ANG2_MOUSE
ID ANG2_MOUSE Reviewed; 145 AA.
AC Q64438; G5E8D0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Angiogenin-2;
DE AltName: Full=Angiogenin-related protein;
DE Flags: Precursor;
GN Name=Ang2; Synonyms=Angrp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129; TISSUE=Liver;
RX PubMed=8530072; DOI=10.1006/geno.1995.1232;
RA Brown W.E., Nobile V., Subramanian V., Shapiro R.;
RT "The mouse angiogenin gene family: structures of an angiogenin-related
RT protein gene and two pseudogenes.";
RL Genomics 29:200-206(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=8633065; DOI=10.1073/pnas.93.9.4331;
RA Nobile V., Vallee B.L., Shapiro R.;
RT "Characterization of mouse angiogenin-related protein: implications for
RT functional studies on angiogenin.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4331-4335(1996).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16045902; DOI=10.1016/j.cellimm.2005.06.001;
RA Hubbard N.E., Lim D., Mukutmoni M., Cai A., Erickson K.L.;
RT "Expression and regulation of murine macrophage angiopoietin-2.";
RL Cell. Immunol. 234:102-109(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 25-145, CATALYTIC ACTIVITY,
RP ACTIVE SITE, SUBUNIT, DISULFIDE BONDS, ACTIVITY REGULATION, AND
RP ZINC-BINDING SITES.
RX PubMed=23170778; DOI=10.1111/febs.12071;
RA Iyer S., Holloway D.E., Acharya K.R.;
RT "Crystal structures of murine angiogenin-2 and -3-probing
RT 'structure-- function' relationships amongst angiogenin homologues.";
RL FEBS J. 280:302-318(2013).
CC -!- FUNCTION: Has ribonuclease activity (in vitro). Seems to lack
CC angiogenic activity. {ECO:0000269|PubMed:8633065}.
CC -!- ACTIVITY REGULATION: Divalent metal ions, such as Cu2+ and Zn2+, may
CC inhibit the ribonucleolytic activity. {ECO:0000269|PubMed:23170778}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23170778}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen
CC {ECO:0000250|UniProtKB:Q3TMQ6}. Secreted
CC {ECO:0000250|UniProtKB:P10152}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P03950}. Note=Rapidly endocytosed by target
CC cells and translocated to the nucleus where it accumulates in the
CC nucleolus and binds to DNA (By similarity).
CC {ECO:0000250|UniProtKB:P03950}.
CC -!- TISSUE SPECIFICITY: Expressed (at protein level) in macrophages.
CC {ECO:0000269|PubMed:16045902}.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; U22519; AAA91367.1; -; Genomic_DNA.
DR EMBL; AC163664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466605; EDL20851.1; -; Genomic_DNA.
DR CCDS; CCDS27040.1; -.
DR RefSeq; NP_031475.2; NM_007449.2.
DR PDB; 3ZBV; X-ray; 1.64 A; A=25-145.
DR PDBsum; 3ZBV; -.
DR AlphaFoldDB; Q64438; -.
DR SMR; Q64438; -.
DR STRING; 10090.ENSMUSP00000062902; -.
DR iPTMnet; Q64438; -.
DR PhosphoSitePlus; Q64438; -.
DR CPTAC; non-CPTAC-3961; -.
DR PaxDb; Q64438; -.
DR PRIDE; Q64438; -.
DR DNASU; 11731; -.
DR Ensembl; ENSMUST00000051274; ENSMUSP00000062902; ENSMUSG00000047894.
DR Ensembl; ENSMUST00000228835; ENSMUSP00000154100; ENSMUSG00000047894.
DR GeneID; 11731; -.
DR KEGG; mmu:11731; -.
DR UCSC; uc007tmu.1; mouse.
DR CTD; 11731; -.
DR MGI; MGI:104984; Ang2.
DR VEuPathDB; HostDB:ENSMUSG00000047894; -.
DR eggNOG; ENOG502S9Q1; Eukaryota.
DR GeneTree; ENSGT00940000162981; -.
DR HOGENOM; CLU_117006_3_1_1; -.
DR InParanoid; Q64438; -.
DR OMA; ACENNLP; -.
DR OrthoDB; 1549558at2759; -.
DR PhylomeDB; Q64438; -.
DR TreeFam; TF333393; -.
DR BioGRID-ORCS; 11731; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q64438; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q64438; protein.
DR Bgee; ENSMUSG00000047894; Expressed in ileal epithelium and 17 other tissues.
DR ExpressionAtlas; Q64438; baseline and differential.
DR Genevisible; Q64438; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0004540; F:ribonuclease activity; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0032431; P:activation of phospholipase A2 activity; ISO:MGI.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISO:MGI.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; IDA:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR GO; GO:0019732; P:antifungal humoral response; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0003300; P:cardiac muscle hypertrophy; IDA:MGI.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IDA:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISO:MGI.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0070528; P:protein kinase C signaling; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0070293; P:renal absorption; IDA:MGI.
DR GO; GO:0009725; P:response to hormone; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0001878; P:response to yeast; ISO:MGI.
DR GO; GO:0009303; P:rRNA transcription; ISO:MGI.
DR Gene3D; 3.10.130.10; -; 1.
DR InterPro; IPR001427; RNaseA.
DR InterPro; IPR036816; RNaseA-like_dom_sf.
DR InterPro; IPR023411; RNaseA_AS.
DR InterPro; IPR023412; RNaseA_domain.
DR PANTHER; PTHR11437; PTHR11437; 1.
DR Pfam; PF00074; RnaseA; 1.
DR PRINTS; PR00794; RIBONUCLEASE.
DR SMART; SM00092; RNAse_Pc; 1.
DR SUPFAM; SSF54076; SSF54076; 1.
DR PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Disulfide bond; DNA-binding;
KW Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..145
FT /note="Angiogenin-2"
FT /id="PRO_0000030858"
FT MOTIF 55..59
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 37
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:23170778"
FT ACT_SITE 137
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:23170778"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT SITE 64
FT /note="Critical for catalytic activity"
FT /evidence="ECO:0000305|PubMed:23170778"
FT DISULFID 50..104
FT /evidence="ECO:0000269|PubMed:23170778"
FT DISULFID 63..115
FT /evidence="ECO:0000269|PubMed:23170778"
FT DISULFID 81..130
FT /evidence="ECO:0000269|PubMed:23170778"
FT CONFLICT 98
FT /note="H -> R (in Ref. 1; AAA91367)"
FT /evidence="ECO:0000305"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:3ZBV"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:3ZBV"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:3ZBV"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:3ZBV"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:3ZBV"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3ZBV"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3ZBV"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3ZBV"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3ZBV"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:3ZBV"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:3ZBV"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:3ZBV"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3ZBV"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:3ZBV"
SQ SEQUENCE 145 AA; 16593 MW; 0F7D97E14429C4B0 CRC64;
MAMSPGPLFL VFLLGLVVIP PTLSQDDSRY TKFLTQHYDA KPKGRDDRYC ESMMVKRKLT
SFCKDVNTFI HDTKNNIKAI CGKKGSPYGR NLRISKSHFQ VTTCTHKGRS PRPPCRYRAS
KGFRYIIIGC ENGWPVHFDE SFISP
