Reviewed, UniProtKB/Swiss-Prot P00669 (RNS_BOVIN)

Names and origin

Protein names

Recommended name:
    Seminal ribonuclease
      Short name=Seminal RNase
      Short name=S-RNase
    EC=3.1.27.5
Alternative name(s):
    Ribonuclease BS-1

Gene names

Name:

SRN

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	150 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. Ref.10
Enzyme regulation	Allosteric regulation by both substrate and reaction products.
Subunit structure	Homodimer; disulfide-linked. Ref.7 Ref.8
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).
Sequence similarities	Belongs to the pancreatic ribonuclease family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond
Technical term	3D-structure Allosteric enzyme Direct protein sequencing
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro pancreatic ribonuclease activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.4

Chain

27 – 150

124

Seminal ribonuclease

PRO_0000030910

Regions

Region

67 – 71

5

Substrate binding

Sites

Active site

38

1

Proton acceptor

Active site

145

1

Proton donor

Binding site

33

1

Substrate

Binding site

36

1

Substrate

Binding site

92

1

Substrate

Binding site

111

1

Substrate

Amino acid modifications

Modified residue

93

1

Deamidated asparagine; by deterioration

Disulfide bond

52 ↔ 110

Ref.7 Ref.8

Disulfide bond

57

Interchain Ref.7 Ref.8

Disulfide bond

58

Interchain Ref.7 Ref.8

Disulfide bond

66 ↔ 121

Ref.7 Ref.8

Disulfide bond

84 ↔ 136

Ref.7 Ref.8

Disulfide bond

91 ↔ 98

Ref.7 Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

150

Helix Strand Turn

Details...

Helix

30 – 38

9

Helix

51 – 55

5

Beta strand

63 – 65

3

Beta strand

68 – 73

6

Helix

77 – 81

5

Helix

82 – 85

4

Beta strand

86 – 89

4

Beta strand

98 – 100

3

Beta strand

105 – 112

8

Beta strand

123 – 137

15

Turn

138 – 141

4

Beta strand

142 – 150

9

Sequences

	Sequence		Length	Mass (Da)
	P00669-1 [UniParc]. Last modified April 1, 1990. Version 2. Checksum: F7A05C930FB83A83	FASTA	150	16,377
	10 20 30 40 50 60 MALKSLVVLP LLVLVLLLVR VQPSLGKESA AAKFERQHMD SGNSPSSSSN YCNLMMCCRK 70 80 90 100 110 120 MTQGKCKPVN TFVHESLADV KAVCSQKKVT CKNGQTNCYQ SKSTMRITDC RETGSSKYPN 130 140 150 CAYKTTQVEK HIIVACGGKP SVPVHFDASV

References

[1]	"Cloning of cDNA encoding the complete precursor for bovine seminal ribonuclease." Preuss K.D., Wagner S., Freudenstein J., Scheit K.H. Nucleic Acids Res. 18:1057-1057(1990) [PubMed: 2315023] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Sasso M.P., Lombardi M., Confalone E., Carsana A., Palmieri M., Furia A. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Molecular evolution of genes encoding ribonucleases in ruminant species." Confalone E., Beintema J.J., Sasso M.P., Carsana A., Palmieri M., Vento M.T., Furia A. J. Mol. Evol. 41:850-858(1995) [PubMed: 8587129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 27-150.
[4]	"Primary structure of seminal ribonuclease (RNAase BS-1)." Suzuki H., Greco L., Parente A., Farina B., la Montagna R., Leone E. Acta Vitaminol. Enzymol. 26:213-214(1972) Cited for: PROTEIN SEQUENCE OF 27-150.
[5]	"Sequence analysis of a cloned cDNA coding for bovine seminal ribonuclease." Palmieri M., Carsana A., Furia A., Libonati M. Eur. J. Biochem. 152:275-277(1985) [PubMed: 3840434] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 73-150.
[6]	"Isolation of bovine seminal ribonuclease by affinity chromatography." Krietsch W.K.G., Simm F.C., Hertenberger B., Kuntz G.W.K., Wachter E. Anal. Biochem. 128:213-216(1983) [PubMed: 6846794] [Abstract] Cited for: SEQUENCE REVISION TO 43.
[7]	"Interchain disulfide bridges in ribonuclease BS-1." di Donato A., D'Alessio G. Biochem. Biophys. Res. Commun. 55:919-928(1973) [PubMed: 4761089] [Abstract] Cited for: INTERCHAIN DISULFIDE BONDS.
[8]	"Intrachain disulfide bridges of bovine seminal ribonuclease." di Donato A., D'Alessio G. Biochim. Biophys. Acta 579:303-313(1979) [PubMed: 534646] [Abstract] Cited for: INTRACHAIN DISULFIDE BONDS.
[9]	"Heterogeneity of bovine seminal ribonuclease." di Donato A., D'Alessio G. Biochemistry 20:7232-7237(1981) [PubMed: 7317378] [Abstract] Cited for: MULTIPLE FORMS.
[10]	"Dimeric structure of seminal ribonuclease." D'Alessio G., Parente A., Guida C., Leone E. FEBS Lett. 27:285-288(1972) [PubMed: 4664228] [Abstract] Cited for: ENZYME ACTIVITY.
[11]	"Seminal RNase: a unique member of the ribonuclease superfamily." D'Alessio G., di Donato A., Parente A., Piccoli R. Trends Biochem. Sci. 16:104-106(1991) [PubMed: 2057997] [Abstract] Cited for: REVIEW.
[12]	"Refinement of the structure of bovine seminal ribonuclease." Capasso S., Giordano F., Mattia C.A., Mazzarella L., Zagari A. Biopolymers 22:327-332(1983) [PubMed: 6673761] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[13]	"Bovine seminal ribonuclease: structure at 1.9-A resolution." Mazzarella L., Capasso S., Demasi D., di Lorenzo G., Mattia C.A., Zagari A. Acta Crystallogr. D 49:389-402(1993) [PubMed: 15299514] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[14]	"Swapping structural determinants of ribonucleases: an energetic analysis of the hinge peptide 16-22." Mazzarella K., Vitagliano L., Zagari A. Proc. Natl. Acad. Sci. U.S.A. 92:3799-3803(1995) [PubMed: 7731986] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
[15]	"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." Vitagliano L., Adinolfi S., Riccio A., Sica F., Zagari A., Mazzarella L. Protein Sci. 7:1691-1699(1998) [PubMed: 10082366] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X51337 mRNA. Translation: CAA35716.1.
AJ000518 Genomic DNA. Translation: CAA04155.1.
S81747 Genomic DNA. Translation: AAB36140.1.
X03029 mRNA. Translation: CAA26832.1.

IPI

IPI00700712.

PIR

NRBOS. S08392.

RefSeq

NP_861526.1.

UniGene

Bt.22955

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
11BA	X-ray	2.06	A/B	27-150	[»]
11BG	X-ray	1.90	A/B	27-150	[»]
1BSR	X-ray	1.90	A/B	27-150	[»]
1N1X	X-ray	1.45	A	27-150	[»]
1N3Z	X-ray	1.65	A	27-150	[»]
1QWQ	NMR	-	A	27-150	[»]
1R3M	X-ray	2.20	A/B	27-150	[»]
1R5C	X-ray	2.10	A/B	27-150	[»]
1R5D	X-ray	2.50	A/B	27-150	[»]
1TQ9	X-ray	2.00	A/B	27-150	[»]
1Y92	X-ray	2.20	A/B	27-150	[»]
1Y94	X-ray	2.20	A/B	27-150	[»]
3BCM	X-ray	2.25	A/B	27-150	[»]
3BCO	X-ray	2.25	A/B	27-150	[»]
3BCP	X-ray	2.57	A/B/C/D	27-150	[»]
3DJO	X-ray	1.60	A/B	27-150	[»]
3DJP	X-ray	1.60	A/B	27-150	[»]
3DJQ	X-ray	1.53	A/B	27-150	[»]
3DJV	X-ray	1.60	A/B	27-150	[»]
3DJX	X-ray	1.69	A/B	27-150	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000036229; ENSBTAP00000036091; ENSBTAG00000025663; Bos taurus. [Genome view]

GeneID

280930.

KEGG

bta:280930.

Organism-specific databases

CTD

280930.

Phylogenomic databases

eggNOG

maNOG20511.

HOVERGEN

P00669.

InParanoid

P00669.

OMA

HESWATV.

PhylomeDB

P00669.

Enzyme and pathway databases

BRENDA

3.1.27.5. 251.

Family and domain databases

InterPro

IPR001427. RNaseA.
[Graphical view]

Gene3D

G3DSA:3.10.130.10. RNaseA. 1 hit.

PANTHER

PTHR11437. RNaseA. 1 hit.

Pfam

PF00074. RnaseA. 1 hit.
[Graphical view]

PRINTS

PR00794. RIBONUCLEASE.

ProDom

PD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00092. RNAse_Pc. 1 hit.
[Graphical view]

PROSITE

PS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RNS_BOVIN

Accession

Primary (citable) accession number: P00669

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1990
Last modified:	January 19, 2010
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)