DNAS1_OREMO
ID DNAS1_OREMO Reviewed; 284 AA.
AC O42446;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Deoxyribonuclease-1;
DE EC=3.1.21.1 {ECO:0000269|PubMed:9395327};
DE AltName: Full=Deoxyribonuclease I;
DE Short=DNase I;
DE Flags: Precursor;
GN Name=dnase1;
OS Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8127;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-284, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP GLYCOSYLATION AT ASN-44.
RC TISSUE=Hepatopancreas;
RX PubMed=9395327; DOI=10.1111/j.1432-1033.1997.t01-2-00786.x;
RA Hsiao Y.-M., Ho H.-C., Wang W.-Y., Tam M.F., Liao T.-H.;
RT "Purification and characterization of tilapia (Oreochromis mossambicus)
RT deoxyribonuclease I. Primary structure and cDNA sequence.";
RL Eur. J. Biochem. 249:786-791(1997).
CC -!- FUNCTION: Serum endocuclease secreted into body fluids by a wide
CC variety of exocrine and endocrine organs (PubMed:9395327). Expressed by
CC non-hematopoietic tissues and preferentially cleaves protein-free DNA
CC (By similarity). Among other functions, seems to be involved in cell
CC death by apoptosis (By similarity). Binds specifically to G-actin and
CC blocks actin polymerization. Preferentially attacks double-stranded DNA
CC and produces oligonucleotides with 5'-phospho and 3'-hydroxy termini
CC (PubMed:9395327). {ECO:0000250|UniProtKB:P21704,
CC ECO:0000269|PubMed:9395327}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-
CC phosphooligonucleotide end-products.; EC=3.1.21.1;
CC Evidence={ECO:0000269|PubMed:9395327};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:9395327};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9395327};
CC Note=Divalent metal cations. Prefers Ca(2+) or Mg(2+) which have a
CC synergistic effect on activation. {ECO:0000269|PubMed:9395327};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:9395327};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9395327}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen
CC granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope
CC {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in
CC zymogen granules and found in the nuclear envelope.
CC {ECO:0000250|UniProtKB:P24855}.
CC -!- SIMILARITY: Belongs to the DNase I family. {ECO:0000305}.
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DR EMBL; AJ001305; CAA04665.1; -; mRNA.
DR AlphaFoldDB; O42446; -.
DR SMR; O42446; -.
DR iPTMnet; O42446; -.
DR PRIDE; O42446; -.
DR BRENDA; 3.1.21.1; 4428.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0042588; C:zymogen granule; IEA:UniProtKB-SubCell.
DR GO; GO:0004530; F:deoxyribonuclease I activity; IEA:UniProtKB-EC.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; ISS:UniProtKB.
DR GO; GO:0002283; P:neutrophil activation involved in immune response; ISS:UniProtKB.
DR GO; GO:0002673; P:regulation of acute inflammatory response; ISS:UniProtKB.
DR GO; GO:0070948; P:regulation of neutrophil mediated cytotoxicity; ISS:UniProtKB.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR018057; Deoxyribonuclease-1_AS.
DR InterPro; IPR016202; DNase_I.
DR InterPro; IPR033125; DNASE_I_2.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR PIRSF; PIRSF000988; DNase_I_euk; 1.
DR PRINTS; PR00130; DNASEI.
DR SMART; SM00476; DNaseIc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS00919; DNASE_I_1; 1.
DR PROSITE; PS00918; DNASE_I_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW Endonuclease; Glycoprotein; Hydrolase; Nuclease; Nucleus; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:9395327"
FT CHAIN 27..284
FT /note="Deoxyribonuclease-1"
FT /id="PRO_0000007283"
FT ACT_SITE 103
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT ACT_SITE 159
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT SITE 90
FT /note="Nitration by tetranitromethane destroys a Ca(2+)
FT binding site and inactivates enzyme"
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT SITE 92
FT /note="Involved in actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9395327"
FT DISULFID 198..234
FT /note="Essential for enzymatic activity"
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT VARIANT 151
FT /note="R -> K"
FT /evidence="ECO:0000269|PubMed:9395327"
SQ SEQUENCE 284 AA; 32216 MW; D5154AF0C782B595 CRC64;
MQTYRSRMHL VCSLGLFLTL LHLSNSLLLG AFNIKSFGDT KASNATLMNI ITKIVKRYDV
ILIQEVRDSD LSATQTLMNY VNKDSPQYKY IVSEPLGAST YKERYLFLYR EALVSVVKSY
TYDDGPEETG QDTFSREPFV VMFSSKNTAV RDFTLIPQHT SPDLAVRELN ALYDVVLDVR
ARWNTNDIVL LGDFNAGCSY VSGSAWQQIR IFTDKTFHWL ITDAADTTVS QTVCPYDRIV
VTTDMMRGVV QNSAKVYNYM TDLNLKQDLA LAVSDHFPVE VKLS
