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Protein

Deoxyribonuclease-1

Gene

DNASE1

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

Functioni

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

Catalytic activityi

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

Cofactori

Ca2+, Mg2+Note: Divalent metal cations. Prefers Ca(2+) or Mg2+.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei35 – 351Involved in actin-binding
Sitei87 – 871Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme
Sitei89 – 891Involved in actin-binding
Active sitei100 – 1001
Active sitei156 – 15611 Publication

GO - Molecular functioni

  1. deoxyribonuclease I activity Source: UniProtKB-EC
  2. endodeoxyribonuclease activity Source: GO_Central

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. DNA catabolic process, endonucleolytic Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Actin-binding, Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyribonuclease-1 (EC:3.1.21.1)
Alternative name(s):
Deoxyribonuclease I
Short name:
DNase I
Gene namesi
Name:DNASE1
Synonyms:DNL1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 25

Subcellular locationi

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

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. nuclear envelope Source: UniProtKB-SubCell
  3. nucleus Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 282260Deoxyribonuclease-1PRO_0000007275Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...)
Disulfide bondi123 ↔ 126
Disulfide bondi195 ↔ 231Essential for enzymatic activity

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP00639.

Expressioni

Gene expression databases

ExpressionAtlasiP00639. baseline.

Interactioni

Protein-protein interaction databases

DIPiDIP-541N.
MINTiMINT-1504668.

Structurei

Secondary structure

1
282
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 3411Combined sources
Helixi35 – 395Combined sources
Helixi41 – 5111Combined sources
Beta strandi55 – 628Combined sources
Beta strandi65 – 673Combined sources
Helixi68 – 7710Combined sources
Beta strandi79 – 813Combined sources
Beta strandi86 – 894Combined sources
Beta strandi95 – 973Combined sources
Beta strandi100 – 1067Combined sources
Turni108 – 1103Combined sources
Beta strandi112 – 1187Combined sources
Beta strandi121 – 1233Combined sources
Turni124 – 1263Combined sources
Helixi127 – 1304Combined sources
Beta strandi136 – 1416Combined sources
Beta strandi145 – 15410Combined sources
Helixi159 – 1613Combined sources
Helixi162 – 18019Combined sources
Beta strandi185 – 1906Combined sources
Turni195 – 1973Combined sources
Helixi200 – 2056Combined sources
Helixi207 – 2104Combined sources
Beta strandi214 – 2185Combined sources
Beta strandi225 – 2284Combined sources
Beta strandi234 – 2407Combined sources
Helixi241 – 2466Combined sources
Helixi257 – 2604Combined sources
Helixi265 – 2717Combined sources
Beta strandi277 – 2815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00639.
SMRiP00639. Positions 23-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00639.

Family & Domainsi

Sequence similaritiesi

Belongs to the DNase I family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG46375.
GeneTreeiENSGT00390000013146.
HOGENOMiHOG000059570.
HOVERGENiHBG051368.
InParanoidiP00639.
KOiK11994.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR018057. Deoxyribonuclease-1_AS.
IPR016202. DNase_I.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERiPTHR11371. PTHR11371. 1 hit.
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
PIRSFiPIRSF000988. DNase_I_euk. 1 hit.
PRINTSiPR00130. DNASEI.
SMARTiSM00476. DNaseIc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.
PROSITEiPS00919. DNASE_I_1. 1 hit.
PS00918. DNASE_I_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00639-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGTRLMGLL LALAGLLQLG LSLKIAAFNI RTFGETKMSN ATLASYIVRI
60 70 80 90 100
VRRYDIVLIQ EVRDSHLVAV GKLLDYLNQD DPNTYHYVVS EPLGRNSYKE
110 120 130 140 150
RYLFLFRPNK VSVLDTYQYD DGCESCGNDS FSREPAVVKF SSHSTKVKEF
160 170 180 190 200
AIVALHSAPS DAVAEINSLY DVYLDVQQKW HLNDVMLMGD FNADCSYVTS
210 220 230 240 250
SQWSSIRLRT SSTFQWLIPD SADTTATSTN CAYDRIVVAG SLLQSSVVPG
260 270 280
SAAPFDFQAA YGLSNEMALA ISDHYPVEVT LT
Length:282
Mass (Da):31,346
Last modified:December 15, 1998 - v3
Checksum:i43904EF0D5F2E0E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti217 – 2171L → V in AAM93248 (PubMed:14680812).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti143 – 1431H → P in allele C/D. 2 Publications

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001538 mRNA. Translation: CAA04819.1.
AF528509 Genomic DNA. Translation: AAM93248.1.
BC142349 mRNA. Translation: AAI42350.1.
PIRiJC6532. NDBOA.
RefSeqiNP_776959.1. NM_174534.2.
XP_010817355.1. XM_010819053.1.
XP_010817356.1. XM_010819054.1.
XP_010817357.1. XM_010819055.1.
XP_010817358.1. XM_010819056.1.
UniGeneiBt.12952.

Genome annotation databases

EnsembliENSBTAT00000026784; ENSBTAP00000026784; ENSBTAG00000020107.
GeneIDi282217.
KEGGibta:282217.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001538 mRNA. Translation: CAA04819.1.
AF528509 Genomic DNA. Translation: AAM93248.1.
BC142349 mRNA. Translation: AAI42350.1.
PIRiJC6532. NDBOA.
RefSeqiNP_776959.1. NM_174534.2.
XP_010817355.1. XM_010819053.1.
XP_010817356.1. XM_010819054.1.
XP_010817357.1. XM_010819055.1.
XP_010817358.1. XM_010819056.1.
UniGeneiBt.12952.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00639.
SMRiP00639. Positions 23-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-541N.
MINTiMINT-1504668.

Chemistry

BindingDBiP00639.
ChEMBLiCHEMBL5712.

Proteomic databases

PRIDEiP00639.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000026784; ENSBTAP00000026784; ENSBTAG00000020107.
GeneIDi282217.
KEGGibta:282217.

Organism-specific databases

CTDi1773.

Phylogenomic databases

eggNOGiNOG46375.
GeneTreeiENSGT00390000013146.
HOGENOMiHOG000059570.
HOVERGENiHBG051368.
InParanoidiP00639.
KOiK11994.

Miscellaneous databases

EvolutionaryTraceiP00639.
NextBioi20806041.

Gene expression databases

ExpressionAtlasiP00639. baseline.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR018057. Deoxyribonuclease-1_AS.
IPR016202. DNase_I.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERiPTHR11371. PTHR11371. 1 hit.
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
PIRSFiPIRSF000988. DNase_I_euk. 1 hit.
PRINTSiPR00130. DNASEI.
SMARTiSM00476. DNaseIc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.
PROSITEiPS00919. DNASE_I_1. 1 hit.
PS00918. DNASE_I_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiDNAS1_BOVIN
AccessioniPrimary (citable) accession number: P00639
Secondary accession number(s): A5PK44, Q8MJ27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 15, 1998
Last modified: March 4, 2015
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, 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

External Data

Dasty 3

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 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.