ID   RNBR_AXIPR              Reviewed;         151 AA.
AC   P87350;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Brain ribonuclease;
DE            Short=BRB;
DE            EC=3.1.27.-;
GN   Name=BRN;
OS   Axis porcinus (Hog deer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Cervinae; Axis.
OX   NCBI_TaxID=57737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9611269; DOI=10.1016/s0378-1119(98)00177-2;
RA   Breukelman H.J., van der Munnik N., Kleineidam R.G., Furia A.,
RA   Beintema J.J.;
RT   "Secretory ribonuclease genes and pseudogenes in true ruminants.";
RL   Gene 212:259-268(1998).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; Y11670; CAA72368.1; -; Genomic_DNA.
DR   AlphaFoldDB; P87350; -.
DR   SMR; P87350; -.
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   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   3: Inferred from homology;
KW   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Nuclease; Secreted.
FT   CHAIN           1..151
FT                   /note="Brain ribonuclease"
FT                   /id="PRO_0000057165"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        12
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        119
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         7
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        129
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        133
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..95
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..72
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   151 AA;  16819 MW;  E95F3757FFC5B233 CRC64;
     KESAAAKFRR QHMDAGSSSS GNSNYCNQMM KRRRMTHGRC KPVNTFVHES LDSVKAVCSQ
     KNITCKNGQP NCYQSNSTMN ITDCRETGSS KYPNCAYKTS QKQKYITVAC EGNPYVPVHF
     DGSVFLPATP LPSLPAPHKH RLLWLEGNNS S