ANGI_PANTR
ID ANGI_PANTR Reviewed; 147 AA.
AC Q8WME8; Q95J16;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-147.
RC STRAIN=Isolate 504, and Isolate 505;
RX PubMed=11569499; DOI=10.1266/ggs.76.159;
RA Satta Y.;
RT "Comparison of DNA and protein polymorphisms between humans and
RT chimpanzees.";
RL Genes Genet. Syst. 76:159-168(2001).
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 -!- SEQUENCE CAUTION:
CC Sequence=BAB55868.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55869.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF441661; AAL61643.1; -; Genomic_DNA.
DR EMBL; AF441676; AAL65148.1; -; Genomic_DNA.
DR EMBL; AB062039; BAB55868.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB062040; BAB55869.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_001009159.1; NM_001009159.1.
DR RefSeq; XP_009425660.1; XM_009427385.2.
DR RefSeq; XP_009425661.1; XM_009427386.2.
DR RefSeq; XP_009425662.1; XM_009427387.2.
DR AlphaFoldDB; Q8WME8; -.
DR SMR; Q8WME8; -.
DR STRING; 9598.ENSPTRP00000054974; -.
DR PaxDb; Q8WME8; -.
DR Ensembl; ENSPTRT00000081505; ENSPTRP00000066875; ENSPTRG00000043768.
DR GeneID; 494026; -.
DR KEGG; ptr:494026; -.
DR CTD; 283; -.
DR VGNC; VGNC:10303; ANG.
DR eggNOG; ENOG502S9Q1; Eukaryota.
DR GeneTree; ENSGT00940000162981; -.
DR HOGENOM; CLU_117006_3_1_1; -.
DR InParanoid; Q8WME8; -.
DR OrthoDB; 1549558at2759; -.
DR TreeFam; TF333393; -.
DR Proteomes; UP000002277; Chromosome 14.
DR Bgee; ENSPTRG00000043768; Expressed in liver and 16 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
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; IEA:Ensembl.
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:0042277; F:peptide binding; IEA:Ensembl.
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:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; ISS: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:0016477; P:cell migration; IEA:Ensembl.
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; 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:0009725; P:response to hormone; IEA:Ensembl.
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;
KW Reference proteome; Secreted; Signal; Stress response.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..147
FT /note="Angiogenin"
FT /id="PRO_0000030846"
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 147 AA; 16572 MW; 60B5ED5FC32CD138 CRC64;
MVMGLGVLLL VFVLGLGLTP PTLAQDNSRY THFLTQHYDA KPQGRDHRYC ESIMRRRGLT
SPCKDINTFI HGNKRSIKAI CENKNGNPHR ENLRISKSSF QVTTCKLHGG SPWPPCQYRA
TAGFRNVVVA CENGLPVHLD QSIFRRP
