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A2AS89

- SPEB_MOUSE

UniProt

A2AS89 - SPEB_MOUSE

Protein

Agmatinase, mitochondrial

Gene

Agmat

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (20 Feb 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Agmatine + H2O = putrescine + urea.

    Cofactori

    Manganese.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi168 – 1681Manganese 1PROSITE-ProRule annotation
    Metal bindingi193 – 1931Manganese 2PROSITE-ProRule annotation
    Metal bindingi284 – 2841Manganese 2PROSITE-ProRule annotation

    GO - Molecular functioni

    1. agmatinase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. putrescine biosynthetic process from arginine Source: UniProtKB-UniPathway
    2. spermidine biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Putrescine biosynthesis, Spermidine biosynthesis

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00534; UER00287.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Agmatinase, mitochondrial (EC:3.5.3.11)
    Alternative name(s):
    Agmatine ureohydrolase
    Short name:
    AUH
    Gene namesi
    Name:Agmat
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1923236. Agmat.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3636MitochondrionSequence AnalysisAdd
    BLAST
    Chaini37 – 358322Agmatinase, mitochondrialPRO_0000320072Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei199 – 1991N6-acetyllysine1 Publication
    Modified residuei223 – 2231N6-acetyllysine; alternate1 Publication
    Modified residuei223 – 2231N6-succinyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiA2AS89.
    PaxDbiA2AS89.
    PRIDEiA2AS89.

    PTM databases

    PhosphoSiteiA2AS89.

    Expressioni

    Tissue specificityi

    Detected only in liver.1 Publication

    Gene expression databases

    ArrayExpressiA2AS89.
    BgeeiA2AS89.
    CleanExiMM_AGMAT.
    GenevestigatoriA2AS89.

    Structurei

    3D structure databases

    ProteinModelPortaliA2AS89.
    SMRiA2AS89. Positions 61-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the arginase family. Agmatinase subfamily.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0010.
    GeneTreeiENSGT00530000063082.
    HOGENOMiHOG000204320.
    HOVERGENiHBG023165.
    InParanoidiA2AS89.
    KOiK01480.
    OMAiERETHGT.
    OrthoDBiEOG7M98GH.
    PhylomeDBiA2AS89.
    TreeFamiTF328612.

    Family and domain databases

    Gene3Di3.40.800.10. 1 hit.
    InterProiIPR005925. Agmatinase-rel.
    IPR006035. Ureohydrolase.
    IPR023696. Ureohydrolase_domain.
    [Graphical view]
    PANTHERiPTHR11358. PTHR11358. 1 hit.
    PfamiPF00491. Arginase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036979. Arginase. 1 hit.
    PRINTSiPR00116. ARGINASE.
    TIGRFAMsiTIGR01230. agmatinase. 1 hit.
    PROSITEiPS51409. ARGINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A2AS89-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRLLRSSWA RGLGSGVATW RPSAGLFRPG CPGIRQASGA SDTPHHQSPS    50
    SESPVQPVGV GVCSMMRLPL QSSPEGLDAA FIGVPLDTGT SNRPGARFGP 100
    CRIREESLML GAVNPSTGAL PFQSLRVADL GNVNVNLYNL QDSCLLIREA 150
    YQNVLAAGCI PLTLGGDQTI TYPILQAVAK EHGPVGLVHV GAHTNTTDKP 200
    REEKVYHRTP FRRSVDEGLL DSKRVVQIGI RGSSRTLDPY RYSRSQGFRV 250
    VLAEDCWMKS LVPLMAEVRQ QMGGKPLYIS FAIDALDPAY APGTGTPEIA 300
    GLTPSQALEI IRGCQGLNVV GCDLVEVSPP YDLSGNTALL AANLLFEMLC 350
    ALPKVTTV 358
    Length:358
    Mass (Da):38,255
    Last modified:February 20, 2007 - v1
    Checksum:iC98ED338165794B0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451L → R in AAI15694. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL928577 Genomic DNA. Translation: CAM23129.1.
    BC115693 mRNA. Translation: AAI15694.1.
    CCDSiCCDS38941.1.
    RefSeqiNP_001074877.1. NM_001081408.1.
    UniGeneiMm.30032.

    Genome annotation databases

    EnsembliENSMUST00000038161; ENSMUSP00000040853; ENSMUSG00000040706.
    GeneIDi75986.
    KEGGimmu:75986.
    UCSCiuc008vpe.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL928577 Genomic DNA. Translation: CAM23129.1 .
    BC115693 mRNA. Translation: AAI15694.1 .
    CCDSi CCDS38941.1.
    RefSeqi NP_001074877.1. NM_001081408.1.
    UniGenei Mm.30032.

    3D structure databases

    ProteinModelPortali A2AS89.
    SMRi A2AS89. Positions 61-355.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei A2AS89.

    Proteomic databases

    MaxQBi A2AS89.
    PaxDbi A2AS89.
    PRIDEi A2AS89.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000038161 ; ENSMUSP00000040853 ; ENSMUSG00000040706 .
    GeneIDi 75986.
    KEGGi mmu:75986.
    UCSCi uc008vpe.1. mouse.

    Organism-specific databases

    CTDi 79814.
    MGIi MGI:1923236. Agmat.

    Phylogenomic databases

    eggNOGi COG0010.
    GeneTreei ENSGT00530000063082.
    HOGENOMi HOG000204320.
    HOVERGENi HBG023165.
    InParanoidi A2AS89.
    KOi K01480.
    OMAi ERETHGT.
    OrthoDBi EOG7M98GH.
    PhylomeDBi A2AS89.
    TreeFami TF328612.

    Enzyme and pathway databases

    UniPathwayi UPA00534 ; UER00287 .

    Miscellaneous databases

    NextBioi 344385.
    PROi A2AS89.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi A2AS89.
    Bgeei A2AS89.
    CleanExi MM_AGMAT.
    Genevestigatori A2AS89.

    Family and domain databases

    Gene3Di 3.40.800.10. 1 hit.
    InterProi IPR005925. Agmatinase-rel.
    IPR006035. Ureohydrolase.
    IPR023696. Ureohydrolase_domain.
    [Graphical view ]
    PANTHERi PTHR11358. PTHR11358. 1 hit.
    Pfami PF00491. Arginase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036979. Arginase. 1 hit.
    PRINTSi PR00116. ARGINASE.
    TIGRFAMsi TIGR01230. agmatinase. 1 hit.
    PROSITEi PS51409. ARGINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "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].
    3. Cited for: TISSUE SPECIFICITY.
    4. "Vertebrate agmatinases: what role do they play in agmatine catabolism?"
      Morris S.M. Jr.
      Ann. N. Y. Acad. Sci. 1009:30-33(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: POTENTIAL LACK OF CATALYTIC ACTIVITY.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiSPEB_MOUSE
    AccessioniPrimary (citable) accession number: A2AS89
    Secondary accession number(s): Q14BN7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    May have little or no activity due to the lack of several residues essential for manganese binding and catalytic activity.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3