Angiogenin precursor - Mus musculus (Mouse)

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P21570 (ANGI_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 125. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	145 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular matrix › basement membrane By similarity. Nucleus › nucleolus 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 process	Angiogenesis Differentiation Stress response
Cellular component	Basement membrane Extracellular matrix Nucleus Secreted
Domain	Signal
Ligand	DNA-binding
Molecular function	Developmental protein Endonuclease Hydrolase Nuclease Protein synthesis inhibitor
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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_component	angiogenin-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_function	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 heparin binding Inferred from sequence or structural similarity. Source: UniProtKB pancreatic ribonuclease activity Inferred from electronic annotation. Source: InterPro 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

Chain

25 – 145

121

Angiogenin

PRO_0000030857

Regions

Region

64 – 68

Substrate binding By similarity

Motif

55 – 59

Nucleolar localization signal By similarity

Sites

Active site

Proton acceptor By similarity

Active site

137

Proton donor By similarity

Amino acid modifications

Modified residue

Pyrrolidone carboxylic acid By similarity

Disulfide bond

Disulfide bond

Disulfide bond

Secondary structure

145

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P21570 [UniParc].

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

FASTA

145

16,228

        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' referencesShow '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.

IPI

IPI00125082.

PIR

A35932.

RefSeq

NP_001155203.1. NM_001161731.2.
NP_031473.1. NM_007447.3.

UniGene

Mm.202665.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BWK	X-ray	1.50	A	25-145	[»]
2BWL	X-ray	1.62	A	25-145	[»]

ProteinModelPortal

P21570.

SMR

P21570. Positions 28-143.

ModBase

Search...

Protein-protein interaction databases

STRING

10090.ENSMUSP00000067434.

PTM databases

PhosphoSite

P21570.

Proteomic databases

PaxDb

P21570.

PRIDE

P21570.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000069011; ENSMUSP00000067434; ENSMUSG00000072115.
ENSMUST00000171688; ENSMUSP00000132084; ENSMUSG00000072115.

GeneID

11727.

KEGG

mmu:11727.

Organism-specific databases

CTD

283.

MGI

MGI:88022. Ang.

Phylogenomic databases

eggNOG

NOG283332.

HOGENOM

HOG000276883.

HOVERGEN

HBG008396.

InParanoid

P21570.

K16631.

OMA

PCKYRAT.

OrthoDB

EOG4Z62Q1.

Enzyme and pathway databases

Reactome

REACT_89750. Hemostasis.

Gene expression databases

ArrayExpress

P21570.

Bgee

P21570.

Genevestigator

P21570.

GermOnline

ENSMUSG00000072115. Mus musculus.

Family and domain databases

Gene3D

3.10.130.10. 1 hit.

InterPro

IPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]

PANTHER

PTHR11437. PTHR11437. 1 hit.

Pfam

PF00074. RnaseA. 1 hit.
[Graphical view]

PRINTS

PR00794. RIBONUCLEASE.

ProDom

PD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00092. RNAse_Pc. 1 hit.
[Graphical view]

SUPFAM

SSF54076. RNaseA. 1 hit.

PROSITE

PS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ANG. mouse.

EvolutionaryTrace

P21570.

NextBio

279409.

SOURCE

Search...

Entry information

Entry name

ANGI_MOUSE

Accession

Primary (citable) accession number: P21570

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents