ANG3_MOUSE
ID ANG3_MOUSE Reviewed; 145 AA.
AC P97802;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Angiogenin-3;
DE EC=3.1.27.-;
DE AltName: Full=Angiogenin-related protein 2;
DE AltName: Full=EF-5;
DE Flags: Precursor;
GN Name=Ang3; Synonyms=Angl;
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 [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=9032278; DOI=10.1128/mcb.17.3.1503;
RA Fu X., Kamps M.P.;
RT "E2a-Pbx1 induces aberrant expression of tissue-specific and
RT developmentally regulated genes when expressed in NIH 3T3 fibroblasts.";
RL Mol. Cell. Biol. 17:1503-1512(1997).
RN [2]
RP FUNCTION.
RX PubMed=11437607; DOI=10.1006/prep.2001.1434;
RA Holloway D.E., Hares M.C., Shapiro R., Subramanian V., Acharya K.R.;
RT "High-level expression of three members of the murine angiogenin family in
RT Escherichia coli and purification of the recombinant proteins.";
RL Protein Expr. Purif. 22:307-317(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 25-145, CATALYTIC ACTIVITY, ACTIVE
RP SITE, SUBUNIT, DISULFIDE BONDS, ACTIVITY REGULATION, AND ZINC-BINDING
RP 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: May promote vascularization of normal and malignant tissues
CC (By similarity). Has low ribonuclease activity (in vitro).
CC {ECO:0000250, ECO:0000269|PubMed:11437607}.
CC -!- ACTIVITY REGULATION: Divalent metal ions, such as Cu2+ and Zn2+, may
CC inhibit the ribonucleolytic activity. {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 -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; U72672; AAC05794.1; -; mRNA.
DR RefSeq; NP_001116866.2; NM_001123394.2.
DR PDB; 3ZBW; X-ray; 1.80 A; A/B=25-145.
DR PDBsum; 3ZBW; -.
DR AlphaFoldDB; P97802; -.
DR SMR; P97802; -.
DR MINT; P97802; -.
DR STRING; 10090.ENSMUSP00000067008; -.
DR CPTAC; non-CPTAC-3367; -.
DR PeptideAtlas; P97802; -.
DR PRIDE; P97802; -.
DR DNASU; 11730; -.
DR GeneID; 11730; -.
DR KEGG; mmu:11730; -.
DR UCSC; uc011zjf.1; mouse.
DR CTD; 11730; -.
DR MGI; MGI:1201793; Ang3.
DR eggNOG; ENOG502S9Q1; Eukaryota.
DR InParanoid; P97802; -.
DR PhylomeDB; P97802; -.
DR BioGRID-ORCS; 11730; 1 hit in 17 CRISPR screens.
DR PRO; PR:P97802; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97802; protein.
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: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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISO: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:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
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:0050714; P:positive regulation of protein secretion; ISO: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; Angiogenesis; Cytoplasmic vesicle; Developmental protein;
KW Differentiation; Disulfide bond; DNA-binding; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Nucleus; Protein synthesis inhibitor;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..145
FT /note="Angiogenin-3"
FT /id="PRO_0000030859"
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 SITE 64
FT /note="Critical for catalytic activity"
FT /evidence="ECO:0000305|PubMed:23170778"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P03950"
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 HELIX 28..37
FT /evidence="ECO:0007829|PDB:3ZBW"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:3ZBW"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:3ZBW"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:3ZBW"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:3ZBW"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3ZBW"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3ZBW"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3ZBW"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:3ZBW"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3ZBW"
FT STRAND 99..109
FT /evidence="ECO:0007829|PDB:3ZBW"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:3ZBW"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:3ZBW"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3ZBW"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:3ZBW"
SQ SEQUENCE 145 AA; 16696 MW; DE9D3BC92F1D682C CRC64;
MVMSPGSLLL VFLLSLDVIP PTLAQDNYRY IKFLTQHYDA KPTGRDYRYC ESMMKKRKLT
SPCKEVNTFI HDTKNNIKAI CGENGRPYGV NFRISNSRFQ VTTCTHKGGS PRPPCQYNAF
KDFRYIVIAC EDGWPVHFDE SFISP
