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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 Ca2+ or Mg2+.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei35Involved in actin-binding1
Sitei87Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme1
Sitei89Involved in actin-binding1
Active sitei1001 Publication1
Active sitei1562 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Actin-binding, Calcium

Enzyme and pathway databases

BRENDAi3.1.21.1. 908.

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
Proteomesi
  • UP000009136 Componenti: Chromosome 25

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5712.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000000727523 – 282Deoxyribonuclease-1Add BLAST260

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...)1
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

PaxDbiP00639.
PRIDEiP00639.

Expressioni

Gene expression databases

BgeeiENSBTAG00000020107.
ExpressionAtlasiP00639. differential.

Interactioni

Protein-protein interaction databases

DIPiDIP-541N.
MINTiMINT-1504668.
STRINGi9913.ENSBTAP00000054758.

Chemistry databases

BindingDBiP00639.

Structurei

Secondary structure

1282
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 34Combined sources11
Helixi35 – 39Combined sources5
Helixi41 – 51Combined sources11
Beta strandi55 – 62Combined sources8
Beta strandi65 – 67Combined sources3
Helixi68 – 77Combined sources10
Beta strandi79 – 81Combined sources3
Beta strandi86 – 89Combined sources4
Beta strandi95 – 97Combined sources3
Beta strandi100 – 106Combined sources7
Turni108 – 110Combined sources3
Beta strandi112 – 118Combined sources7
Beta strandi121 – 123Combined sources3
Turni124 – 126Combined sources3
Helixi127 – 130Combined sources4
Beta strandi136 – 141Combined sources6
Beta strandi145 – 154Combined sources10
Helixi159 – 161Combined sources3
Helixi162 – 180Combined sources19
Beta strandi185 – 190Combined sources6
Turni195 – 197Combined sources3
Helixi200 – 205Combined sources6
Helixi207 – 210Combined sources4
Beta strandi214 – 218Combined sources5
Beta strandi225 – 228Combined sources4
Beta strandi234 – 240Combined sources7
Helixi241 – 246Combined sources6
Helixi257 – 260Combined sources4
Helixi265 – 271Combined sources7
Beta strandi277 – 281Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00639.

Family & Domainsi

Sequence similaritiesi

Belongs to the DNase I family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFZB. Eukaryota.
ENOG410Z4MV. LUCA.
GeneTreeiENSGT00390000013146.
HOGENOMiHOG000059570.
HOVERGENiHBG051368.
InParanoidiP00639.
KOiK11994.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR018057. Deoxyribonuclease-1_AS.
IPR016202. DNase_I.
IPR033125. DNASE_I_2.
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)DescriptionActionsGraphical viewLength
Sequence conflicti217L → V in AAM93248 (PubMed:14680812).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti143H → P in allele C/D. 2 Publications1

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_010817356.1. XM_010819054.2.
XP_015315660.1. XM_015460174.1.
XP_015315661.1. XM_015460175.1.
XP_015315662.1. XM_015460176.1.
XP_015315663.1. XM_015460177.1.
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_010817356.1. XM_010819054.2.
XP_015315660.1. XM_015460174.1.
XP_015315661.1. XM_015460175.1.
XP_015315662.1. XM_015460176.1.
XP_015315663.1. XM_015460177.1.
UniGeneiBt.12952.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-541N.
MINTiMINT-1504668.
STRINGi9913.ENSBTAP00000054758.

Chemistry databases

BindingDBiP00639.
ChEMBLiCHEMBL5712.

Proteomic databases

PaxDbiP00639.
PRIDEiP00639.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1773.

Phylogenomic databases

eggNOGiENOG410IFZB. Eukaryota.
ENOG410Z4MV. LUCA.
GeneTreeiENSGT00390000013146.
HOGENOMiHOG000059570.
HOVERGENiHBG051368.
InParanoidiP00639.
KOiK11994.

Enzyme and pathway databases

BRENDAi3.1.21.1. 908.

Miscellaneous databases

EvolutionaryTraceiP00639.
PROiP00639.

Gene expression databases

BgeeiENSBTAG00000020107.
ExpressionAtlasiP00639. differential.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR018057. Deoxyribonuclease-1_AS.
IPR016202. DNase_I.
IPR033125. DNASE_I_2.
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...

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: November 30, 2016
This is version 156 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

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.