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Protein

Arginase-1

Gene

Arg1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-arginine + H2O = L-ornithine + urea.2 Publications

Cofactori

Mn2+PROSITE-ProRule annotation6 PublicationsNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation6 Publications

Enzyme regulationi

Inactivated by diethyl pyrocarbonate (DEPC).

Kineticsi

  1. KM=1.4 mM for arginine2 Publications

    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-1 (Arg1), Arginase (Arg2), Arginase-2, mitochondrial (Arg2), Arginase (Arg2)
    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 bindingi101Manganese 1Combined sources5 Publications1
    Metal bindingi124Manganese 1Combined sources6 Publications1
    Metal bindingi124Manganese 2Combined sources6 Publications1
    Metal bindingi126Manganese 2Combined sources6 Publications1
    Metal bindingi128Manganese 1Combined sources6 Publications1
    Binding sitei183SubstrateCombined sources1
    Metal bindingi232Manganese 1Combined sources6 Publications1
    Metal bindingi232Manganese 2Combined sources6 Publications1
    Metal bindingi234Manganese 2Combined sources6 Publications1
    Binding sitei246SubstrateBy similarity1
    Binding sitei277SubstrateBy similarity1

    GO - Molecular functioni

    • arginase activity Source: RGD
    • manganese ion binding Source: RGD

    GO - Biological processi

    • aging Source: RGD
    • arginine catabolic process to ornithine Source: RGD
    • arginine metabolic process Source: RGD
    • cellular response to dexamethasone stimulus Source: RGD
    • cellular response to glucagon stimulus Source: RGD
    • cellular response to hydrogen peroxide Source: RGD
    • cellular response to interleukin-4 Source: RGD
    • cellular response to lipopolysaccharide Source: RGD
    • cellular response to transforming growth factor beta stimulus Source: RGD
    • collagen biosynthetic process Source: RGD
    • female pregnancy Source: RGD
    • liver development Source: RGD
    • lung development Source: RGD
    • mammary gland involution Source: RGD
    • maternal process involved in female pregnancy Source: RGD
    • positive regulation of endothelial cell proliferation Source: RGD
    • protein homotrimerization Source: RGD
    • regulation of L-arginine import Source: RGD
    • response to amine Source: RGD
    • response to amino acid Source: RGD
    • response to axon injury Source: RGD
    • response to cadmium ion Source: RGD
    • response to drug Source: RGD
    • response to herbicide Source: RGD
    • response to lipopolysaccharide Source: RGD
    • response to manganese ion Source: RGD
    • response to methylmercury Source: RGD
    • response to peptide hormone Source: RGD
    • response to selenium ion Source: RGD
    • response to steroid hormone Source: RGD
    • response to vitamin A Source: RGD
    • response to vitamin E Source: RGD
    • response to wounding Source: RGD
    • response to zinc ion Source: RGD
    • urea cycle Source: RGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Arginine metabolism, Urea cycle

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.5.3.1. 5301.
    ReactomeiR-RNO-6798695. Neutrophil degranulation.
    R-RNO-70635. Urea cycle.
    SABIO-RKP07824.
    UniPathwayiUPA00158; UER00270.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginase-1 (EC:3.5.3.12 Publications)
    Alternative name(s):
    Liver-type arginase
    Type I arginase
    Gene namesi
    Name:Arg1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 1

    Organism-specific databases

    RGDi2150. Arg1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: RGD
    • extracellular exosome Source: Ensembl
    • extracellular space Source: RGD
    • mitochondrial outer membrane Source: RGD
    • neuronal cell body Source: RGD
    • neuron projection Source: RGD
    • nucleus Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi101H → E: Reduced catalytic activity. No effect on manganese binding. 1 Publication1
    Mutagenesisi128D → E or N: Reduced manganese binding and strongly reduced catalytic activity. 1 Publication1
    Mutagenesisi141H → A, C or D: Strongly reduced catalytic activity. Minor effect on affinity for arginine. 1 Publication1
    Mutagenesisi141H → N: Reduced affinity for arginine and reduced catalytic activity. 1 Publication1
    Mutagenesisi232D → A: Loss of one manganese ion and strongly reduced catalytic activity. 1 Publication1
    Mutagenesisi232D → C: Reduced manganese binding and strongly reduced catalytic activity. 1 Publication1
    Mutagenesisi234D → A, E or H: Reduced manganese binding and strongly reduced catalytic activity. 1 Publication1
    Mutagenesisi235G → A: 56% of wild-type activity. 1 Publication1
    Mutagenesisi235G → R: Loss of manganese-binding and activity. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL3232699.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001736971 – 323Arginase-1Add BLAST323

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei17N6-succinyllysineBy similarity1
    Modified residuei62PhosphoserineCombined sources1
    Modified residuei72PhosphoserineBy similarity1
    Modified residuei75N6-succinyllysineBy similarity1
    Modified residuei163PhosphoserineBy similarity1
    Modified residuei217PhosphoserineBy similarity1
    Modified residuei281PhosphothreonineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP07824.
    PRIDEiP07824.

    PTM databases

    iPTMnetiP07824.
    PhosphoSitePlusiP07824.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level).1 Publication

    Inductioni

    By arginine or homoarginine.

    Gene expression databases

    BgeeiENSRNOG00000013304.
    GenevisibleiP07824. RN.

    Interactioni

    Subunit structurei

    Homotrimer.2 Publications

    Protein-protein interaction databases

    BioGridi247899. 2 interactors.
    IntActiP07824. 1 interactor.
    MINTiMINT-4567374.
    STRINGi10116.ENSRNOP00000017911.

    Chemistry databases

    BindingDBiP07824.

    Structurei

    Secondary structure

    1323
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi8 – 12Combined sources5
    Beta strandi19 – 21Combined sources3
    Helixi22 – 26Combined sources5
    Helixi27 – 33Combined sources7
    Helixi36 – 40Combined sources5
    Beta strandi43 – 45Combined sources3
    Beta strandi47 – 52Combined sources6
    Beta strandi64 – 66Combined sources3
    Beta strandi67 – 69Combined sources3
    Helixi70 – 89Combined sources20
    Beta strandi93 – 97Combined sources5
    Helixi101 – 103Combined sources3
    Helixi104 – 114Combined sources11
    Beta strandi119 – 126Combined sources8
    Turni132 – 134Combined sources3
    Beta strandi136 – 138Combined sources3
    Helixi140 – 142Combined sources3
    Helixi144 – 148Combined sources5
    Helixi150 – 152Combined sources3
    Beta strandi153 – 156Combined sources4
    Turni160 – 164Combined sources5
    Helixi171 – 173Combined sources3
    Beta strandi174 – 179Combined sources6
    Helixi184 – 193Combined sources10
    Beta strandi196 – 199Combined sources4
    Helixi200 – 206Combined sources7
    Helixi208 – 220Combined sources13
    Beta strandi221 – 223Combined sources3
    Beta strandi227 – 232Combined sources6
    Helixi233 – 235Combined sources3
    Turni238 – 240Combined sources3
    Beta strandi244 – 246Combined sources3
    Helixi254 – 267Combined sources14
    Beta strandi270 – 276Combined sources7
    Helixi280 – 282Combined sources3
    Beta strandi283 – 285Combined sources3
    Helixi286 – 303Combined sources18

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP07824.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni126 – 130Substrate bindingCombined sources5
    Regioni137 – 139Substrate bindingCombined sources3

    Sequence similaritiesi

    Belongs to the arginase family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiKOG2965. Eukaryota.
    COG0010. LUCA.
    GeneTreeiENSGT00530000063082.
    HOGENOMiHOG000204319.
    HOVERGENiHBG003030.
    InParanoidiP07824.
    KOiK01476.
    OMAiEQECDVK.
    OrthoDBiEOG091G0A38.
    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

            10         20         30         40         50
    MSSKPKPIEI IGAPFSKGQP RGGVEKGPAA LRKAGLVEKL KETEYNVRDH
    60 70 80 90 100
    GDLAFVDVPN DSPFQIVKNP RSVGKANEQL AAVVAETQKN GTISVVLGGD
    110 120 130 140 150
    HSMAIGSISG HARVHPDLCV IWVDAHTDIN TPLTTSSGNL HGQPVAFLLK
    160 170 180 190 200
    ELKGKFPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYII KTLGIKYFSM
    210 220 230 240 250
    TEVDKLGIGK VMEETFSYLL GRKKRPIHLS FDVDGLDPVF TPATGTPVVG
    260 270 280 290 300
    GLSYREGLYI TEEIYKTGLL SGLDIMEVNP TLGKTPEEVT RTVNTAVALT
    310 320
    LSCFGTKREG NHKPETDYLK PPK
    Length:323
    Mass (Da):34,973
    Last modified:April 1, 1990 - v2
    Checksum:i5A92CB0931F9A053
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti298A → P in AAA40761 (PubMed:3571256).Curated1
    Sequence conflicti298A → P in AAA40760 (PubMed:3571256).Curated1

    Sequence databases

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

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi247899. 2 interactors.
    IntActiP07824. 1 interactor.
    MINTiMINT-4567374.
    STRINGi10116.ENSRNOP00000017911.

    Chemistry databases

    BindingDBiP07824.
    ChEMBLiCHEMBL3232699.

    PTM databases

    iPTMnetiP07824.
    PhosphoSitePlusiP07824.

    Proteomic databases

    PaxDbiP07824.
    PRIDEiP07824.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi383.
    RGDi2150. Arg1.

    Phylogenomic databases

    eggNOGiKOG2965. Eukaryota.
    COG0010. LUCA.
    GeneTreeiENSGT00530000063082.
    HOGENOMiHOG000204319.
    HOVERGENiHBG003030.
    InParanoidiP07824.
    KOiK01476.
    OMAiEQECDVK.
    OrthoDBiEOG091G0A38.
    PhylomeDBiP07824.
    TreeFamiTF300034.

    Enzyme and pathway databases

    UniPathwayiUPA00158; UER00270.
    BRENDAi3.5.3.1. 5301.
    ReactomeiR-RNO-6798695. Neutrophil degranulation.
    R-RNO-70635. Urea cycle.
    SABIO-RKP07824.

    Miscellaneous databases

    EvolutionaryTraceiP07824.
    PROiP07824.

    Gene expression databases

    BgeeiENSRNOG00000013304.
    GenevisibleiP07824. RN.

    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 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: November 30, 2016
    This is version 165 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

    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.