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P00639

- DNAS1_BOVIN

UniProt

P00639 - DNAS1_BOVIN

Protein

Deoxyribonuclease-1

Gene

DNASE1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (15 Dec 1998)
      Previous versions | rss
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    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

    Divalent cations. Prefers calcium or magnesium.

    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

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW

    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

    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.

    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 – 3411
    Helixi35 – 395
    Helixi41 – 5111
    Beta strandi55 – 628
    Beta strandi65 – 673
    Helixi68 – 7710
    Beta strandi79 – 813
    Beta strandi86 – 894
    Beta strandi95 – 973
    Beta strandi100 – 1067
    Turni108 – 1103
    Beta strandi112 – 1187
    Beta strandi121 – 1233
    Turni124 – 1263
    Helixi127 – 1304
    Beta strandi136 – 1416
    Beta strandi145 – 15410
    Helixi159 – 1613
    Helixi162 – 18019
    Beta strandi185 – 1906
    Turni195 – 1973
    Helixi200 – 2056
    Helixi207 – 2104
    Beta strandi214 – 2185
    Beta strandi225 – 2284
    Beta strandi234 – 2407
    Helixi241 – 2466
    Helixi257 – 2604
    Helixi265 – 2717
    Beta strandi277 – 2815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MRGTRLMGLL LALAGLLQLG LSLKIAAFNI RTFGETKMSN ATLASYIVRI    50
    VRRYDIVLIQ EVRDSHLVAV GKLLDYLNQD DPNTYHYVVS EPLGRNSYKE 100
    RYLFLFRPNK VSVLDTYQYD DGCESCGNDS FSREPAVVKF SSHSTKVKEF 150
    AIVALHSAPS DAVAEINSLY DVYLDVQQKW HLNDVMLMGD FNADCSYVTS 200
    SQWSSIRLRT SSTFQWLIPD SADTTATSTN CAYDRIVVAG SLLQSSVVPG 250
    SAAPFDFQAA YGLSNEMALA ISDHYPVEVT LT 282
    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:
    EMBL
    GenBank
    DDBJ
    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_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.
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001538 mRNA. Translation: CAA04819.1 .
    AF528509 Genomic DNA. Translation: AAM93248.1 .
    BC142349 mRNA. Translation: AAI42350.1 .
    PIRi JC6532. NDBOA.
    RefSeqi NP_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.
    UniGenei Bt.12952.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    3W3D X-ray 1.80 B 23-282 [» ]
    ProteinModelPortali P00639.
    SMRi P00639. Positions 23-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-541N.
    MINTi MINT-1504668.

    Chemistry

    BindingDBi P00639.
    ChEMBLi CHEMBL5712.

    Proteomic databases

    PRIDEi P00639.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000026784 ; ENSBTAP00000026784 ; ENSBTAG00000020107 .
    GeneIDi 282217.
    KEGGi bta:282217.

    Organism-specific databases

    CTDi 1773.

    Phylogenomic databases

    eggNOGi NOG46375.
    GeneTreei ENSGT00390000013146.
    HOGENOMi HOG000059570.
    HOVERGENi HBG051368.
    InParanoidi P00639.
    KOi K11994.

    Miscellaneous databases

    EvolutionaryTracei P00639.
    NextBioi 20806041.

    Family and domain databases

    Gene3Di 3.60.10.10. 1 hit.
    InterProi IPR018057. Deoxyribonuclease-1_AS.
    IPR016202. DNase_I.
    IPR005135. Endo/exonuclease/phosphatase.
    [Graphical view ]
    PANTHERi PTHR11371. PTHR11371. 1 hit.
    Pfami PF03372. Exo_endo_phos. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000988. DNase_I_euk. 1 hit.
    PRINTSi PR00130. DNASEI.
    SMARTi SM00476. DNaseIc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56219. SSF56219. 1 hit.
    PROSITEi PS00919. DNASE_I_1. 1 hit.
    PS00918. DNASE_I_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 133 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