ID   ANGI_HORSE              Reviewed;         146 AA.
AC   Q5VI84;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
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   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Quarter Horse;
RA   Chang S.-I., Nguyen H.G.;
RT   "Cloning, sequencing, and expression of horse angiogenin.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AY450362; AAS15049.1; -; mRNA.
DR   RefSeq; NP_001075368.1; NM_001081899.1.
DR   RefSeq; XP_005602650.1; XM_005602593.2.
DR   RefSeq; XP_014588930.1; XM_014733444.1.
DR   RefSeq; XP_014588931.1; XM_014733445.1.
DR   AlphaFoldDB; Q5VI84; -.
DR   SMR; Q5VI84; -.
DR   PRIDE; Q5VI84; -.
DR   GeneID; 100034041; -.
DR   KEGG; ecb:100034041; -.
DR   CTD; 283; -.
DR   InParanoid; Q5VI84; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
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:0045087; P:innate immune response; 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   2: Evidence at transcript level;
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..146
FT                   /note="Angiogenin"
FT                   /id="PRO_0000041863"
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;  16410 MW;  E26A6975602F90AF CRC64;
     MAMSLCPLLL VFVLGLGLTP PSLAQDDSRY RQFLTKHYDA NPRGRNDRYC ESMMVRRHLT
     TPCKDTNTFI HGSKSSIKAI CGNKNGNPYG ETLRISKTRF QVTTCKHAGG SPRPPCRYRA
     TPGFRSIVIA CENGLPVHFD ESFFRP