RNBR_CAPCA
ID RNBR_CAPCA Reviewed; 151 AA.
AC P79351;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Brain ribonuclease;
DE Short=BRB;
DE EC=3.1.27.-;
GN Name=BRN;
OS Capreolus capreolus (European roe deer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Odocoileinae; Capreolus.
OX NCBI_TaxID=9858;
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; Y11673; CAA72371.1; -; Genomic_DNA.
DR AlphaFoldDB; P79351; -.
DR SMR; P79351; -.
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_0000057166"
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; 16971 MW; 392D0E6302F006A6 CRC64;
KESAAAKFRR QHMDSGSSSS GNPNYCNQMM KRRRMTHGRC KPVNTFVHES LDNVKAVCSQ
KNITCKNGQP NCYQSNSTMN ITDCRQTGSS KYPNCAYKTS QKQKYITVAC EGDPYVPVHF
DASVFLPATP LPSLPRPHKH RLLWLEGNNS S