P00639 (DNAS1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Deoxyribonuclease-1
EC=3.1.21.1

Alternative name(s):
Deoxyribonuclease I
Short name=DNase I

Gene names

Name:	DNASE1
Synonyms:	DNL1

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	282 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	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 process	Apoptosis
Cellular component	Nucleus Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Actin-binding Calcium
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA catabolic process Inferred from electronic annotation. Source: InterPro apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear envelope Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW deoxyribonuclease I 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 – 22

22

Ref.4

Chain

23 – 282

260

Deoxyribonuclease-1

PRO_0000007275

Sites

Active site

100

1

Active site

156

1

Ref.8

Site

35

1

Involved in actin-binding

Site

87

1

Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme

Site

89

1

Involved in actin-binding

Amino acid modifications

Glycosylation

40

1

N-linked (GlcNAc...)

Disulfide bond

123 ↔ 126

Disulfide bond

195 ↔ 231

Essential for enzymatic activity

Natural variations

Natural variant

143

1

H → P in allele C/D. Ref.6 Ref.7

Experimental info

Sequence conflict

217

1

L → V in AAM93248. Ref.2

Secondary structure

1

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282

Helix Strand Turn

Details...

Beta strand

24 – 34

11

Helix

35 – 39

5

Helix

41 – 51

11

Beta strand

55 – 62

8

Helix

68 – 77

10

Beta strand

86 – 89

4

Beta strand

95 – 97

3

Beta strand

100 – 106

7

Turn

108 – 110

3

Beta strand

111 – 118

8

Beta strand

136 – 142

7

Beta strand

145 – 147

3

Beta strand

149 – 154

6

Helix

159 – 161

3

Helix

162 – 180

19

Beta strand

185 – 190

6

Helix

195 – 197

3

Helix

202 – 205

4

Helix

207 – 210

4

Beta strand

215 – 218

4

Beta strand

225 – 229

5

Beta strand

234 – 240

7

Helix

241 – 244

4

Helix

257 – 261

5

Helix

265 – 271

7

Beta strand

277 – 281

5

Sequences

	Sequence		Length	Mass (Da)
	P00639 [UniParc]. Last modified December 15, 1998. Version 3. Checksum: 43904EF0D5F2E0E2	FASTA	282	31,346
	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

References

	« Hide 'large scale' referencesShow '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: 9469931] [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: 14680812] [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: 4734471] [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: 1348510] [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: 4735137] [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: 4856650] [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: 4976790] [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: 5166750] [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: 3713845] [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: 3560229] [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: 3352748] [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: 1748997] [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: 1518054] [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: 2395459] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH ACTIN.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ001538 mRNA. Translation: CAA04819.1.
AF528509 Genomic DNA. Translation: AAM93248.1.
BC142349 mRNA. Translation: AAI42350.1.

IPI

IPI00694607.

PIR

NDBOA. JC6532.

RefSeq

NP_776959.1. NM_174534.2.

UniGene

Bt.12952.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ATN	X-ray	2.80	D	23-282	[»]
1DNK	X-ray	2.30	A	23-282	[»]
2A3Z	X-ray	2.08	B	23-282	[»]
2A40	X-ray	1.80	B/E	23-282	[»]
2A41	X-ray	2.60	B	23-282	[»]
2A42	X-ray	1.85	B	23-282	[»]
2D1K	X-ray	2.50	B	23-282	[»]
2DNJ	X-ray	2.00	A	23-282	[»]
3CJC	X-ray	3.90	D	23-282	[»]
3DNI	X-ray	2.00	A	23-282	[»]

ProteinModelPortal

P00639.

SMR

P00639. Positions 23-282.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-541N.

STRING

P00639.

Proteomic databases

PRIDE

P00639.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000026784; ENSBTAP00000026784; ENSBTAG00000020107.

GeneID

282217.

KEGG

bta:282217.

Organism-specific databases

CTD

1773.

Phylogenomic databases

eggNOG

maNOG04659.

HOVERGEN

HBG051368.

InParanoid

P00639.

OMA

SYKERYL.

OrthoDB

EOG4ZS93V.

PhylomeDB

P00639.

Family and domain databases

InterPro

IPR018057. Deoxyribonuclease-1_AS.
IPR016202. DNase_I-like.
IPR008185. DNase_I_euk.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]

KO

K11994.

PANTHER

PTHR11371. DNase_I. 1 hit.

Pfam

PF03372. Exo_endo_phos. 1 hit.
[Graphical view]

PIRSF

PIRSF000988. DNase_I_euk. 1 hit.

PRINTS

PR00130. DNASEI.

SMART

SM00476. DNaseIc. 1 hit.
[Graphical view]

SUPFAM

SSF56219. Exo_endo_phos. 1 hit.

PROSITE

PS00919. DNASE_I_1. 1 hit.
PS00918. DNASE_I_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DNAS1_BOVIN

Accession

Primary (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:	November 16, 2011
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program