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P00639 (DNAS1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxyribonuclease-1

EC=3.1.21.1
Alternative name(s):
Deoxyribonuclease I
Short name=DNase I
Gene names
Name:DNASE1
Synonyms:DNL1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization By similarity.

Catalytic activity

Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.

Cofactor

Divalent cations. Prefers calcium or magnesium.

Subcellular location

Secreted. Nucleus envelope. Note: Secretory protein, stored in zymogen granules and found in the nuclear envelope.

Post-translational modification

The only differences between the A and B forms and the C and D forms are in the compositions of the carbohydrate bound to Asn-40.

Sequence similarities

Belongs to the DNase I family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentNucleus
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandActin-binding
Calcium
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear envelope

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondeoxyribonuclease I activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.4
Chain23 – 282260Deoxyribonuclease-1
PRO_0000007275

Sites

Active site1001
Active site1561 Ref.8
Site351Involved in actin-binding
Site871Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme
Site891Involved in actin-binding

Amino acid modifications

Glycosylation401N-linked (GlcNAc...)
Disulfide bond123 ↔ 126
Disulfide bond195 ↔ 231Essential for enzymatic activity

Natural variations

Natural variant1431H → P in allele C/D. Ref.6 Ref.7

Experimental info

Sequence conflict2171L → V in AAM93248. Ref.2

Secondary structure

....................................................... 282
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00639 [UniParc].

Last modified December 15, 1998. Version 3.
Checksum: 43904EF0D5F2E0E2

FASTA28231,346
        10         20         30         40         50         60 
MRGTRLMGLL LALAGLLQLG LSLKIAAFNI RTFGETKMSN ATLASYIVRI VRRYDIVLIQ 

        70         80         90        100        110        120 
EVRDSHLVAV GKLLDYLNQD DPNTYHYVVS EPLGRNSYKE RYLFLFRPNK VSVLDTYQYD 

       130        140        150        160        170        180 
DGCESCGNDS FSREPAVVKF SSHSTKVKEF AIVALHSAPS DAVAEINSLY DVYLDVQQKW 

       190        200        210        220        230        240 
HLNDVMLMGD FNADCSYVTS SQWSSIRLRT SSTFQWLIPD SADTTATSTN CAYDRIVVAG 

       250        260        270        280 
SLLQSSVVPG SAAPFDFQAA YGLSNEMALA ISDHYPVEVT LT 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing and expression of a cDNA encoding bovine pancreatic deoxyribonuclease I in Escherichia coli: purification and characterization of the recombinant enzyme."
Chen C.Y., Lu S.C., Liao T.H.
Gene 206:181-184(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[2]"Bovine DNase I: gene organization, mRNA expression, and changes in the topological distribution of the protein during apoptosis in lens epithelial cells."
De Maria A., Arruti C.
Biochem. Biophys. Res. Commun. 312:634-641(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal pancreas.
[4]"Bovine pancreatic deoxyribonuclease A. Isolation of cyanogen bromide peptides; complete covalent structure of the polypeptide chain."
Liao T.-H., Salnikow J., Moore S., Stein W.H.
J. Biol. Chem. 248:1489-1495(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-260.
[5]Erratum
Liao T.-H., Salnikow J., Moore S., Stein W.H.
J. Biol. Chem. 267:7957-7957(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[6]"Bovine pancreatic deoxyribonucleases A and C. A proline for histidine substitution in deoxyribonuclease C."
Salnikow J., Murphy D.
J. Biol. Chem. 248:1499-1501(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALLELE C/D PRO-143.
[7]"Bovine pancreatic deoxyribonuclease D."
Liao T.-H.
J. Biol. Chem. 249:2354-2356(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALLELE C/D PRO-143.
[8]"Alkylation of a histidine residue at the active site of bovine pancreatic deoxyribonuclease."
Price P.A., Moore S., Stein W.H.
J. Biol. Chem. 244:924-928(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE HIS-156.
[9]"Involvement of a tyrosine residue in the activity of bovine pancreatic deoxyribonuclease A."
Hugli T.E., Stein W.H.
J. Biol. Chem. 246:7191-7200(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE TYR-87.
[10]"Structure of DNase I at 2.0-A resolution suggests a mechanism for binding to and cutting DNA."
Suck D., Oefner C.
Nature 321:620-625(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
[11]"Crystallographic refinement and structure of DNase I at 2-A resolution."
Oefner C., Suck D.
J. Mol. Biol. 192:605-632(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
[12]"Structure refined to 2 A of a nicked DNA octanucleotide complex with DNase I."
Suck D., Lahm A., Oefner C.
Nature 332:464-468(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS) WITH NICKED DNA OCTANUCLEOTIDE.
[13]"DNase I-induced DNA conformation. 2-A structure of a DNase I-octamer complex."
Lahm A., Suck D.
J. Mol. Biol. 222:645-667(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
[14]"X-ray structure of the DNase I-d(GGTATACC)2 complex at 2.3-A resolution."
Weston S.A., Lahm A., Suck D.
J. Mol. Biol. 226:1237-1256(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[15]"Atomic structure of the actin:DNase I complex."
Kabsch W., Mannherz H.G., Suck D., Pai E.F., Holmes K.C.
Nature 347:37-44(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH ACTIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ001538 mRNA. Translation: CAA04819.1.
AF528509 Genomic DNA. Translation: AAM93248.1.
BC142349 mRNA. Translation: AAI42350.1.
PIRNDBOA. JC6532.
RefSeqNP_776959.1. NM_174534.2.
XP_005224438.1. XM_005224381.1.
XP_005224439.1. XM_005224382.1.
XP_005224440.1. XM_005224383.1.
XP_005224441.1. XM_005224384.1.
XP_005224442.1. XM_005224385.1.
UniGeneBt.12952.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ATNX-ray2.80D23-282[»]
1DNKX-ray2.30A23-282[»]
2A3ZX-ray2.08B23-282[»]
2A40X-ray1.80B/E23-282[»]
2A41X-ray2.60B23-282[»]
2A42X-ray1.85B23-282[»]
2D1KX-ray2.50B23-282[»]
2DNJX-ray2.00A23-282[»]
3CJCX-ray3.90D23-282[»]
3DNIX-ray2.00A23-282[»]
3W3DX-ray1.80B23-282[»]
ProteinModelPortalP00639.
SMRP00639. Positions 23-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-541N.
MINTMINT-1504668.

Chemistry

BindingDBP00639.
ChEMBLCHEMBL5712.

Proteomic databases

PRIDEP00639.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000026784; ENSBTAP00000026784; ENSBTAG00000020107.
GeneID282217.
KEGGbta:282217.

Organism-specific databases

CTD1773.

Phylogenomic databases

eggNOGNOG46375.
GeneTreeENSGT00390000013146.
HOGENOMHOG000059570.
HOVERGENHBG051368.
InParanoidP00639.
KOK11994.

Family and domain databases

Gene3D3.60.10.10. 1 hit.
InterProIPR018057. Deoxyribonuclease-1_AS.
IPR016202. DNase_I.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERPTHR11371. PTHR11371. 1 hit.
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
PIRSFPIRSF000988. DNase_I_euk. 1 hit.
PRINTSPR00130. DNASEI.
SMARTSM00476. DNaseIc. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 1 hit.
PROSITEPS00919. DNASE_I_1. 1 hit.
PS00918. DNASE_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00639.
NextBio20806041.

Entry information

Entry nameDNAS1_BOVIN
AccessionPrimary (citable) accession number: P00639
Secondary accession number(s): A5PK44, Q8MJ27
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 15, 1998
Last modified: April 16, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references