation

    Enzyme regulationi

    Inactivated by diethyl pyrocarbonate (DEPC).

    Kineticsi

    1. KM=1.4 mM for arginine2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi101 – 1011Manganese 1
    Metal bindingi124 – 1241Manganese 1
    Metal bindingi124 – 1241Manganese 2
    Metal bindingi126 – 1261Manganese 2
    Metal bindingi128 – 1281Manganese 1
    Binding sitei183 – 1831Substrate
    Metal bindingi232 – 2321Manganese 1
    Metal bindingi232 – 2321Manganese 2
    Metal bindingi234 – 2341Manganese 2

    GO - Molecular functioni

    1. arginase activity Source: RGD
    2. manganese ion binding Source: RGD

    GO - Biological processi

    1. arginine metabolic process Source: RGD
    2. cellular response to dexamethasone stimulus Source: RGD
    3. cellular response to glucagon stimulus Source: RGD
    4. cellular response to hydrogen peroxide Source: RGD
    5. cellular response to interleukin-4 Source: RGD
    6. cellular response to lipopolysaccharide Source: RGD
    7. cellular response to transforming growth factor beta stimulus Source: RGD
    8. collagen biosynthetic process Source: RGD
    9. female pregnancy Source: RGD
    10. liver development Source: RGD
    11. lung development Source: RGD
    12. mammary gland involution Source: RGD
    13. maternal process involved in female pregnancy Source: RGD
    14. positive regulation of endothelial cell proliferation Source: RGD
    15. protein homotrimerization Source: RGD
    16. regulation of L-arginine import Source: RGD
    17. response to amine Source: RGD
    18. response to amino acid Source: RGD
    19. response to axon injury Source: RGD
    20. response to cadmium ion Source: RGD
    21. response to drug Source: RGD
    22. response to herbicide Source: RGD
    23. response to lipopolysaccharide Source: RGD
    24. response to manganese ion Source: RGD
    25. response to methylmercury Source: RGD
    26. response to peptide hormone Source: RGD
    27. response to selenium ion Source: RGD
    28. response to steroid hormone Source: RGD
    29. response to vitamin A Source: RGD
    30. response to vitamin E Source: RGD
    31. response to wounding Source: RGD
    32. response to zinc ion Source: RGD
    33. urea cycle Source: RGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Arginine metabolism, Urea cycle

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_216480. Urea cycle.
    SABIO-RKP07824.
    UniPathwayiUPA00158; UER00270.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginase-1 (EC:3.5.3.1)
    Alternative name(s):
    Liver-type arginase
    Type I arginase
    Gene namesi
    Name:Arg1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi2150. Arg1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. extracellular space Source: RGD
    3. neuronal cell body Source: RGD
    4. neuron projection Source: RGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi101 – 1011H → E: Reduced catalytic activity. No effect on manganese binding. 1 Publication
    Mutagenesisi128 – 1281D → E or N: Reduced manganese binding and strongly reduced catalytic activity. 1 Publication
    Mutagenesisi141 – 1411H → A, C or D: Strongly reduced catalytic activity. Minor effect on affinity for arginine. 1 Publication
    Mutagenesisi141 – 1411H → N: Reduced affinity for arginine and reduced catalytic activity. 1 Publication
    Mutagenesisi232 – 2321D → A: Loss of one manganese ion and strongly reduced catalytic activity. 1 Publication
    Mutagenesisi232 – 2321D → C: Reduced manganese binding and strongly reduced catalytic activity. 1 Publication
    Mutagenesisi234 – 2341D → A, E or H: Reduced manganese binding and strongly reduced catalytic activity. 1 Publication
    Mutagenesisi235 – 2351G → A: 56% of wild-type activity. 1 Publication
    Mutagenesisi235 – 2351G → R: Loss of manganese-binding and activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Arginase-1PRO_0000173697Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171N6-succinyllysineBy similarity
    Modified residuei72 – 721PhosphoserineBy similarity
    Modified residuei75 – 751N6-succinyllysineBy similarity
    Modified residuei281 – 2811PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP07824.
    PRIDEiP07824.

    PTM databases

    PhosphoSiteiP07824.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level).1 Publication

    Inductioni

    By arginine or homoarginine.

    Gene expression databases

    GenevestigatoriP07824.

    Interactioni

    Subunit structurei

    Homotrimer.2 Publications

    Protein-protein interaction databases

    BioGridi247899. 1 interaction.
    IntActiP07824. 1 interaction.
    MINTiMINT-4567374.
    STRINGi10116.ENSRNOP00000017911.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 125
    Beta strandi19 – 213
    Helixi22 – 265
    Helixi27 – 337
    Helixi36 – 405
    Beta strandi43 – 453
    Beta strandi47 – 526
    Beta strandi64 – 663
    Beta strandi67 – 693
    Helixi70 – 8920
    Beta strandi93 – 975
    Helixi101 – 1033
    Helixi104 – 11411
    Beta strandi119 – 1268
    Turni132 – 1343
    Beta strandi136 – 1383
    Helixi140 – 1423
    Helixi144 – 1485
    Helixi150 – 1523
    Beta strandi153 – 1564
    Turni160 – 1645
    Helixi171 – 1733
    Beta strandi174 – 1796
    Helixi184 – 19310
    Beta strandi196 – 1994
    Helixi200 – 2067
    Helixi208 – 22013
    Beta strandi221 – 2233
    Beta strandi227 – 2326
    Helixi233 – 2353
    Turni238 – 2403
    Beta strandi244 – 2463
    Helixi254 – 26714
    Beta strandi270 – 2767
    Helixi280 – 2823
    Beta strandi283 – 2853
    Helixi286 – 30318

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D3VX-ray1.70A/B1-323[»]
    1HQ5X-ray2.30A/B1-323[»]
    1HQFX-ray2.90A/B/C1-323[»]
    1HQGX-ray2.00A/B/C1-323[»]
    1HQHX-ray2.80A/B/C1-323[»]
    1HQXX-ray3.00A/B/C1-323[»]
    1P8MX-ray2.84A/B/C6-319[»]
    1P8NX-ray2.90A/B/C6-319[»]
    1P8OX-ray2.96A/B/C6-319[»]
    1P8PX-ray2.50A/B/C6-319[»]
    1P8QX-ray2.95A/B/C6-319[»]
    1P8RX-ray2.50A/B6-313[»]
    1P8SX-ray3.20A/B/C6-319[»]
    1R1OX-ray2.80A/B/C1-323[»]
    1RLAX-ray2.10A/B/C1-323[»]
    1T4PX-ray2.60A/B/C6-319[»]
    1T4RX-ray2.60A/B/C6-319[»]
    1T4SX-ray2.80A/B/C6-319[»]
    1T4TX-ray2.20A/B/C6-319[»]
    1T5FX-ray2.20A/B/C6-319[»]
    1T5GX-ray2.40A/B/C6-319[»]
    1TA1X-ray2.50A/B/C6-319[»]
    1TBHX-ray2.70A/B/C6-319[»]
    1TBJX-ray2.80A/B/C6-319[»]
    1TBLX-ray3.10A/B/C6-319[»]
    1ZPEX-ray1.70A/B/C6-319[»]
    1ZPGX-ray1.90A/B/C6-319[»]
    2RLAX-ray3.00A/B/C1-323[»]
    3E8QX-ray2.90A/B/C1-323[»]
    3E8ZX-ray2.00A/B/C1-323[»]
    3E9BX-ray2.15A/B/C1-323[»]
    3RLAX-ray2.54A/B/C1-323[»]
    4RLAX-ray2.94A/B/C1-323[»]
    5RLAX-ray2.74A/B/C1-323[»]
    ProteinModelPortaliP07824.
    SMRiP07824. Positions 6-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07824.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni126 – 1305Substrate binding
    Regioni137 – 1393Substrate binding

    Sequence similaritiesi

    Belongs to the arginase family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0010.
    GeneTreeiENSGT00530000063082.
    HOGENOMiHOG000204319.
    HOVERGENiHBG003030.
    InParanoidiP07824.
    KOiK01476.
    OMAiFLIRIEV.
    OrthoDBiEOG747PJ5.
    PhylomeDBiP07824.
    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.

    P07824-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSKPKPIEI IGAPFSKGQP RGGVEKGPAA LRKAGLVEKL KETEYNVRDH    50
    GDLAFVDVPN DSPFQIVKNP RSVGKANEQL AAVVAETQKN GTISVVLGGD 100
    HSMAIGSISG HARVHPDLCV IWVDAHTDIN TPLTTSSGNL HGQPVAFLLK 150
    ELKGKFPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYII KTLGIKYFSM 200
    TEVDKLGIGK VMEETFSYLL GRKKRPIHLS FDVDGLDPVF TPATGTPVVG 250
    GLSYREGLYI TEEIYKTGLL SGLDIMEVNP TLGKTPEEVT RTVNTAVALT 300
    LSCFGTKREG NHKPETDYLK PPK 323
    Length:323
    Mass (Da):34,973
    Last modified:April 1, 1990 - v2
    Checksum:i5A92CB0931F9A053
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti298 – 2981A → P in AAA40761. (PubMed:3571256)Curated
    Sequence conflicti298 – 2981A → P in AAA40760. (PubMed:3571256)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02720 mRNA. Translation: AAA40761.1.
    M17931
    , M17924, M17925, M17926, M17927, M17928, M17929, M17930 Genomic DNA. Translation: AAA40760.1.
    BC091158 mRNA. Translation: AAH91158.1.
    PIRiA26702.
    RefSeqiNP_058830.2. NM_017134.3.
    UniGeneiRn.9857.

    Genome annotation databases

    EnsembliENSRNOT00000017911; ENSRNOP00000017911; ENSRNOG00000013304.
    GeneIDi29221.
    KEGGirno:29221.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02720 mRNA. Translation: AAA40761.1 .
    M17931
    , M17924 , M17925 , M17926 , M17927 , M17928 , M17929 , M17930 Genomic DNA. Translation: AAA40760.1 .
    BC091158 mRNA. Translation: AAH91158.1 .
    PIRi A26702.
    RefSeqi NP_058830.2. NM_017134.3.
    UniGenei Rn.9857.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D3V X-ray 1.70 A/B 1-323 [» ]
    1HQ5 X-ray 2.30 A/B 1-323 [» ]
    1HQF X-ray 2.90 A/B/C 1-323 [» ]
    1HQG X-ray 2.00 A/B/C 1-323 [» ]
    1HQH X-ray 2.80 A/B/C 1-323 [» ]
    1HQX X-ray 3.00 A/B/C 1-323 [» ]
    1P8M X-ray 2.84 A/B/C 6-319 [» ]
    1P8N X-ray 2.90 A/B/C 6-319 [» ]
    1P8O X-ray 2.96 A/B/C 6-319 [» ]
    1P8P X-ray 2.50 A/B/C 6-319 [» ]
    1P8Q X-ray 2.95 A/B/C 6-319 [» ]
    1P8R X-ray 2.50 A/B 6-313 [» ]
    1P8S X-ray 3.20 A/B/C 6-319 [» ]
    1R1O X-ray 2.80 A/B/C 1-323 [» ]
    1RLA X-ray 2.10 A/B/C 1-323 [» ]
    1T4P X-ray 2.60 A/B/C 6-319 [» ]
    1T4R X-ray 2.60 A/B/C 6-319 [» ]
    1T4S X-ray 2.80 A/B/C 6-319 [» ]
    1T4T X-ray 2.20 A/B/C 6-319 [» ]
    1T5F X-ray 2.20 A/B/C 6-319 [» ]
    1T5G X-ray 2.40 A/B/C 6-319 [» ]
    1TA1 X-ray 2.50 A/B/C 6-319 [» ]
    1TBH X-ray 2.70 A/B/C 6-319 [» ]
    1TBJ X-ray 2.80 A/B/C 6-319 [» ]
    1TBL X-ray 3.10 A/B/C 6-319 [» ]
    1ZPE X-ray 1.70 A/B/C 6-319 [» ]
    1ZPG X-ray 1.90 A/B/C 6-319 [» ]
    2RLA X-ray 3.00 A/B/C 1-323 [» ]
    3E8Q X-ray 2.90 A/B/C 1-323 [» ]
    3E8Z X-ray 2.00 A/B/C 1-323 [» ]
    3E9B X-ray 2.15 A/B/C 1-323 [» ]
    3RLA X-ray 2.54 A/B/C 1-323 [» ]
    4RLA X-ray 2.94 A/B/C 1-323 [» ]
    5RLA X-ray 2.74 A/B/C 1-323 [» ]
    ProteinModelPortali P07824.
    SMRi P07824. Positions 6-319.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247899. 1 interaction.
    IntActi P07824. 1 interaction.
    MINTi MINT-4567374.
    STRINGi 10116.ENSRNOP00000017911.

    PTM databases

    PhosphoSitei P07824.

    Proteomic databases

    PaxDbi P07824.
    PRIDEi P07824.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000017911 ; ENSRNOP00000017911 ; ENSRNOG00000013304 .
    GeneIDi 29221.
    KEGGi rno:29221.

    Organism-specific databases

    CTDi 383.
    RGDi 2150. Arg1.

    Phylogenomic databases

    eggNOGi COG0010.
    GeneTreei ENSGT00530000063082.
    HOGENOMi HOG000204319.
    HOVERGENi HBG003030.
    InParanoidi P07824.
    KOi K01476.
    OMAi FLIRIEV.
    OrthoDBi EOG747PJ5.
    PhylomeDBi P07824.
    TreeFami TF300034.

    Enzyme and pathway databases

    UniPathwayi UPA00158 ; UER00270 .
    Reactomei REACT_216480. Urea cycle.
    SABIO-RK P07824.

    Miscellaneous databases

    EvolutionaryTracei P07824.
    NextBioi 608419.
    PROi P07824.

    Gene expression databases

    Genevestigatori P07824.

    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. "Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver arginase."
      Kawamoto S., Amaya Y., Murakami K., Tokunaga F., Iwanaga S., Kobayashi K., Saheki T., Kimura S., Mori M.
      J. Biol. Chem. 262:6280-6283(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Structural organization of the gene for rat liver-type arginase."
      Ohtake A., Takiguchi M., Shigeto Y., Amaya Y., Kawamoto S., Mori M.
      J. Biol. Chem. 263:2245-2249(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Liver.
    3. "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: Liver.
    4. "Functional consequences of the G235R mutation in liver arginase leading to hyperargininemia."
      Lavulo L.T., Emig F.A., Ash D.E.
      Arch. Biochem. Biophys. 399:49-55(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-235.
    5. "Structure of a unique binuclear manganese cluster in arginase."
      Kanyo Z.F., Scolnick L.R., Ash D.E., Christianson D.W.
      Nature 383:554-557(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    6. "Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function."
      Scolnick L.R., Kanyo Z.F., Cavalli R.C., Ash D.E., Christianson D.W.
      Biochemistry 36:10558-10565(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    7. "Arginase-boronic acid complex highlights a physiological role in erectile function."
      Cox J.D., Kim N.N., Traish A.M., Christianson D.W.
      Nat. Struct. Biol. 6:1043-1047(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    8. "Structural and functional importance of first-shell metal ligands in the binuclear manganese cluster of arginase I."
      Cama E., Emig F.A., Ash D.E., Christianson D.W.
      Biochemistry 42:7748-7758(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 6-319 OF MUTANTS ASN-101; GLU-101; ASN-128; GLU-128; ALA-232; CYS-232 AND GLU-234 IN COMPLEXES WITH MANGANESE IONS, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-101; ASP-128; ASP-232 AND ASP-234.
    9. "Design of amino acid aldehydes as transition-state analogue inhibitors of arginase."
      Shin H., Cama E., Christianson D.W.
      J. Am. Chem. Soc. 126:10278-10284(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 6-319 IN COMPLEX WITH MANGANESE IONS AND THE SYNTHETIC INHIBITOR (S)-2-AMINO-7-OXOHEPTANOIC ACID.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 6-319 OF MUTANTS ALA-141; ASN-141; ASP-141 AND CYS-141 IN COMPLEX WITH MANGANESE IONS, COFACTOR, MUTAGENESIS OF HIS-141, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiARGI1_RAT
    AccessioniPrimary (citable) accession number: P07824
    Secondary accession number(s): Q5BK93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3