ID   ANG2_BOVIN              Reviewed;         123 AA.
AC   P80929;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Angiogenin-2;
DE            EC=3.1.27.-;
GN   Name=ANG2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, GLYCOSYLATION AT
RP   ASN-33, AND SUBCELLULAR LOCATION.
RC   TISSUE=Milk, and Serum;
RX   PubMed=9266695; DOI=10.1111/j.1432-1033.1997.00535.x;
RA   Strydom D.J., Bond M.D., Vallee B.L.;
RT   "An angiogenic protein from bovine serum and milk -- purification and
RT   primary structure of angiogenin-2.";
RL   Eur. J. Biochem. 247:535-544(1997).
CC   -!- FUNCTION: Binds tightly to placental ribonuclease inhibitor and has
CC       very low ribonuclease activity. Has potent angiogenic activity.
CC       Angiogenin induces vascularization of normal and malignant tissues.
CC       Abolishes protein synthesis by specifically hydrolyzing cellular tRNAs.
CC   -!- ACTIVITY REGULATION: Divalent metal ions, such as Cu2+ and Zn2+, may
CC       inhibit the ribonucleolytic activity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen
CC       {ECO:0000250|UniProtKB:Q3TMQ6}. Secreted {ECO:0000269|PubMed:9266695}.
CC       Nucleus, nucleolus {ECO:0000250|UniProtKB:P03950}. Note=Rapidly
CC       endocytosed by target cells and translocated to the nucleus where it
CC       accumulates in the nucleolus and binds to DNA (By similarity).
CC       {ECO:0000250|UniProtKB:P03950}.
CC   -!- TISSUE SPECIFICITY: Serum and milk. {ECO:0000269|PubMed:9266695}.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P80929; -.
DR   SMR; P80929; -.
DR   STRING; 9913.ENSBTAP00000049727; -.
DR   iPTMnet; P80929; -.
DR   PaxDb; P80929; -.
DR   PRIDE; P80929; -.
DR   eggNOG; ENOG502S9Q1; Eukaryota.
DR   HOGENOM; CLU_117006_3_1_1; -.
DR   InParanoid; P80929; -.
DR   Proteomes; UP000009136; Unplaced.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central.
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   Angiogenesis; Cytoplasmic vesicle; Developmental protein; Differentiation;
KW   Direct protein sequencing; Disulfide bond; DNA-binding; Endonuclease;
KW   Glycoprotein; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW   Protein synthesis inhibitor; Pyrrolidone carboxylic acid;
KW   Reference proteome; Secreted; Zinc.
FT   CHAIN           1..123
FT                   /note="Angiogenin-2"
FT                   /id="PRO_0000057159"
FT   MOTIF           30..34
FT                   /note="Nucleolar localization signal"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        12
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        113
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         39..43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:9266695"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:9266695"
FT   DISULFID        25..80
FT   DISULFID        38..91
FT   DISULFID        56..106
SQ   SEQUENCE   123 AA;  14522 MW;  B703B9839919FD2F CRC64;
     QNDAYRGFLR KHYDPSPTGH DDRYCNTMME RRNMTRPCKD TNTFIHGNSD DIRAVCDDRN
     GEPYRNGLRR SRSPFQVTTC RHRGGSPRPP CRYRAFRANR VIVIRCRDGF PIHLEENFIP
     PRP