ANGI_RABIT
ID ANGI_RABIT Reviewed; 125 AA.
AC P31347;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Angiogenin;
DE EC=3.1.27.-;
DE AltName: Full=Ribonuclease 5;
DE Short=RNase 5;
GN Name=ANG;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, AND FUNCTION.
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).
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 ECO:0000269|PubMed:8448182}.
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 PIR; S29833; B43825.
DR AlphaFoldDB; P31347; -.
DR SMR; P31347; -.
DR InParanoid; P31347; -.
DR Proteomes; UP000001811; 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; 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 1: Evidence at protein level;
KW Angiogenesis; Cytoplasmic vesicle; Developmental protein; Differentiation;
KW Direct protein sequencing; Disulfide bond; DNA-binding; Endonuclease;
KW Hydrolase; Nuclease; Nucleus; Protein synthesis inhibitor;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Stress response.
FT CHAIN 1..125
FT /note="Angiogenin"
FT /id="PRO_0000057158"
FT MOTIF 31..35
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 13
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 40..44
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8448182"
FT DISULFID 26..81
FT /evidence="ECO:0000250"
FT DISULFID 39..92
FT /evidence="ECO:0000250"
FT DISULFID 57..107
FT /evidence="ECO:0000250"
SQ SEQUENCE 125 AA; 14361 MW; 3A737E595D767B04 CRC64;
QDDSRYKHFL TQHYDAKPFG RNDRYCETMM KRRDLTSPCK DTNTFVHGNK GSIKDVCEDK
NGKPYGKNFR ISKSSFQVTT CKHVGGSPWP PCRYRATSGS RNIVIACENG LPVHFDESVF
QQKVH
