ID   ANG2_MOUSE              Reviewed;         145 AA.
AC   Q64438; G5E8D0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Angiogenin-2;
DE   AltName: Full=Angiogenin-related protein;
DE   Flags: Precursor;
GN   Name=Ang2; Synonyms=Angrp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129; TISSUE=Liver;
RX   PubMed=8530072; DOI=10.1006/geno.1995.1232;
RA   Brown W.E., Nobile V., Subramanian V., Shapiro R.;
RT   "The mouse angiogenin gene family: structures of an angiogenin-related
RT   protein gene and two pseudogenes.";
RL   Genomics 29:200-206(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=8633065; DOI=10.1073/pnas.93.9.4331;
RA   Nobile V., Vallee B.L., Shapiro R.;
RT   "Characterization of mouse angiogenin-related protein: implications for
RT   functional studies on angiogenin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:4331-4335(1996).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=16045902; DOI=10.1016/j.cellimm.2005.06.001;
RA   Hubbard N.E., Lim D., Mukutmoni M., Cai A., Erickson K.L.;
RT   "Expression and regulation of murine macrophage angiopoietin-2.";
RL   Cell. Immunol. 234:102-109(2005).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 25-145, CATALYTIC ACTIVITY,
RP   ACTIVE SITE, SUBUNIT, DISULFIDE BONDS, ACTIVITY REGULATION, AND
RP   ZINC-BINDING SITES.
RX   PubMed=23170778; DOI=10.1111/febs.12071;
RA   Iyer S., Holloway D.E., Acharya K.R.;
RT   "Crystal structures of murine angiogenin-2 and -3-probing
RT   'structure-- function' relationships amongst angiogenin homologues.";
RL   FEBS J. 280:302-318(2013).
CC   -!- FUNCTION: Has ribonuclease activity (in vitro). Seems to lack
CC       angiogenic activity. {ECO:0000269|PubMed:8633065}.
CC   -!- ACTIVITY REGULATION: Divalent metal ions, such as Cu2+ and Zn2+, may
CC       inhibit the ribonucleolytic activity. {ECO:0000269|PubMed:23170778}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23170778}.
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   -!- TISSUE SPECIFICITY: Expressed (at protein level) in macrophages.
CC       {ECO:0000269|PubMed:16045902}.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; U22519; AAA91367.1; -; Genomic_DNA.
DR   EMBL; AC163664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466605; EDL20851.1; -; Genomic_DNA.
DR   CCDS; CCDS27040.1; -.
DR   RefSeq; NP_031475.2; NM_007449.2.
DR   PDB; 3ZBV; X-ray; 1.64 A; A=25-145.
DR   PDBsum; 3ZBV; -.
DR   AlphaFoldDB; Q64438; -.
DR   SMR; Q64438; -.
DR   STRING; 10090.ENSMUSP00000154100; -.
DR   iPTMnet; Q64438; -.
DR   PhosphoSitePlus; Q64438; -.
DR   CPTAC; non-CPTAC-3961; -.
DR   PaxDb; 10090-ENSMUSP00000062902; -.
DR   DNASU; 11731; -.
DR   Ensembl; ENSMUST00000051274.2; ENSMUSP00000062902.2; ENSMUSG00000047894.3.
DR   Ensembl; ENSMUST00000228835.2; ENSMUSP00000154100.2; ENSMUSG00000047894.3.
DR   GeneID; 11731; -.
DR   KEGG; mmu:11731; -.
DR   UCSC; uc007tmu.1; mouse.
DR   AGR; MGI:104984; -.
DR   CTD; 11731; -.
DR   MGI; MGI:104984; Ang2.
DR   VEuPathDB; HostDB:ENSMUSG00000047894; -.
DR   eggNOG; ENOG502S9Q1; Eukaryota.
DR   GeneTree; ENSGT00940000162981; -.
DR   HOGENOM; CLU_117006_3_1_1; -.
DR   InParanoid; Q64438; -.
DR   OMA; VHYAKHI; -.
DR   OrthoDB; 4612546at2759; -.
DR   PhylomeDB; Q64438; -.
DR   TreeFam; TF333393; -.
DR   BioGRID-ORCS; 11731; 0 hits in 76 CRISPR screens.
DR   PRO; PR:Q64438; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q64438; Protein.
DR   Bgee; ENSMUSG00000047894; Expressed in ileal epithelium and 17 other cell types or tissues.
DR   ExpressionAtlas; Q64438; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR   GO; GO:0005604; C:basement membrane; ISO:MGI.
DR   GO; GO:0005694; C:chromosome; ISO:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0003779; F:actin binding; ISO:MGI.
DR   GO; GO:0005507; F:copper ion binding; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0042277; F:peptide binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0004540; F:RNA nuclease activity; IDA:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR   GO; GO:0038166; P:angiotensin-activated signaling pathway; IDA:MGI.
DR   GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR   GO; GO:0019732; P:antifungal humoral response; ISO:MGI.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR   GO; GO:0003300; P:cardiac muscle hypertrophy; IDA:MGI.
DR   GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IDA:MGI.
DR   GO; GO:0016477; P:cell migration; ISO:MGI.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IDA:MGI.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR   GO; GO:0006651; P:diacylglycerol biosynthetic process; ISO:MGI.
DR   GO; GO:0010467; P:gene expression; IDA:MGI.
DR   GO; GO:0045087; P:innate immune response; ISO:MGI.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR   GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
DR   GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR   GO; GO:0070528; P:protein kinase C signaling; IDA:MGI.
DR   GO; GO:0070293; P:renal absorption; IDA:MGI.
DR   GO; GO:0009725; P:response to hormone; ISO:MGI.
DR   GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR   GO; GO:0001878; P:response to yeast; ISO:MGI.
DR   GO; GO:0009303; P:rRNA transcription; ISO:MGI.
DR   CDD; cd06265; RNase_A_canonical; 1.
DR   Gene3D; 3.10.130.10; Ribonuclease A-like domain; 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:SF60; ANGIOGENIN; 1.
DR   PANTHER; PTHR11437; RIBONUCLEASE; 1.
DR   Pfam; PF00074; RnaseA; 1.
DR   PRINTS; PR00794; RIBONUCLEASE.
DR   SMART; SM00092; RNAse_Pc; 1.
DR   SUPFAM; SSF54076; RNase A-like; 1.
DR   PROSITE; PS00127; RNASE_PANCREATIC; 1.
DR   Genevisible; Q64438; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasmic vesicle; Disulfide bond; DNA-binding;
KW   Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..145
FT                   /note="Angiogenin-2"
FT                   /id="PRO_0000030858"
FT   MOTIF           55..59
FT                   /note="Nucleolar localization signal"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        37
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:23170778"
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:23170778"
FT   BINDING         32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   SITE            64
FT                   /note="Critical for catalytic activity"
FT                   /evidence="ECO:0000305|PubMed:23170778"
FT   DISULFID        50..104
FT                   /evidence="ECO:0000269|PubMed:23170778"
FT   DISULFID        63..115
FT                   /evidence="ECO:0000269|PubMed:23170778"
FT   DISULFID        81..130
FT                   /evidence="ECO:0000269|PubMed:23170778"
FT   CONFLICT        98
FT                   /note="H -> R (in Ref. 1; AAA91367)"
FT                   /evidence="ECO:0000305"
FT   HELIX           28..37
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   HELIX           47..56
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   TURN            60..63
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   STRAND          65..70
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   HELIX           74..78
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   TURN            82..84
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   STRAND          92..97
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   STRAND          99..106
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   STRAND          117..124
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   STRAND          127..131
FT                   /evidence="ECO:0007829|PDB:3ZBV"
FT   STRAND          134..138
FT                   /evidence="ECO:0007829|PDB:3ZBV"
SQ   SEQUENCE   145 AA;  16593 MW;  0F7D97E14429C4B0 CRC64;
     MAMSPGPLFL VFLLGLVVIP PTLSQDDSRY TKFLTQHYDA KPKGRDDRYC ESMMVKRKLT
     SFCKDVNTFI HDTKNNIKAI CGKKGSPYGR NLRISKSHFQ VTTCTHKGRS PRPPCRYRAS
     KGFRYIIIGC ENGWPVHFDE SFISP
//