ANGI_SAGOE
ID ANGI_SAGOE Reviewed; 146 AA.
AC Q8WN62;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Angiogenin;
DE EC=3.1.27.-;
DE AltName: Full=Ribonuclease 5;
DE Short=RNase 5;
DE Flags: Precursor;
GN Name=ANG; Synonyms=RNASE5;
OS Saguinus oedipus (Cotton-top tamarin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Saguinus.
OX NCBI_TaxID=9490;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11919285; DOI=10.1093/oxfordjournals.molbev.a004099;
RA Zhang J., Rosenberg H.F.;
RT "Diversifying selection of the tumor-growth promoter angiogenin in primate
RT evolution.";
RL Mol. Biol. Evol. 19:438-445(2002).
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 (By similarity). {ECO:0000250}.
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}.
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; AF441668; AAL61650.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WN62; -.
DR SMR; Q8WN62; -.
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; 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; 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:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004540; F:ribonuclease activity; ISS:UniProtKB.
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:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS: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:0050714; P:positive regulation of protein secretion; ISS: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 3: Inferred from homology;
KW Angiogenesis; Cytoplasmic vesicle; Developmental protein; Differentiation;
KW Disulfide bond; DNA-binding; Endonuclease; Hydrolase; Nuclease; Nucleus;
KW Protein synthesis inhibitor; Pyrrolidone carboxylic acid; Secreted; Signal;
KW Stress response.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..146
FT /note="Angiogenin"
FT /id="PRO_0000030852"
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 138
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..105
FT /evidence="ECO:0000250"
FT DISULFID 63..116
FT /evidence="ECO:0000250"
FT DISULFID 81..131
FT /evidence="ECO:0000250"
SQ SEQUENCE 146 AA; 16435 MW; F62FCE4219C4E3E9 CRC64;
MVMGLHLLFL VFILGLGLTP PTLAQNDLRY NRFLEEHYDP KTKNGNDRYC DKMMRLRNMI
SPCKAINTFI HGKKESIKAI CGTENGVPYN GNKRKSKSAF QVTICKHRGG SPRPPCQYRA
TAGSRNVVVA CENGLPVHLD ESIFRP
