RNS_BOVIN
ID RNS_BOVIN Reviewed; 150 AA.
AC P00669;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Seminal ribonuclease;
DE Short=S-RNase;
DE Short=Seminal RNase;
DE EC=4.6.1.18 {ECO:0000269|PubMed:4664228};
DE AltName: Full=Ribonuclease BS-1;
DE Flags: Precursor;
GN Name=SRN;
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 [MRNA].
RX PubMed=2315023; DOI=10.1093/nar/18.4.1057;
RA Preuss K.D., Wagner S., Freudenstein J., Scheit K.H.;
RT "Cloning of cDNA encoding the complete precursor for bovine seminal
RT ribonuclease.";
RL Nucleic Acids Res. 18:1057-1057(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Sasso M.P., Lombardi M., Confalone E., Carsana A., Palmieri M., Furia A.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE OF 27-150.
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).
RN [4]
RP PROTEIN SEQUENCE OF 27-150.
RA Suzuki H., Greco L., Parente A., Farina B., la Montagna R., Leone E.;
RT "Primary structure of seminal ribonuclease (RNAase BS-1).";
RL Acta Vitaminol. Enzymol. 26:213-214(1972).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-150.
RX PubMed=3840434; DOI=10.1111/j.1432-1033.1985.tb09194.x;
RA Palmieri M., Carsana A., Furia A., Libonati M.;
RT "Sequence analysis of a cloned cDNA coding for bovine seminal
RT ribonuclease.";
RL Eur. J. Biochem. 152:275-277(1985).
RN [6]
RP SEQUENCE REVISION TO 43.
RX PubMed=6846794; DOI=10.1016/0003-2697(83)90366-4;
RA Krietsch W.K.G., Simm F.C., Hertenberger B., Kuntz G.W.K., Wachter E.;
RT "Isolation of bovine seminal ribonuclease by affinity chromatography.";
RL Anal. Biochem. 128:213-216(1983).
RN [7]
RP INTERCHAIN DISULFIDE BONDS.
RX PubMed=4761089; DOI=10.1016/0006-291x(73)91231-x;
RA di Donato A., D'Alessio G.;
RT "Interchain disulfide bridges in ribonuclease BS-1.";
RL Biochem. Biophys. Res. Commun. 55:919-928(1973).
RN [8]
RP INTRACHAIN DISULFIDE BONDS.
RX PubMed=534646; DOI=10.1016/0005-2795(79)90058-8;
RA di Donato A., D'Alessio G.;
RT "Intrachain disulfide bridges of bovine seminal ribonuclease.";
RL Biochim. Biophys. Acta 579:303-313(1979).
RN [9]
RP MULTIPLE FORMS.
RX PubMed=7317378; DOI=10.1021/bi00528a028;
RA di Donato A., D'Alessio G.;
RT "Heterogeneity of bovine seminal ribonuclease.";
RL Biochemistry 20:7232-7237(1981).
RN [10]
RP CATALYTIC ACTIVITY.
RX PubMed=4664228; DOI=10.1016/0014-5793(72)80642-2;
RA D'Alessio G., Parente A., Guida C., Leone E.;
RT "Dimeric structure of seminal ribonuclease.";
RL FEBS Lett. 27:285-288(1972).
RN [11]
RP REVIEW, AND DEAMIDATION AT ASN-93.
RX PubMed=2057997; DOI=10.1016/0968-0004(91)90042-t;
RA D'Alessio G., di Donato A., Parente A., Piccoli R.;
RT "Seminal RNase: a unique member of the ribonuclease superfamily.";
RL Trends Biochem. Sci. 16:104-106(1991).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=6673761; DOI=10.1002/bip.360220142;
RA Capasso S., Giordano F., Mattia C.A., Mazzarella L., Zagari A.;
RT "Refinement of the structure of bovine seminal ribonuclease.";
RL Biopolymers 22:327-332(1983).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=15299514; DOI=10.1107/s0907444993003403;
RA Mazzarella L., Capasso S., Demasi D., di Lorenzo G., Mattia C.A.,
RA Zagari A.;
RT "Bovine seminal ribonuclease: structure at 1.9-A resolution.";
RL Acta Crystallogr. D 49:389-402(1993).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
RX PubMed=7731986; DOI=10.1073/pnas.92.9.3799;
RA Mazzarella K., Vitagliano L., Zagari A.;
RT "Swapping structural determinants of ribonucleases: an energetic analysis
RT of the hinge peptide 16-22.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3799-3803(1995).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS).
RX PubMed=10082366; DOI=10.1002/pro.5560070804;
RA Vitagliano L., Adinolfi S., Riccio A., Sica F., Zagari A., Mazzarella L.;
RT "Binding of a substrate analog to a domain swapping protein: X-ray
RT structure of the complex of bovine seminal ribonuclease with
RT uridylyl(2',5')adenosine.";
RL Protein Sci. 7:1691-1699(1998).
CC -!- FUNCTION: This enzyme hydrolyzes both single- and double-stranded RNA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-
CC phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
CC Evidence={ECO:0000269|PubMed:4664228};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-
CC phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
CC Evidence={ECO:0000269|PubMed:4664228};
CC -!- ACTIVITY REGULATION: Allosteric regulation by both substrate and
CC reaction products.
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- INTERACTION:
CC P00669; P00669: SRN; NbExp=7; IntAct=EBI-8524799, EBI-8524799;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Seminal plasma. Can reach 3% of the protein content
CC of this fluid.
CC -!- MISCELLANEOUS: Progressive deamidation of Asn-93 transforms the
CC homodimer (beta- 2) into and heterodimer (alpha-beta) and finally a
CC doubly deamidated dimer (alpha-2). {ECO:0000269|PubMed:2057997}.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; X51337; CAA35716.1; -; mRNA.
DR EMBL; AJ000518; CAA04155.1; -; Genomic_DNA.
DR EMBL; S81747; AAB36140.1; -; Genomic_DNA.
DR EMBL; X03029; CAA26832.1; -; mRNA.
DR PIR; S08392; NRBOS.
DR RefSeq; NP_861526.1; NM_181810.1.
DR PDB; 11BA; X-ray; 2.06 A; A/B=27-150.
DR PDB; 11BG; X-ray; 1.90 A; A/B=27-150.
DR PDB; 1BSR; X-ray; 1.90 A; A/B=27-150.
DR PDB; 1N1X; X-ray; 1.45 A; A=27-150.
DR PDB; 1N3Z; X-ray; 1.65 A; A=27-150.
DR PDB; 1QWQ; NMR; -; A=27-150.
DR PDB; 1R3M; X-ray; 2.20 A; A/B=27-150.
DR PDB; 1R5C; X-ray; 2.10 A; A/B=27-150.
DR PDB; 1R5D; X-ray; 2.50 A; A/B=27-150.
DR PDB; 1TQ9; X-ray; 2.00 A; A/B=27-150.
DR PDB; 1Y92; X-ray; 2.20 A; A/B=27-150.
DR PDB; 1Y94; X-ray; 2.20 A; A/B=27-150.
DR PDB; 2LFJ; NMR; -; A=27-150.
DR PDB; 3BCM; X-ray; 2.25 A; A/B=27-150.
DR PDB; 3BCO; X-ray; 2.25 A; A/B=27-150.
DR PDB; 3BCP; X-ray; 2.57 A; A/B/C/D=27-150.
DR PDB; 3DJO; X-ray; 1.60 A; A/B=27-150.
DR PDB; 3DJP; X-ray; 1.60 A; A/B=27-150.
DR PDB; 3DJQ; X-ray; 1.53 A; A/B=27-150.
DR PDB; 3DJV; X-ray; 1.60 A; A/B=27-150.
DR PDB; 3DJX; X-ray; 1.69 A; A/B=27-150.
DR PDB; 4N4C; X-ray; 2.48 A; A/B=27-150.
DR PDBsum; 11BA; -.
DR PDBsum; 11BG; -.
DR PDBsum; 1BSR; -.
DR PDBsum; 1N1X; -.
DR PDBsum; 1N3Z; -.
DR PDBsum; 1QWQ; -.
DR PDBsum; 1R3M; -.
DR PDBsum; 1R5C; -.
DR PDBsum; 1R5D; -.
DR PDBsum; 1TQ9; -.
DR PDBsum; 1Y92; -.
DR PDBsum; 1Y94; -.
DR PDBsum; 2LFJ; -.
DR PDBsum; 3BCM; -.
DR PDBsum; 3BCO; -.
DR PDBsum; 3BCP; -.
DR PDBsum; 3DJO; -.
DR PDBsum; 3DJP; -.
DR PDBsum; 3DJQ; -.
DR PDBsum; 3DJV; -.
DR PDBsum; 3DJX; -.
DR PDBsum; 4N4C; -.
DR AlphaFoldDB; P00669; -.
DR BMRB; P00669; -.
DR SMR; P00669; -.
DR MINT; P00669; -.
DR STRING; 9913.ENSBTAP00000036091; -.
DR BindingDB; P00669; -.
DR ChEMBL; CHEMBL1075179; -.
DR PaxDb; P00669; -.
DR PeptideAtlas; P00669; -.
DR Ensembl; ENSBTAT00000036229; ENSBTAP00000036091; ENSBTAG00000025663.
DR GeneID; 280930; -.
DR KEGG; bta:280930; -.
DR CTD; 6035; -.
DR VEuPathDB; HostDB:ENSBTAG00000025663; -.
DR eggNOG; ENOG502SQ4K; Eukaryota.
DR GeneTree; ENSGT00940000160869; -.
DR HOGENOM; CLU_117006_0_0_1; -.
DR InParanoid; P00669; -.
DR OMA; HITECRL; -.
DR OrthoDB; 1549558at2759; -.
DR TreeFam; TF333393; -.
DR BRENDA; 4.6.1.18; 908.
DR SABIO-RK; P00669; -.
DR EvolutionaryTrace; P00669; -.
DR PRO; PR:P00669; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000025663; Expressed in mammary gland fat and 6 other tissues.
DR ExpressionAtlas; P00669; baseline.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004522; F:ribonuclease A activity; IEA:UniProtKB-EC.
DR GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:UniProtKB.
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 3D-structure; Allosteric enzyme; Direct protein sequencing; Disulfide bond;
KW Endonuclease; Hydrolase; Lyase; Nuclease; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 27..150
FT /note="Seminal ribonuclease"
FT /id="PRO_0000030910"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT ACT_SITE 145
FT /note="Proton donor"
FT BINDING 33
FT /ligand="substrate"
FT BINDING 36
FT /ligand="substrate"
FT BINDING 67..71
FT /ligand="substrate"
FT BINDING 92
FT /ligand="substrate"
FT BINDING 111
FT /ligand="substrate"
FT MOD_RES 93
FT /note="Deamidated asparagine; by deterioration"
FT /evidence="ECO:0000269|PubMed:2057997"
FT DISULFID 52..110
FT DISULFID 57
FT /note="Interchain"
FT DISULFID 58
FT /note="Interchain"
FT DISULFID 66..121
FT DISULFID 84..136
FT DISULFID 91..98
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:1N1X"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3DJQ"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:1N1X"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:1N1X"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1N1X"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1N1X"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:1N1X"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1N1X"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1N1X"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4N4C"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1N1X"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:1N1X"
FT STRAND 123..137
FT /evidence="ECO:0007829|PDB:1N1X"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:1N1X"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:1N1X"
SQ SEQUENCE 150 AA; 16377 MW; F7A05C930FB83A83 CRC64;
MALKSLVVLP LLVLVLLLVR VQPSLGKESA AAKFERQHMD SGNSPSSSSN YCNLMMCCRK
MTQGKCKPVN TFVHESLADV KAVCSQKKVT CKNGQTNCYQ SKSTMRITDC RETGSSKYPN
CAYKTTQVEK HIIVACGGKP SVPVHFDASV
