Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q64438 (ANG2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. 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-2
Alternative name(s):
Angiogenin-related protein
Gene names
Name:Ang2
Synonyms:Angrp
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

Has ribonuclease activity (in vitro). Seems to lack angiogenic activity. Ref.4

Enzyme regulation

Divalent metal ions, such as Cu2+ and Zn2+, may inhibit the ribonucleolytic activity. Ref.6

Subunit structure

Homodimer. Ref.6

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.

Tissue specificity

Expressed (at protein level) in macrophages. Ref.5

Sequence similarities

Belongs to the pancreatic ribonuclease family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 145121Angiogenin-2
PRO_0000030858

Regions

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

Sites

Active site371Proton acceptor Ref.6
Active site641 Ref.6
Active site1371Proton donor Ref.6
Metal binding651Zinc
Metal binding1061Zinc
Metal binding1371Zinc
Binding site321Substrate By similarity

Amino acid modifications

Disulfide bond50 ↔ 104 Ref.6
Disulfide bond63 ↔ 115 Ref.6
Disulfide bond81 ↔ 130 Ref.6

Experimental info

Sequence conflict981H → R in AAA91367. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q64438 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 0F7D97E14429C4B0

FASTA14516,593
        10         20         30         40         50         60 
MAMSPGPLFL VFLLGLVVIP PTLSQDDSRY TKFLTQHYDA KPKGRDDRYC ESMMVKRKLT 

        70         80         90        100        110        120 
SFCKDVNTFI HDTKNNIKAI CGKKGSPYGR NLRISKSHFQ VTTCTHKGRS PRPPCRYRAS 

       130        140 
KGFRYIIIGC ENGWPVHFDE SFISP 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U22519 Genomic DNA. Translation: AAA91367.1.
AC163664 Genomic DNA. No translation available.
CH466605 Genomic DNA. Translation: EDL20851.1.
RefSeqNP_031475.2. NM_007449.2.
UniGeneMm.377077.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZBVX-ray1.64A25-145[»]
ProteinModelPortalQ64438.
SMRQ64438. Positions 27-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000062902.

Proteomic databases

PRIDEQ64438.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000051274; ENSMUSP00000062902; ENSMUSG00000047894.
GeneID11731.
KEGGmmu:11731.
UCSCuc007tmu.1. mouse.

Organism-specific databases

CTD11731.
MGIMGI:104984. Ang2.

Phylogenomic databases

eggNOGNOG283332.
HOGENOMHOG000276883.
HOVERGENHBG008396.
InParanoidQ64438.
KOK16631.
OMAIGCENGW.
OrthoDBEOG7J1826.
TreeFamTF333393.

Gene expression databases

CleanExMM_ANG2.
GenevestigatorQ64438.

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

NextBio279423.
PROQ64438.
SOURCESearch...

Entry information

Entry nameANG2_MOUSE
AccessionPrimary (citable) accession number: Q64438
Secondary accession number(s): G5E8D0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 94 of the entry and version 2 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