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Protein

Seminal ribonuclease

Gene

SRN

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme hydrolyzes both single- and double-stranded RNA.

Catalytic activityi

Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates.1 Publication

Enzyme regulationi

Allosteric regulation by both substrate and reaction products.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331Substrate
Binding sitei36 – 361Substrate
Active sitei38 – 381Proton acceptor
Binding sitei92 – 921Substrate
Binding sitei111 – 1111Substrate
Active sitei145 – 1451Proton donor

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • nucleic acid binding Source: InterPro
  • ribonuclease A activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

BRENDAi3.1.27.5. 908.
SABIO-RKP00669.

Names & Taxonomyi

Protein namesi
Recommended name:
Seminal ribonuclease (EC:3.1.27.5)
Short name:
S-RNase
Short name:
Seminal RNase
Alternative name(s):
Ribonuclease BS-1
Gene namesi
Name:SRN
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 10

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 150124Seminal ribonucleasePRO_0000030910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 110
Disulfide bondi57 – 57Interchain
Disulfide bondi58 – 58Interchain
Disulfide bondi66 ↔ 121
Disulfide bondi84 ↔ 136
Disulfide bondi91 ↔ 98
Modified residuei93 – 931Deamidated asparagine; by deterioration1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP00669.
PRIDEiP00669.

Expressioni

Tissue specificityi

Seminal plasma. Can reach 3% of the protein content of this fluid.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-8524799,EBI-8524799

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

MINTiMINT-8050403.
STRINGi9913.ENSBTAP00000036091.

Chemistry

BindingDBiP00669.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 389Combined sources
Helixi48 – 503Combined sources
Helixi51 – 588Combined sources
Turni59 – 624Combined sources
Beta strandi63 – 653Combined sources
Beta strandi68 – 736Combined sources
Helixi77 – 815Combined sources
Helixi82 – 854Combined sources
Beta strandi86 – 894Combined sources
Beta strandi92 – 943Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi105 – 1128Combined sources
Beta strandi123 – 13715Combined sources
Turni138 – 1414Combined sources
Beta strandi142 – 1509Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
11BAX-ray2.06A/B27-150[»]
11BGX-ray1.90A/B27-150[»]
1BSRX-ray1.90A/B27-150[»]
1N1XX-ray1.45A27-150[»]
1N3ZX-ray1.65A27-150[»]
1QWQNMR-A27-150[»]
1R3MX-ray2.20A/B27-150[»]
1R5CX-ray2.10A/B27-150[»]
1R5DX-ray2.50A/B27-150[»]
1TQ9X-ray2.00A/B27-150[»]
1Y92X-ray2.20A/B27-150[»]
1Y94X-ray2.20A/B27-150[»]
2LFJNMR-A27-150[»]
3BCMX-ray2.25A/B27-150[»]
3BCOX-ray2.25A/B27-150[»]
3BCPX-ray2.57A/B/C/D27-150[»]
3DJOX-ray1.60A/B27-150[»]
3DJPX-ray1.60A/B27-150[»]
3DJQX-ray1.53A/B27-150[»]
3DJVX-ray1.60A/B27-150[»]
3DJXX-ray1.69A/B27-150[»]
4N4CX-ray2.48A/B27-150[»]
ProteinModelPortaliP00669.
SMRiP00669. Positions 27-150.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00669.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 715Substrate binding

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IYEN. Eukaryota.
ENOG41113F1. LUCA.
HOGENOMiHOG000276883.
HOVERGENiHBG008396.
InParanoidiP00669.
KOiK01168.
OMAiKSTMRIT.
OrthoDBiEOG7J1826.
TreeFamiTF333393.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00669-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALKSLVVLP LLVLVLLLVR VQPSLGKESA AAKFERQHMD SGNSPSSSSN
60 70 80 90 100
YCNLMMCCRK MTQGKCKPVN TFVHESLADV KAVCSQKKVT CKNGQTNCYQ
110 120 130 140 150
SKSTMRITDC RETGSSKYPN CAYKTTQVEK HIIVACGGKP SVPVHFDASV
Length:150
Mass (Da):16,377
Last modified:April 1, 1990 - v2
Checksum:iF7A05C930FB83A83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51337 mRNA. Translation: CAA35716.1.
AJ000518 Genomic DNA. Translation: CAA04155.1.
S81747 Genomic DNA. Translation: AAB36140.1.
X03029 mRNA. Translation: CAA26832.1.
PIRiS08392. NRBOS.
RefSeqiNP_861526.1. NM_181810.1.
UniGeneiBt.22955.

Genome annotation databases

EnsembliENSBTAT00000036229; ENSBTAP00000036091; ENSBTAG00000025663.
GeneIDi280930.
KEGGibta:280930.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51337 mRNA. Translation: CAA35716.1.
AJ000518 Genomic DNA. Translation: CAA04155.1.
S81747 Genomic DNA. Translation: AAB36140.1.
X03029 mRNA. Translation: CAA26832.1.
PIRiS08392. NRBOS.
RefSeqiNP_861526.1. NM_181810.1.
UniGeneiBt.22955.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
11BAX-ray2.06A/B27-150[»]
11BGX-ray1.90A/B27-150[»]
1BSRX-ray1.90A/B27-150[»]
1N1XX-ray1.45A27-150[»]
1N3ZX-ray1.65A27-150[»]
1QWQNMR-A27-150[»]
1R3MX-ray2.20A/B27-150[»]
1R5CX-ray2.10A/B27-150[»]
1R5DX-ray2.50A/B27-150[»]
1TQ9X-ray2.00A/B27-150[»]
1Y92X-ray2.20A/B27-150[»]
1Y94X-ray2.20A/B27-150[»]
2LFJNMR-A27-150[»]
3BCMX-ray2.25A/B27-150[»]
3BCOX-ray2.25A/B27-150[»]
3BCPX-ray2.57A/B/C/D27-150[»]
3DJOX-ray1.60A/B27-150[»]
3DJPX-ray1.60A/B27-150[»]
3DJQX-ray1.53A/B27-150[»]
3DJVX-ray1.60A/B27-150[»]
3DJXX-ray1.69A/B27-150[»]
4N4CX-ray2.48A/B27-150[»]
ProteinModelPortaliP00669.
SMRiP00669. Positions 27-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8050403.
STRINGi9913.ENSBTAP00000036091.

Chemistry

BindingDBiP00669.
ChEMBLiCHEMBL1075179.

Proteomic databases

PaxDbiP00669.
PRIDEiP00669.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000036229; ENSBTAP00000036091; ENSBTAG00000025663.
GeneIDi280930.
KEGGibta:280930.

Organism-specific databases

CTDi6035.

Phylogenomic databases

eggNOGiENOG410IYEN. Eukaryota.
ENOG41113F1. LUCA.
HOGENOMiHOG000276883.
HOVERGENiHBG008396.
InParanoidiP00669.
KOiK01168.
OMAiKSTMRIT.
OrthoDBiEOG7J1826.
TreeFamiTF333393.

Enzyme and pathway databases

BRENDAi3.1.27.5. 908.
SABIO-RKP00669.

Miscellaneous databases

EvolutionaryTraceiP00669.
PROiP00669.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 43.
  7. 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] [Europe PMC] [Abstract]
    Cited for: INTRACHAIN DISULFIDE BONDS.
  9. "Heterogeneity of bovine seminal ribonuclease."
    di Donato A., D'Alessio G.
    Biochemistry 20:7232-7237(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: MULTIPLE FORMS.
  10. 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] [Europe PMC] [Abstract]
    Cited for: REVIEW, DEAMIDATION AT ASN-93.
  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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  13. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS).

Entry informationi

Entry nameiRNS_BOVIN
AccessioniPrimary (citable) accession number: P00669
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: June 8, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Progressive deamidation of Asn-93 transforms the homodimer (beta- 2) into and heterodimer (alpha-beta) and finally a doubly deamidated dimer (alpha-2).1 Publication

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.