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Seminal ribonuclease (S-RNase) (Seminal RNase) (EC 3.1.27.5) (Ribonuclease BS-1)

 RNS_BOVIN               Reviewed;         150 AA.
P00669;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 2.
12-SEP-2018, entry version 159.
RecName: Full=Seminal ribonuclease;
Short=S-RNase;
Short=Seminal RNase;
EC=3.1.27.5;
AltName: Full=Ribonuclease BS-1;
Flags: Precursor;
Name=SRN;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2315023; DOI=10.1093/nar/18.4.1057;
Preuss K.D., Wagner S., Freudenstein J., Scheit K.H.;
"Cloning of cDNA encoding the complete precursor for bovine seminal
ribonuclease.";
Nucleic Acids Res. 18:1057-1057(1990).
[2]
NUCLEOTIDE SEQUENCE.
Sasso M.P., Lombardi M., Confalone E., Carsana A., Palmieri M.,
Furia A.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE OF 27-150.
PubMed=8587129; DOI=10.1007/BF00173164;
Confalone E., Beintema J.J., Sasso M.P., Carsana A., Palmieri M.,
Vento M.T., Furia A.;
"Molecular evolution of genes encoding ribonucleases in ruminant
species.";
J. Mol. Evol. 41:850-858(1995).
[4]
PROTEIN SEQUENCE OF 27-150.
Suzuki H., Greco L., Parente A., Farina B., la Montagna R., Leone E.;
"Primary structure of seminal ribonuclease (RNAase BS-1).";
Acta Vitaminol. Enzymol. 26:213-214(1972).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 73-150.
PubMed=3840434; DOI=10.1111/j.1432-1033.1985.tb09194.x;
Palmieri M., Carsana A., Furia A., Libonati M.;
"Sequence analysis of a cloned cDNA coding for bovine seminal
ribonuclease.";
Eur. J. Biochem. 152:275-277(1985).
[6]
SEQUENCE REVISION TO 43.
PubMed=6846794; DOI=10.1016/0003-2697(83)90366-4;
Krietsch W.K.G., Simm F.C., Hertenberger B., Kuntz G.W.K., Wachter E.;
"Isolation of bovine seminal ribonuclease by affinity
chromatography.";
Anal. Biochem. 128:213-216(1983).
[7]
INTERCHAIN DISULFIDE BONDS.
PubMed=4761089; DOI=10.1016/0006-291X(73)91231-X;
di Donato A., D'Alessio G.;
"Interchain disulfide bridges in ribonuclease BS-1.";
Biochem. Biophys. Res. Commun. 55:919-928(1973).
[8]
INTRACHAIN DISULFIDE BONDS.
PubMed=534646; DOI=10.1016/0005-2795(79)90058-8;
di Donato A., D'Alessio G.;
"Intrachain disulfide bridges of bovine seminal ribonuclease.";
Biochim. Biophys. Acta 579:303-313(1979).
[9]
MULTIPLE FORMS.
PubMed=7317378; DOI=10.1021/bi00528a028;
di Donato A., D'Alessio G.;
"Heterogeneity of bovine seminal ribonuclease.";
Biochemistry 20:7232-7237(1981).
[10]
ENZYME ACTIVITY.
PubMed=4664228; DOI=10.1016/0014-5793(72)80642-2;
D'Alessio G., Parente A., Guida C., Leone E.;
"Dimeric structure of seminal ribonuclease.";
FEBS Lett. 27:285-288(1972).
[11]
REVIEW, AND DEAMIDATION AT ASN-93.
PubMed=2057997; DOI=10.1016/0968-0004(91)90042-T;
D'Alessio G., di Donato A., Parente A., Piccoli R.;
"Seminal RNase: a unique member of the ribonuclease superfamily.";
Trends Biochem. Sci. 16:104-106(1991).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=6673761; DOI=10.1002/bip.360220142;
Capasso S., Giordano F., Mattia C.A., Mazzarella L., Zagari A.;
"Refinement of the structure of bovine seminal ribonuclease.";
Biopolymers 22:327-332(1983).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=15299514; DOI=10.1107/S0907444993003403;
Mazzarella L., Capasso S., Demasi D., di Lorenzo G., Mattia C.A.,
Zagari A.;
"Bovine seminal ribonuclease: structure at 1.9-A resolution.";
Acta Crystallogr. D 49:389-402(1993).
[14]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
PubMed=7731986; DOI=10.1073/pnas.92.9.3799;
Mazzarella K., Vitagliano L., Zagari A.;
"Swapping structural determinants of ribonucleases: an energetic
analysis of the hinge peptide 16-22.";
Proc. Natl. Acad. Sci. U.S.A. 92:3799-3803(1995).
[15]
X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS).
PubMed=10082366; DOI=10.1002/pro.5560070804;
Vitagliano L., Adinolfi S., Riccio A., Sica F., Zagari A.,
Mazzarella L.;
"Binding of a substrate analog to a domain swapping protein: X-ray
structure of the complex of bovine seminal ribonuclease with
uridylyl(2',5')adenosine.";
Protein Sci. 7:1691-1699(1998).
-!- FUNCTION: This enzyme hydrolyzes both single- and double-stranded
RNA.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to nucleoside 3'-
phosphates and 3'-phosphooligonucleotides ending in Cp or Up with
2',3'-cyclic phosphate intermediates.
{ECO:0000269|PubMed:4664228}.
-!- ACTIVITY REGULATION: Allosteric regulation by both substrate and
reaction products.
-!- SUBUNIT: Homodimer; disulfide-linked.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-8524799, EBI-8524799;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Seminal plasma. Can reach 3% of the protein
content of this fluid.
-!- MISCELLANEOUS: Progressive deamidation of Asn-93 transforms the
homodimer (beta- 2) into and heterodimer (alpha-beta) and finally
a doubly deamidated dimer (alpha-2). {ECO:0000269|PubMed:2057997}.
-!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X51337; CAA35716.1; -; mRNA.
EMBL; AJ000518; CAA04155.1; -; Genomic_DNA.
EMBL; S81747; AAB36140.1; -; Genomic_DNA.
EMBL; X03029; CAA26832.1; -; mRNA.
PIR; S08392; NRBOS.
RefSeq; NP_861526.1; NM_181810.1.
UniGene; Bt.22955; -.
PDB; 11BA; X-ray; 2.06 A; A/B=27-150.
PDB; 11BG; X-ray; 1.90 A; A/B=27-150.
PDB; 1BSR; X-ray; 1.90 A; A/B=27-150.
PDB; 1N1X; X-ray; 1.45 A; A=27-150.
PDB; 1N3Z; X-ray; 1.65 A; A=27-150.
PDB; 1QWQ; NMR; -; A=27-150.
PDB; 1R3M; X-ray; 2.20 A; A/B=27-150.
PDB; 1R5C; X-ray; 2.10 A; A/B=27-150.
PDB; 1R5D; X-ray; 2.50 A; A/B=27-150.
PDB; 1TQ9; X-ray; 2.00 A; A/B=27-150.
PDB; 1Y92; X-ray; 2.20 A; A/B=27-150.
PDB; 1Y94; X-ray; 2.20 A; A/B=27-150.
PDB; 2LFJ; NMR; -; A=27-150.
PDB; 3BCM; X-ray; 2.25 A; A/B=27-150.
PDB; 3BCO; X-ray; 2.25 A; A/B=27-150.
PDB; 3BCP; X-ray; 2.57 A; A/B/C/D=27-150.
PDB; 3DJO; X-ray; 1.60 A; A/B=27-150.
PDB; 3DJP; X-ray; 1.60 A; A/B=27-150.
PDB; 3DJQ; X-ray; 1.53 A; A/B=27-150.
PDB; 3DJV; X-ray; 1.60 A; A/B=27-150.
PDB; 3DJX; X-ray; 1.69 A; A/B=27-150.
PDB; 4N4C; X-ray; 2.48 A; A/B=27-150.
PDBsum; 11BA; -.
PDBsum; 11BG; -.
PDBsum; 1BSR; -.
PDBsum; 1N1X; -.
PDBsum; 1N3Z; -.
PDBsum; 1QWQ; -.
PDBsum; 1R3M; -.
PDBsum; 1R5C; -.
PDBsum; 1R5D; -.
PDBsum; 1TQ9; -.
PDBsum; 1Y92; -.
PDBsum; 1Y94; -.
PDBsum; 2LFJ; -.
PDBsum; 3BCM; -.
PDBsum; 3BCO; -.
PDBsum; 3BCP; -.
PDBsum; 3DJO; -.
PDBsum; 3DJP; -.
PDBsum; 3DJQ; -.
PDBsum; 3DJV; -.
PDBsum; 3DJX; -.
PDBsum; 4N4C; -.
ProteinModelPortal; P00669; -.
SMR; P00669; -.
MINT; P00669; -.
STRING; 9913.ENSBTAP00000036091; -.
BindingDB; P00669; -.
ChEMBL; CHEMBL1075179; -.
PaxDb; P00669; -.
PeptideAtlas; P00669; -.
PRIDE; P00669; -.
Ensembl; ENSBTAT00000036229; ENSBTAP00000036091; ENSBTAG00000025663.
GeneID; 280930; -.
KEGG; bta:280930; -.
CTD; 6035; -.
eggNOG; ENOG410IYEN; Eukaryota.
eggNOG; ENOG41113F1; LUCA.
GeneTree; ENSGT00900000140967; -.
HOGENOM; HOG000276883; -.
HOVERGEN; HBG008396; -.
InParanoid; P00669; -.
KO; K01168; -.
OMA; HIIVACH; -.
OrthoDB; EOG091G15X3; -.
TreeFam; TF333393; -.
BRENDA; 3.1.27.5; 908.
SABIO-RK; P00669; -.
EvolutionaryTrace; P00669; -.
PRO; PR:P00669; -.
Proteomes; UP000009136; Chromosome 10.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004519; F:endonuclease activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0004522; F:ribonuclease A activity; IEA:UniProtKB-EC.
GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:UniProtKB.
Gene3D; 3.10.130.10; -; 1.
InterPro; IPR001427; RNaseA.
InterPro; IPR036816; RNaseA-like_dom_sf.
InterPro; IPR023411; RNaseA_AS.
InterPro; IPR023412; RNaseA_domain.
PANTHER; PTHR11437; PTHR11437; 1.
Pfam; PF00074; RnaseA; 1.
PRINTS; PR00794; RIBONUCLEASE.
ProDom; PD000535; RNaseA; 1.
SMART; SM00092; RNAse_Pc; 1.
SUPFAM; SSF54076; SSF54076; 1.
PROSITE; PS00127; RNASE_PANCREATIC; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Complete proteome;
Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase;
Nuclease; Reference proteome; Secreted; Signal.
SIGNAL 1 26 {ECO:0000269|Ref.4}.
CHAIN 27 150 Seminal ribonuclease.
/FTId=PRO_0000030910.
REGION 67 71 Substrate binding.
ACT_SITE 38 38 Proton acceptor.
ACT_SITE 145 145 Proton donor.
BINDING 33 33 Substrate.
BINDING 36 36 Substrate.
BINDING 92 92 Substrate.
BINDING 111 111 Substrate.
MOD_RES 93 93 Deamidated asparagine; by deterioration.
{ECO:0000269|PubMed:2057997}.
DISULFID 52 110
DISULFID 57 57 Interchain.
DISULFID 58 58 Interchain.
DISULFID 66 121
DISULFID 84 136
DISULFID 91 98
HELIX 30 38 {ECO:0000244|PDB:1N1X}.
HELIX 48 50 {ECO:0000244|PDB:3DJQ}.
HELIX 51 58 {ECO:0000244|PDB:1N1X}.
TURN 59 62 {ECO:0000244|PDB:1N1X}.
STRAND 63 65 {ECO:0000244|PDB:1N1X}.
STRAND 68 73 {ECO:0000244|PDB:1N1X}.
HELIX 77 81 {ECO:0000244|PDB:1N1X}.
HELIX 82 85 {ECO:0000244|PDB:1N1X}.
STRAND 86 89 {ECO:0000244|PDB:1N1X}.
STRAND 92 94 {ECO:0000244|PDB:4N4C}.
STRAND 98 100 {ECO:0000244|PDB:1N1X}.
STRAND 105 112 {ECO:0000244|PDB:1N1X}.
STRAND 123 137 {ECO:0000244|PDB:1N1X}.
TURN 138 141 {ECO:0000244|PDB:1N1X}.
STRAND 142 150 {ECO:0000244|PDB:1N1X}.
SEQUENCE 150 AA; 16377 MW; F7A05C930FB83A83 CRC64;
MALKSLVVLP LLVLVLLLVR VQPSLGKESA AAKFERQHMD SGNSPSSSSN YCNLMMCCRK
MTQGKCKPVN TFVHESLADV KAVCSQKKVT CKNGQTNCYQ SKSTMRITDC RETGSSKYPN
CAYKTTQVEK HIIVACGGKP SVPVHFDASV


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