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Q64438

- ANG2_MOUSE

UniProt

Q64438 - ANG2_MOUSE

Protein

Angiogenin-2

Gene

Ang2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Has ribonuclease activity (in vitro). Seems to lack angiogenic activity.1 Publication

    Enzyme regulationi

    Divalent metal ions, such as Cu2+ and Zn2+, may inhibit the ribonucleolytic activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei32 – 321SubstrateBy similarity
    Active sitei37 – 371Proton acceptor1 Publication
    Active sitei64 – 6411 Publication
    Metal bindingi65 – 651Zinc
    Metal bindingi106 – 1061Zinc
    Active sitei137 – 1371Proton donor1 Publication
    Metal bindingi137 – 1371Zinc

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. endoribonuclease activity, producing 3'-phosphomonoesters Source: InterPro
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular response to glucose stimulus Source: MGI

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Angiogenin-2
    Alternative name(s):
    Angiogenin-related protein
    Gene namesi
    Name:Ang2
    Synonyms:Angrp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:104984. Ang2.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrixbasement membrane By similarity. Nucleusnucleolus By similarity
    Note: Rapidly endocytosed by target cells and translocated to the nucleus where it accumulates in the nucleolus and binds to DNA.By similarity

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB-SubCell
    2. nucleolus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Nucleus, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 145121Angiogenin-2PRO_0000030858Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi50 ↔ 1041 Publication
    Disulfide bondi63 ↔ 1151 Publication
    Disulfide bondi81 ↔ 1301 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiQ64438.

    Expressioni

    Tissue specificityi

    Expressed (at protein level) in macrophages.1 Publication

    Gene expression databases

    CleanExiMM_ANG2.
    GenevestigatoriQ64438.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000062902.

    Structurei

    Secondary structure

    1
    145
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi28 – 3710
    Helixi47 – 5610
    Turni60 – 634
    Beta strandi65 – 706
    Helixi74 – 785
    Helixi79 – 813
    Turni82 – 843
    Beta strandi85 – 873
    Beta strandi92 – 976
    Beta strandi99 – 1068
    Beta strandi111 – 1144
    Beta strandi117 – 1248
    Beta strandi127 – 1315
    Beta strandi134 – 1385

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZBVX-ray1.64A25-145[»]
    ProteinModelPortaliQ64438.
    SMRiQ64438. Positions 27-144.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni64 – 685Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi55 – 595Nucleolar localization signalBy similarity

    Sequence similaritiesi

    Belongs to the pancreatic ribonuclease family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG283332.
    HOGENOMiHOG000276883.
    HOVERGENiHBG008396.
    InParanoidiQ64438.
    KOiK16631.
    OMAiIGCENGW.
    OrthoDBiEOG7J1826.
    TreeFamiTF333393.

    Family and domain databases

    Gene3Di3.10.130.10. 1 hit.
    InterProiIPR001427. RNaseA.
    IPR023411. RNaseA_AS.
    IPR023412. RNaseA_domain.
    [Graphical view]
    PANTHERiPTHR11437. PTHR11437. 1 hit.
    PfamiPF00074. RnaseA. 1 hit.
    [Graphical view]
    PRINTSiPR00794. RIBONUCLEASE.
    ProDomiPD000535. RNaseA. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00092. RNAse_Pc. 1 hit.
    [Graphical view]
    SUPFAMiSSF54076. SSF54076. 1 hit.
    PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q64438-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMSPGPLFL VFLLGLVVIP PTLSQDDSRY TKFLTQHYDA KPKGRDDRYC    50
    ESMMVKRKLT SFCKDVNTFI HDTKNNIKAI CGKKGSPYGR NLRISKSHFQ 100
    VTTCTHKGRS PRPPCRYRAS KGFRYIIIGC ENGWPVHFDE SFISP 145
    Length:145
    Mass (Da):16,593
    Last modified:October 3, 2012 - v2
    Checksum:i0F7D97E14429C4B0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981H → R in AAA91367. (PubMed:8530072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22519 Genomic DNA. Translation: AAA91367.1.
    AC163664 Genomic DNA. No translation available.
    CH466605 Genomic DNA. Translation: EDL20851.1.
    CCDSiCCDS27040.1.
    RefSeqiNP_031475.2. NM_007449.2.
    UniGeneiMm.377077.

    Genome annotation databases

    EnsembliENSMUST00000051274; ENSMUSP00000062902; ENSMUSG00000047894.
    GeneIDi11731.
    KEGGimmu:11731.
    UCSCiuc007tmu.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22519 Genomic DNA. Translation: AAA91367.1 .
    AC163664 Genomic DNA. No translation available.
    CH466605 Genomic DNA. Translation: EDL20851.1 .
    CCDSi CCDS27040.1.
    RefSeqi NP_031475.2. NM_007449.2.
    UniGenei Mm.377077.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZBV X-ray 1.64 A 25-145 [» ]
    ProteinModelPortali Q64438.
    SMRi Q64438. Positions 27-144.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000062902.

    Proteomic databases

    PRIDEi Q64438.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000051274 ; ENSMUSP00000062902 ; ENSMUSG00000047894 .
    GeneIDi 11731.
    KEGGi mmu:11731.
    UCSCi uc007tmu.1. mouse.

    Organism-specific databases

    CTDi 11731.
    MGIi MGI:104984. Ang2.

    Phylogenomic databases

    eggNOGi NOG283332.
    HOGENOMi HOG000276883.
    HOVERGENi HBG008396.
    InParanoidi Q64438.
    KOi K16631.
    OMAi IGCENGW.
    OrthoDBi EOG7J1826.
    TreeFami TF333393.

    Miscellaneous databases

    NextBioi 279423.
    PROi Q64438.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_ANG2.
    Genevestigatori Q64438.

    Family and domain databases

    Gene3Di 3.10.130.10. 1 hit.
    InterProi IPR001427. RNaseA.
    IPR023411. RNaseA_AS.
    IPR023412. RNaseA_domain.
    [Graphical view ]
    PANTHERi PTHR11437. PTHR11437. 1 hit.
    Pfami PF00074. RnaseA. 1 hit.
    [Graphical view ]
    PRINTSi PR00794. RIBONUCLEASE.
    ProDomi PD000535. RNaseA. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00092. RNAse_Pc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54076. SSF54076. 1 hit.
    PROSITEi PS00127. RNASE_PANCREATIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The mouse angiogenin gene family: structures of an angiogenin-related protein gene and two pseudogenes."
      Brown W.E., Nobile V., Subramanian V., Shapiro R.
      Genomics 29:200-206(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129.
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Characterization of mouse angiogenin-related protein: implications for functional studies on angiogenin."
      Nobile V., Vallee B.L., Shapiro R.
      Proc. Natl. Acad. Sci. U.S.A. 93:4331-4335(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Expression and regulation of murine macrophage angiopoietin-2."
      Hubbard N.E., Lim D., Mukutmoni M., Cai A., Erickson K.L.
      Cell. Immunol. 234:102-109(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "Crystal structures of murine angiogenin-2 and -3-probing 'structure--function' relationships amongst angiogenin homologues."
      Iyer S., Holloway D.E., Acharya K.R.
      FEBS J. 280:302-318(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 25-145, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DISULFIDE BONDS, ENZYME REGULATION, ZINC-BINDING SITES.

    Entry informationi

    Entry nameiANG2_MOUSE
    AccessioniPrimary (citable) accession number: Q64438
    Secondary accession number(s): G5E8D0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 96 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    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