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P21570

- ANGI_MOUSE

UniProt

P21570 - ANGI_MOUSE

Protein

Angiogenin

Gene

Ang

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

    Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. Stimulates ribosomal RNA synthesis including that containing the initiation site sequences of 45S rRNA. Cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs). Angiogenin induces vascularization of normal and malignant tissues. Angiogenic activity is regulated by interaction with RNH1 in vivo By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei37 – 371Proton acceptorBy similarity
    Active sitei137 – 1371Proton donorBy similarity

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. copper ion binding Source: UniProtKB
    3. DNA binding Source: UniProtKB-KW
    4. endoribonuclease activity, producing 3'-phosphomonoesters Source: InterPro
    5. heparin binding Source: UniProtKB
    6. receptor binding Source: UniProtKB
    7. ribonuclease activity Source: UniProtKB
    8. RNA binding Source: MGI

    GO - Biological processi

    1. actin filament polymerization Source: UniProtKB
    2. activation of phospholipase A2 activity Source: UniProtKB
    3. activation of phospholipase C activity Source: UniProtKB
    4. angiogenesis Source: UniProtKB
    5. cell differentiation Source: UniProtKB-KW
    6. central nervous system development Source: UniProtKB
    7. diacylglycerol biosynthetic process Source: UniProtKB
    8. negative regulation of smooth muscle cell proliferation Source: UniProtKB
    9. negative regulation of translation Source: UniProtKB-KW
    10. positive regulation of endothelial cell proliferation Source: UniProtKB
    11. positive regulation of protein secretion Source: UniProtKB
    12. response to hypoxia Source: UniProtKB
    13. RNA phosphodiester bond hydrolysis Source: GOC
    14. rRNA transcription Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Endonuclease, Hydrolase, Nuclease, Protein synthesis inhibitor

    Keywords - Biological processi

    Angiogenesis, Differentiation, Stress response

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_211860. Tie2 Signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Angiogenin (EC:3.1.27.-)
    Alternative name(s):
    Angiogenin-1
    Ribonuclease 5
    Short name:
    RNase 5
    Gene namesi
    Name:Ang
    Synonyms:Ang1, Rnase5, Rnase5a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:88022. Ang.

    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. angiogenin-PRI complex Source: UniProtKB
    2. basal lamina Source: UniProtKB
    3. extracellular region Source: Reactome
    4. extracellular space Source: UniProtKB
    5. growth cone Source: UniProtKB
    6. neuronal cell body Source: UniProtKB
    7. nucleolus Source: UniProtKB
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Nucleus, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 145121AngiogeninPRO_0000030857Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251Pyrrolidone carboxylic acidBy similarity
    Disulfide bondi50 ↔ 1041 Publication
    Disulfide bondi63 ↔ 1151 Publication
    Disulfide bondi81 ↔ 1301 Publication

    Keywords - PTMi

    Disulfide bond, Pyrrolidone carboxylic acid

    Proteomic databases

    PaxDbiP21570.
    PRIDEiP21570.

    PTM databases

    PhosphoSiteiP21570.

    Expressioni

    Gene expression databases

    ArrayExpressiP21570.
    BgeeiP21570.
    GenevestigatoriP21570.

    Interactioni

    Subunit structurei

    Interacts with and forms a tight 1:1 complex with RNH1. Dimerization of two such complexes may occur By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000067434.

    Structurei

    Secondary structure

    1
    145
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi29 – 379
    Helixi47 – 5610
    Turni60 – 634
    Beta strandi65 – 706
    Helixi74 – 785
    Helixi79 – 813
    Turni82 – 843
    Beta strandi85 – 884
    Turni89 – 913
    Beta strandi92 – 976
    Beta strandi99 – 10810
    Beta strandi111 – 1144
    Beta strandi116 – 1249
    Beta strandi127 – 1315
    Beta strandi134 – 1385
    Helixi140 – 1423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BWKX-ray1.50A25-145[»]
    2BWLX-ray1.62A25-145[»]
    ProteinModelPortaliP21570.
    SMRiP21570. Positions 28-143.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21570.

    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.
    InParanoidiP21570.
    KOiK16631.
    OMAiPCKYRAT.
    OrthoDBiEOG7J1826.
    PhylomeDBiP21570.
    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.

    P21570-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAISPGPLFL IFVLGLVVIP PTLAQDDSRY TKFLTQHHDA KPKGRDDRYC    50
    ERMMKRRSLT SPCKDVNTFI HGNKSNIKAI CGANGSPYRE NLRMSKSPFQ 100
    VTTCKHTGGS PRPPCQYRAS AGFRHVVIAC ENGLPVHFDE SFFSL 145
    Length:145
    Mass (Da):16,228
    Last modified:May 1, 1991 - v1
    Checksum:i06944260BB764938
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22516 Genomic DNA. Translation: AAA91366.1.
    BC055355 mRNA. Translation: AAH55355.1.
    CCDSiCCDS27034.1.
    PIRiA35932.
    RefSeqiNP_001155203.1. NM_001161731.2.
    NP_031473.1. NM_007447.3.
    UniGeneiMm.202665.

    Genome annotation databases

    EnsembliENSMUST00000069011; ENSMUSP00000067434; ENSMUSG00000072115.
    ENSMUST00000171688; ENSMUSP00000132084; ENSMUSG00000072115.
    GeneIDi11727.
    KEGGimmu:11727.
    UCSCiuc007tml.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22516 Genomic DNA. Translation: AAA91366.1 .
    BC055355 mRNA. Translation: AAH55355.1 .
    CCDSi CCDS27034.1.
    PIRi A35932.
    RefSeqi NP_001155203.1. NM_001161731.2.
    NP_031473.1. NM_007447.3.
    UniGenei Mm.202665.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BWK X-ray 1.50 A 25-145 [» ]
    2BWL X-ray 1.62 A 25-145 [» ]
    ProteinModelPortali P21570.
    SMRi P21570. Positions 28-143.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000067434.

    PTM databases

    PhosphoSitei P21570.

    Proteomic databases

    PaxDbi P21570.
    PRIDEi P21570.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000069011 ; ENSMUSP00000067434 ; ENSMUSG00000072115 .
    ENSMUST00000171688 ; ENSMUSP00000132084 ; ENSMUSG00000072115 .
    GeneIDi 11727.
    KEGGi mmu:11727.
    UCSCi uc007tml.2. mouse.

    Organism-specific databases

    CTDi 283.
    MGIi MGI:88022. Ang.

    Phylogenomic databases

    eggNOGi NOG283332.
    HOGENOMi HOG000276883.
    HOVERGENi HBG008396.
    InParanoidi P21570.
    KOi K16631.
    OMAi PCKYRAT.
    OrthoDBi EOG7J1826.
    PhylomeDBi P21570.
    TreeFami TF333393.

    Enzyme and pathway databases

    Reactomei REACT_211860. Tie2 Signaling.

    Miscellaneous databases

    ChiTaRSi ANG. mouse.
    EvolutionaryTracei P21570.
    NextBioi 279409.
    PROi P21570.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21570.
    Bgeei P21570.
    Genevestigatori P21570.

    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. "Isolation and sequencing of mouse angiogenin DNA."
      Bond M.D., Vallee B.L.
      Biochem. Biophys. Res. Commun. 171:988-995(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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].
      Strain: FVB/N.
      Tissue: Liver.
    3. "Characterization and sequencing of rabbit, pig and mouse angiogenins: discernment of functionally important residues and regions."
      Bond M.D., Strydom D.J., Vallee B.L.
      Biochim. Biophys. Acta 1162:177-186(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Serum.
    4. "Stress induces tRNA cleavage by angiogenin in mammalian cells."
      Fu H., Feng J., Liu Q., Sun F., Tie Y., Zhu J., Xing R., Sun Z., Zheng X.
      FEBS Lett. 583:437-442(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Structure of murine angiogenin: features of the substrate- and cell-binding regions and prospects for inhibitor-binding studies."
      Holloway D.E., Chavali G.B., Hares M.C., Subramanian V., Acharya K.R.
      Acta Crystallogr. D 61:1568-1578(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 25-145, DISULFIDE BONDS.

    Entry informationi

    Entry nameiANGI_MOUSE
    AccessioniPrimary (citable) accession number: P21570
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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