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Q64438

- ANG2_MOUSE

UniProt

Q64438 - ANG2_MOUSE

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Protein

Angiogenin-2

Gene
Ang2, Angrp
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 321Substrate By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed predictionAdd
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.

Family & Domainsi

Region

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

Motif

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981H → R in AAA91367. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 95 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

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