ID   ANGI_PIG                Reviewed;         123 AA.
AC   P31346;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Angiogenin;
DE            EC=3.1.27.-;
DE   AltName: Full=Ribonuclease 5;
DE            Short=RNase 5;
GN   Name=ANG;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE, 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; S29834; A43825.
DR   AlphaFoldDB; P31346; -.
DR   SMR; P31346; -.
DR   IntAct; P31346; 2.
DR   STRING; 9823.ENSSSCP00000020122; -.
DR   PaxDb; P31346; -.
DR   PeptideAtlas; P31346; -.
DR   eggNOG; ENOG502S9Q1; Eukaryota.
DR   HOGENOM; CLU_117006_3_1_1; -.
DR   InParanoid; P31346; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; P31346; SS.
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   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   Reference proteome; Secreted; Stress response.
FT   CHAIN           1..123
FT                   /note="Angiogenin"
FT                   /id="PRO_0000057157"
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        113
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         40..44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..80
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..91
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..106
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   123 AA;  14058 MW;  17C327F0E6BC3BF4 CRC64;
     KDEDRYTHFL TQHYDAKPKG RDGRYCESIM KQRGLTRPCK EVNTFIHGTR NDIKAICNDK
     NGEPYNNFRR SKSPFQITTC KHKGGSNRPP CGYRATAGFR TIAVACENGL PVHFDESFII
     TSQ