ANGI_CHICK
ID ANGI_CHICK Reviewed; 139 AA.
AC P27043;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Angiogenin;
DE EC=3.1.27.-;
DE AltName: Full=Ribonuclease A;
DE Flags: Precursor;
GN Name=ANG;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=White leghorn; TISSUE=Bone marrow;
RX PubMed=1549365;
RA Nakano T., Graf T.;
RT "Identification of genes differentially expressed in two types of v-myb-
RT transformed avian myelomonocytic cells.";
RL Oncogene 7:527-534(1992).
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}.
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; X61192; CAA43494.1; -; Genomic_DNA.
DR EMBL; X61193; CAA43495.1; -; mRNA.
DR PIR; I50677; I50677.
DR RefSeq; NP_990590.1; NM_205259.2.
DR PDB; 4PER; X-ray; 1.92 A; B=25-137.
DR PDBsum; 4PER; -.
DR AlphaFoldDB; P27043; -.
DR SMR; P27043; -.
DR STRING; 9031.ENSGALP00000040224; -.
DR PaxDb; P27043; -.
DR Ensembl; ENSGALT00000041019; ENSGALP00000040224; ENSGALG00000003196.
DR Ensembl; ENSGALT00000087312; ENSGALP00000062296; ENSGALG00000003196.
DR GeneID; 396194; -.
DR KEGG; gga:396194; -.
DR CTD; 6039; -.
DR VEuPathDB; HostDB:geneid_396194; -.
DR eggNOG; ENOG502T1FH; Eukaryota.
DR GeneTree; ENSGT00940000166697; -.
DR HOGENOM; CLU_117006_3_1_1; -.
DR InParanoid; P27043; -.
DR OMA; VPNCRYR; -.
DR OrthoDB; 1549558at2759; -.
DR PhylomeDB; P27043; -.
DR TreeFam; TF333393; -.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR Reactome; R-GGA-6803157; Antimicrobial peptides.
DR PRO; PR:P27043; -.
DR Proteomes; UP000000539; Chromosome 6.
DR Bgee; ENSGALG00000003196; Expressed in spleen and 10 other tissues.
DR ExpressionAtlas; P27043; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004540; F:ribonuclease activity; IMP:AgBase.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
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:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
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; Disulfide bond; Endonuclease; Hydrolase; Nuclease;
KW Nucleus; Protein synthesis inhibitor; Reference proteome; Secreted; Signal;
KW Stress response.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..139
FT /note="Angiogenin"
FT /id="PRO_0000030855"
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 133
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 65..69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 49..102
FT /evidence="ECO:0000250"
FT DISULFID 64..111
FT /evidence="ECO:0000250"
FT DISULFID 82..126
FT /evidence="ECO:0000250"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:4PER"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:4PER"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4PER"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:4PER"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4PER"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:4PER"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4PER"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:4PER"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:4PER"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:4PER"
SQ SEQUENCE 139 AA; 15767 MW; F881E9F10D726F84 CRC64;
MAMSSLWWTA ILLLALTVSM CYGVPTYQDF LRTHVDFPKT SFPNIAAYCN VMMVRRGINV
HGRCKSLNTF VHTDPRNLNT LCINQPNRAL RTTQQQLPVT DCKLIRSHPT CSYTGNQFNH
RVRVGCWGGL PVHLDGTFP
