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Protein

Arginase-1

Gene

Arg1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.Curated
Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion (By similarity). In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival. Plays a role in the immune response of alternatively activated or M2 macrophages in processes such as wound healing and tissue regeneration, immune defense against multicellular pathogens and parasites, and immune suppression and allergic inflammation; the regulatory outcome seems to be organ specific. In tumor-infiltrating dendritic cells (DCs) and myeloid-derived suppressor cells (MDSCs) plays a role in suppression of T cell-mediated antitumor immunity.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inactivated by diethyl pyrocarbonate (DEPC).

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.4 mM for arginine2 Publications

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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, Arginase (Arg2), Arginase-1 (Arg1), Arginase-2, mitochondrial (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
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>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
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei183SubstrateCombined sources1
    Metal bindingi232Manganese 1Combined sources6 Publications1
    Metal bindingi232Manganese 2Combined sources6 Publications1
    Metal bindingi234Manganese 2Combined sources6 Publications1
    Binding sitei246SubstrateBy similarity1
    Binding sitei277SubstrateBy similarity1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase
    Biological processAdaptive immunity, Arginine metabolism, Immunity, Innate immunity, Urea cycle
    LigandManganese, Metal-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.5.3.1 5301

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-RNO-6798695 Neutrophil degranulation
    R-RNO-70635 Urea cycle

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P07824

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00158;UER00270

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Arginase-1 (EC:3.5.3.12 Publications)
    Alternative name(s):
    Liver-type arginase
    Type I arginase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:Arg1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

    Organism-specific databases

    Rat genome database

    More...
    RGDi
    2150 Arg1

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3232699

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001736971 – 323Arginase-1Add BLAST323

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P07824

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P07824

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P07824

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P07824

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P07824

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Detected in liver (at protein level).1 Publication

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    By arginine or homoarginine.

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSRNOG00000013304 Expressed in 9 organ(s), highest expression level in liver

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P07824 RN

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotrimer (PubMed:15315440, PubMed:16266687). Interacts with CMTM6 (By similarity).By similarity2 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    247899, 2 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P07824, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    10116.ENSRNOP00000017911

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P07824

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1323
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P07824

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P07824

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P07824

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni126 – 130Substrate bindingCombined sources5
    Regioni137 – 139Substrate bindingCombined sources3

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the arginase family.PROSITE-ProRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2965 Eukaryota
    COG0010 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000153994

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000204319

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG003030

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P07824

    KEGG Orthology (KO)

    More...
    KOi
    K01476

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    NCLPKDQ

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G0A38

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P07824

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF300034

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR014033 Arginase
    IPR006035 Ureohydrolase
    IPR023696 Ureohydrolase_dom_sf
    IPR020855 Ureohydrolase_Mn_BS

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00491 Arginase, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF036979 Arginase, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00116 ARGINASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52768 SSF52768, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01229 rocF_arginase, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01053 ARGINASE_1, 1 hit
    PS51409 ARGINASE_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5A92CB0931F9A053
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti298A → P in AAA40761 (PubMed:3571256).Curated1
    Sequence conflicti298A → P in AAA40760 (PubMed:3571256).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A26702

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_058830.2, NM_017134.3

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Rn.9857

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSRNOT00000017911; ENSRNOP00000017911; ENSRNOG00000013304

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    29221

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    rno:29221

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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
    STRINGi10116.ENSRNOP00000017911

    Chemistry databases

    BindingDBiP07824
    ChEMBLiCHEMBL3232699

    PTM databases

    CarbonylDBiP07824
    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

    Comparative Toxicogenomics Database

    More...
    CTDi
    383
    RGDi2150 Arg1

    Phylogenomic databases

    eggNOGiKOG2965 Eukaryota
    COG0010 LUCA
    GeneTreeiENSGT00940000153994
    HOGENOMiHOG000204319
    HOVERGENiHBG003030
    InParanoidiP07824
    KOiK01476
    OMAiNCLPKDQ
    OrthoDBiEOG091G0A38
    PhylomeDBiP07824
    TreeFamiTF300034

    Enzyme and pathway databases

    UniPathwayi
    UPA00158;UER00270

    BRENDAi3.5.3.1 5301
    ReactomeiR-RNO-6798695 Neutrophil degranulation
    R-RNO-70635 Urea cycle
    SABIO-RKiP07824

    Miscellaneous databases

    EvolutionaryTraceiP07824

    Protein Ontology

    More...
    PROi
    PR:P07824

    Gene expression databases

    BgeeiENSRNOG00000013304 Expressed in 9 organ(s), highest expression level in liver
    GenevisibleiP07824 RN

    Family and domain databases

    InterProiView protein in InterPro
    IPR014033 Arginase
    IPR006035 Ureohydrolase
    IPR023696 Ureohydrolase_dom_sf
    IPR020855 Ureohydrolase_Mn_BS
    PfamiView protein in Pfam
    PF00491 Arginase, 1 hit
    PIRSFiPIRSF036979 Arginase, 1 hit
    PRINTSiPR00116 ARGINASE
    SUPFAMiSSF52768 SSF52768, 1 hit
    TIGRFAMsiTIGR01229 rocF_arginase, 1 hit
    PROSITEiView protein in PROSITE
    PS01053 ARGINASE_1, 1 hit
    PS51409 ARGINASE_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiARGI1_RAT
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07824
    Secondary accession number(s): Q5BK93
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: April 1, 1990
    Last modified: December 5, 2018
    This is version 178 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    UniProt is an ELIXIR core data resource
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