ANGI_MOUSE
ID ANGI_MOUSE Reviewed; 145 AA.
AC P21570;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Angiogenin;
DE EC=3.1.27.-;
DE AltName: Full=Angiogenin-1;
DE AltName: Full=Ribonuclease 5;
DE Short=RNase 5;
DE Flags: Precursor;
GN Name=Ang; Synonyms=Ang1, Rnase5, Rnase5a;
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].
RX PubMed=2222458; DOI=10.1016/0006-291x(90)90781-h;
RA Bond M.D., Vallee B.L.;
RT "Isolation and sequencing of mouse angiogenin DNA.";
RL Biochem. Biophys. Res. Commun. 171:988-995(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Serum;
RX PubMed=8448182; DOI=10.1016/0167-4838(93)90145-h;
RA Bond M.D., Strydom D.J., Vallee B.L.;
RT "Characterization and sequencing of rabbit, pig and mouse angiogenins:
RT discernment of functionally important residues and regions.";
RL Biochim. Biophys. Acta 1162:177-186(1993).
RN [4]
RP FUNCTION.
RX PubMed=19114040; DOI=10.1016/j.febslet.2008.12.043;
RA Fu H., Feng J., Liu Q., Sun F., Tie Y., Zhu J., Xing R., Sun Z., Zheng X.;
RT "Stress induces tRNA cleavage by angiogenin in mammalian cells.";
RL FEBS Lett. 583:437-442(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 25-145, AND DISULFIDE BONDS.
RX PubMed=16301790; DOI=10.1107/s0907444905029616;
RA Holloway D.E., Chavali G.B., Hares M.C., Subramanian V., Acharya K.R.;
RT "Structure of murine angiogenin: features of the substrate- and cell-
RT binding regions and prospects for inhibitor-binding studies.";
RL Acta Crystallogr. D 61:1568-1578(2005).
CC -!- FUNCTION: Binds to actin on the surface of endothelial cells; once
CC bound, angiogenin is endocytosed and translocated to the nucleus.
CC Stimulates ribosomal RNA synthesis including that containing the
CC initiation site sequences of 45S rRNA. Cleaves tRNA within anticodon
CC loops to produce tRNA-derived stress-induced fragments (tiRNAs) which
CC inhibit protein synthesis and triggers the assembly of stress granules
CC (SGs). Angiogenin induces vascularization of normal and malignant
CC tissues. Angiogenic activity is regulated by interaction with RNH1 in
CC vivo (By similarity). {ECO:0000250, ECO:0000269|PubMed:19114040}.
CC -!- SUBUNIT: Homodimer. Interacts with and forms a tight 1:1 complex with
CC RNH1. Dimerization of two such complexes may occur (By similarity).
CC {ECO:0000250|UniProtKB:P03950}.
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; U22516; AAA91366.1; -; Genomic_DNA.
DR EMBL; BC055355; AAH55355.1; -; mRNA.
DR CCDS; CCDS27034.1; -.
DR PIR; A35932; A35932.
DR RefSeq; NP_001155203.1; NM_001161731.2.
DR RefSeq; NP_031473.1; NM_007447.3.
DR PDB; 2BWK; X-ray; 1.50 A; A=25-145.
DR PDB; 2BWL; X-ray; 1.62 A; A=25-145.
DR PDBsum; 2BWK; -.
DR PDBsum; 2BWL; -.
DR AlphaFoldDB; P21570; -.
DR SMR; P21570; -.
DR STRING; 10090.ENSMUSP00000067434; -.
DR PhosphoSitePlus; P21570; -.
DR CPTAC; non-CPTAC-3960; -.
DR PaxDb; P21570; -.
DR PeptideAtlas; P21570; -.
DR PRIDE; P21570; -.
DR ProteomicsDB; 296290; -.
DR DNASU; 11727; -.
DR Ensembl; ENSMUST00000069011; ENSMUSP00000067434; ENSMUSG00000072115.
DR Ensembl; ENSMUST00000171688; ENSMUSP00000132084; ENSMUSG00000072115.
DR GeneID; 11727; -.
DR KEGG; mmu:11727; -.
DR UCSC; uc007tml.2; mouse.
DR CTD; 283; -.
DR MGI; MGI:88022; Ang.
DR VEuPathDB; HostDB:ENSMUSG00000072115; -.
DR eggNOG; ENOG502S9Q1; Eukaryota.
DR GeneTree; ENSGT00940000162981; -.
DR HOGENOM; CLU_117006_3_1_1; -.
DR InParanoid; P21570; -.
DR OMA; FIHGNKG; -.
DR PhylomeDB; P21570; -.
DR TreeFam; TF333393; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR BioGRID-ORCS; 11727; 4 hits in 73 CRISPR screens.
DR EvolutionaryTrace; P21570; -.
DR PRO; PR:P21570; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P21570; protein.
DR Bgee; ENSMUSG00000072115; Expressed in left lobe of liver and 172 other tissues.
DR ExpressionAtlas; P21570; baseline and differential.
DR Genevisible; P21570; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0032311; C:angiogenin-PRI complex; ISS:UniProtKB.
DR GO; GO:0005604; C:basement membrane; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004540; F:ribonuclease activity; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IC:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0032431; P:activation of phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0019732; P:antifungal humoral response; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0007417; P:central nervous system development; NAS:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
DR GO; GO:0009725; P:response to hormone; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0001878; P:response to yeast; IDA:UniProtKB.
DR GO; GO:0009303; P:rRNA transcription; ISS:UniProtKB.
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; Direct protein sequencing; Disulfide bond; DNA-binding;
KW Endonuclease; Hydrolase; Nuclease; Nucleus; Protein synthesis inhibitor;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW Stress response.
FT SIGNAL 1..24
FT CHAIN 25..145
FT /note="Angiogenin"
FT /id="PRO_0000030857"
FT MOTIF 55..59
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 37
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 137
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P03950"
FT DISULFID 50..104
FT /evidence="ECO:0000269|PubMed:16301790"
FT DISULFID 63..115
FT /evidence="ECO:0000269|PubMed:16301790"
FT DISULFID 81..130
FT /evidence="ECO:0000269|PubMed:16301790"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:2BWK"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:2BWK"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:2BWK"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2BWK"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:2BWK"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2BWK"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2BWK"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2BWK"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2BWK"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:2BWK"
FT STRAND 99..108
FT /evidence="ECO:0007829|PDB:2BWK"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2BWK"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:2BWK"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:2BWK"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:2BWK"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2BWK"
SQ SEQUENCE 145 AA; 16228 MW; 06944260BB764938 CRC64;
MAISPGPLFL IFVLGLVVIP PTLAQDDSRY TKFLTQHHDA KPKGRDDRYC ERMMKRRSLT
SPCKDVNTFI HGNKSNIKAI CGANGSPYRE NLRMSKSPFQ VTTCKHTGGS PRPPCQYRAS
AGFRHVVIAC ENGLPVHFDE SFFSL
