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P21570 (ANGI_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Angiogenin

EC=3.1.27.-
Alternative name(s):
Angiogenin-1
Ribonuclease 5
Short name=RNase 5
Gene names
Name:Ang
Synonyms:Ang1, Rnase5, Rnase5a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length145 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Subunit structure

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

Subcellular location

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.

Sequence similarities

Belongs to the pancreatic ribonuclease family.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
Stress response
   Cellular componentBasement membrane
Extracellular matrix
Nucleus
Secreted
   DomainSignal
   LigandDNA-binding
   Molecular functionDevelopmental protein
Endonuclease
Hydrolase
Nuclease
Protein synthesis inhibitor
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from electronic annotation. Source: GOC

actin filament polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

activation of phospholipase A2 activity

Inferred from sequence or structural similarity. Source: UniProtKB

activation of phospholipase C activity

Inferred from sequence or structural similarity. Source: UniProtKB

angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

central nervous system development

Non-traceable author statement PubMed 17468498. Source: UniProtKB

diacylglycerol biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of endothelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein secretion

Inferred from sequence or structural similarity. Source: UniProtKB

rRNA transcription

Inferred from sequence or structural similarity. Source: UniProtKB

response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentangiogenin-PRI complex

Inferred from sequence or structural similarity. Source: UniProtKB

basal lamina

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

growth cone

Inferred from direct assay PubMed 17468498. Source: UniProtKB

neuronal cell body

Inferred from direct assay PubMed 17468498. Source: UniProtKB

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred by curator Ref.3. Source: MGI

actin binding

Inferred from sequence or structural similarity. Source: UniProtKB

copper ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

endoribonuclease activity, producing 3'-phosphomonoesters

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from sequence or structural similarity. Source: UniProtKB

receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

ribonuclease activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 145121Angiogenin
PRO_0000030857

Regions

Region64 – 685Substrate binding By similarity
Motif55 – 595Nucleolar localization signal By similarity

Sites

Active site371Proton acceptor By similarity
Active site1371Proton donor By similarity

Amino acid modifications

Modified residue251Pyrrolidone carboxylic acid By similarity
Disulfide bond50 ↔ 104 Ref.5
Disulfide bond63 ↔ 115 Ref.5
Disulfide bond81 ↔ 130 Ref.5

Secondary structure

............................ 145
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21570 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 06944260BB764938

FASTA14516,228
        10         20         30         40         50         60 
MAISPGPLFL IFVLGLVVIP PTLAQDDSRY TKFLTQHHDA KPKGRDDRYC ERMMKRRSLT 

        70         80         90        100        110        120 
SPCKDVNTFI HGNKSNIKAI CGANGSPYRE NLRMSKSPFQ VTTCKHTGGS PRPPCQYRAS 

       130        140 
AGFRHVVIAC ENGLPVHFDE SFFSL 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U22516 Genomic DNA. Translation: AAA91366.1.
BC055355 mRNA. Translation: AAH55355.1.
PIRA35932.
RefSeqNP_001155203.1. NM_001161731.2.
NP_031473.1. NM_007447.3.
UniGeneMm.202665.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BWKX-ray1.50A25-145[»]
2BWLX-ray1.62A25-145[»]
ProteinModelPortalP21570.
SMRP21570. Positions 28-143.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000067434.

PTM databases

PhosphoSiteP21570.

Proteomic databases

PaxDbP21570.
PRIDEP21570.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000069011; ENSMUSP00000067434; ENSMUSG00000072115.
ENSMUST00000171688; ENSMUSP00000132084; ENSMUSG00000072115.
GeneID11727.
KEGGmmu:11727.
UCSCuc007tml.2. mouse.

Organism-specific databases

CTD283.
MGIMGI:88022. Ang.

Phylogenomic databases

eggNOGNOG283332.
HOGENOMHOG000276883.
HOVERGENHBG008396.
InParanoidP21570.
KOK16631.
OMAPCKYRAT.
OrthoDBEOG7J1826.
TreeFamTF333393.

Gene expression databases

ArrayExpressP21570.
BgeeP21570.
GenevestigatorP21570.

Family and domain databases

Gene3D3.10.130.10. 1 hit.
InterProIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERPTHR11437. PTHR11437. 1 hit.
PfamPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSPR00794. RIBONUCLEASE.
ProDomPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMSSF54076. SSF54076. 1 hit.
PROSITEPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANG. mouse.
EvolutionaryTraceP21570.
NextBio279409.
PROP21570.
SOURCESearch...

Entry information

Entry nameANGI_MOUSE
AccessionPrimary (citable) accession number: P21570
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: March 19, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot