RNBR_BOVIN
ID RNBR_BOVIN Reviewed; 167 AA.
AC P39873; Q1RMP6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Brain ribonuclease;
DE Short=BRB;
DE EC=3.1.27.-;
DE Flags: Precursor;
GN Name=BRN;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1754384; DOI=10.1093/nar/19.23.6469;
RA Sasso M.P., Carsana A., Confalone E., Cosi C., Sorrentino S., Viola M.,
RA Palmieri M., Russo E., Furia A.;
RT "Molecular cloning of the gene encoding the bovine brain ribonuclease and
RT its expression in different regions of the brain.";
RL Nucleic Acids Res. 19:6469-6474(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 27-167, AND GLYCOSYLATION AT ASN-88; THR-155 AND
RP SER-159.
RC TISSUE=Brain;
RX PubMed=3243767; DOI=10.1093/oxfordjournals.jbchem.a122587;
RA Watanabe H., Katoh H., Ishii M., Komoda Y., Sanda A., Takizawa Y., Ohgi K.,
RA Irie M.;
RT "Primary structure of a ribonuclease from bovine brain.";
RL J. Biochem. 104:939-945(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-167.
RX PubMed=8587129; DOI=10.1007/bf00173164;
RA Confalone E., Beintema J.J., Sasso M.P., Carsana A., Palmieri M.,
RA Vento M.T., Furia A.;
RT "Molecular evolution of genes encoding ribonucleases in ruminant species.";
RL J. Mol. Evol. 41:850-858(1995).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; X59767; CAA42439.1; -; Genomic_DNA.
DR EMBL; BC114791; AAI14792.1; -; mRNA.
DR EMBL; S81744; AAB36138.1; -; Genomic_DNA.
DR PIR; S20066; S20066.
DR RefSeq; NP_776316.1; NM_173891.2.
DR AlphaFoldDB; P39873; -.
DR SMR; P39873; -.
DR STRING; 9913.ENSBTAP00000006510; -.
DR GlyConnect; 528; 19 N-Linked glycans (1 site).
DR iPTMnet; P39873; -.
DR PaxDb; P39873; -.
DR Ensembl; ENSBTAT00000006510; ENSBTAP00000006510; ENSBTAG00000004950.
DR GeneID; 280720; -.
DR KEGG; bta:280720; -.
DR CTD; 247925; -.
DR VEuPathDB; HostDB:ENSBTAG00000004950; -.
DR eggNOG; ENOG502SQ4K; Eukaryota.
DR GeneTree; ENSGT00940000160869; -.
DR HOGENOM; CLU_117006_0_0_1; -.
DR InParanoid; P39873; -.
DR OMA; SNSTYCN; -.
DR OrthoDB; 1549558at2759; -.
DR TreeFam; TF333393; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000004950; Expressed in omental fat pad and 106 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GO_Central.
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 Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
KW Hydrolase; Nuclease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:3243767"
FT CHAIN 27..167
FT /note="Brain ribonuclease"
FT /id="PRO_0000030909"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 145
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3243767"
FT /id="CAR_000005"
FT CARBOHYD 155
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3243767"
FT CARBOHYD 159
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:3243767"
FT DISULFID 52..110
FT /evidence="ECO:0000250"
FT DISULFID 66..121
FT /evidence="ECO:0000250"
FT DISULFID 84..136
FT /evidence="ECO:0000250"
FT DISULFID 91..98
FT /evidence="ECO:0000250"
FT CONFLICT 155
FT /note="T -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 18450 MW; 681CAAC3CC2FC459 CRC64;
MALKSLVLLS LLVLVLLLVQ VQPSLGKESA AAKFRRQHMD SGSSSSSNPN YCNQMMKRRR
MTHGRCKPVN TFVHESLDDV KAVCSQKNIT CKNGHPNCYQ SKSTMSITDC RETGSSKYPN
CAYKTSQKQK YITVACEGNP YVPVHFDGAV LLPATPVPSL PPPHRLL
