ANG1_BOVIN
ID ANG1_BOVIN Reviewed; 148 AA.
AC P10152; Q9GKP9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 4.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Angiogenin-1;
DE EC=3.1.27.-;
DE Flags: Precursor;
GN Name=ANG1; Synonyms=ANG;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RA Chang S.-I.;
RT "Cloning, sequencing, and expression of bovine angiogenin.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION, AND PROTEIN SEQUENCE OF 24-148.
RC TISSUE=Milk;
RX PubMed=3197838; DOI=10.1016/0014-5793(88)81027-5;
RA Maes P., Damart D., Rommens C., Montreuil J., Spik G., Tartar A.;
RT "The complete amino acid sequence of bovine milk angiogenin.";
RL FEBS Lett. 241:41-45(1988).
RN [3]
RP SUBCELLULAR LOCATION, AND PROTEIN SEQUENCE OF 24-148.
RC TISSUE=Plasma;
RX PubMed=2775757; DOI=10.1021/bi00440a057;
RA Bond M.D., Strydom D.J.;
RT "Amino acid sequence of bovine angiogenin.";
RL Biochemistry 28:6110-6113(1989).
RN [4]
RP SUBCELLULAR LOCATION, AND PROTEIN SEQUENCE OF 25-55.
RC TISSUE=Plasma;
RX PubMed=3064806; DOI=10.1021/bi00417a013;
RA Bond M.D., Vallee B.L.;
RT "Isolation of bovine angiogenin using a placental ribonuclease inhibitor
RT binding assay.";
RL Biochemistry 27:6282-6287(1988).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 24-148.
RX PubMed=7708754; DOI=10.1073/pnas.92.7.2949;
RA Acharya K.R., Shapiro R., Riordan J.F., Vallee B.L.;
RT "Crystal structure of bovine angiogenin at 1.5-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:2949-2953(1995).
RN [6]
RP STRUCTURE BY NMR OF 24-148.
RX PubMed=8688423; DOI=10.1021/bi960022r;
RA Lequin O., Albaret C., Bontems F., Spik G., Lallemand J.-Y.;
RT "Solution structure of bovine angiogenin by 1H nuclear magnetic resonance
RT spectroscopy.";
RL Biochemistry 35:8870-8880(1996).
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) (By similarity). Angiogenin induces vascularization of normal and
CC malignant tissues. Angiogenic activity is regulated by interaction with
CC RNH1 in vivo. Has very low ribonuclease activity. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with and forms a tight 1:1 complex with RNH1.
CC Dimerization of two such complexes may occur (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen
CC {ECO:0000250|UniProtKB:Q3TMQ6}. Secreted {ECO:0000269|PubMed:2775757,
CC ECO:0000269|PubMed:3064806, ECO:0000269|PubMed:3197838}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P03950}. Note=Rapidly endocytosed by
CC target cells and translocated to the nucleus where it accumulates in
CC the nucleolus and binds to DNA (By similarity).
CC {ECO:0000250|UniProtKB:P03950}.
CC -!- TISSUE SPECIFICITY: Serum and milk. {ECO:0000269|PubMed:2775757,
CC ECO:0000269|PubMed:3064806}.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF135124; AAG47631.1; -; Genomic_DNA.
DR PDB; 1AGI; X-ray; 1.50 A; A=24-148.
DR PDB; 1GIO; NMR; -; A=24-148.
DR PDBsum; 1AGI; -.
DR PDBsum; 1GIO; -.
DR AlphaFoldDB; P10152; -.
DR SMR; P10152; -.
DR STRING; 9913.ENSBTAP00000026126; -.
DR PaxDb; P10152; -.
DR PRIDE; P10152; -.
DR eggNOG; ENOG502S9Q1; Eukaryota.
DR InParanoid; P10152; -.
DR EvolutionaryTrace; P10152; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0032311; C:angiogenin-PRI complex; ISS:UniProtKB.
DR GO; GO:0005604; C:basement membrane; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA: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:0004540; F:ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IDA:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; IDA: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:0001525; P:angiogenesis; IDA:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0001541; P:ovarian follicle development; NAS:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; IDA:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS: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 Reference proteome; Secreted; Signal; Stress response.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:2775757,
FT ECO:0000269|PubMed:3197838"
FT CHAIN 24..148
FT /note="Angiogenin-1"
FT /id="PRO_0000030856"
FT MOTIF 55..59
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 37
FT /note="Proton acceptor"
FT ACT_SITE 138
FT /note="Proton donor"
FT BINDING 64..68
FT /ligand="substrate"
FT DISULFID 50..105
FT DISULFID 63..116
FT DISULFID 81..131
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:1AGI"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:1AGI"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:1AGI"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1AGI"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:1AGI"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1AGI"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1AGI"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1AGI"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1AGI"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1AGI"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:1AGI"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1AGI"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:1AGI"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1AGI"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1AGI"
SQ SEQUENCE 148 AA; 16970 MW; B7999124CBB523DD CRC64;
MVMVLSPLLL VFILGLGLTP VAPAQDDYRY IHFLTQHYDA KPKGRNDEYC FNMMKNRRLT
RPCKDRNTFI HGNKNDIKAI CEDRNGQPYR GDLRISKSEF QITICKHKGG SSRPPCRYGA
TEDSRVIVVG CENGLPVHFD ESFITPRH
