RNAS6_BOVIN
ID RNAS6_BOVIN Reviewed; 154 AA.
AC P08904; Q32L16; Q95324; Q9TUP9;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ribonuclease K6;
DE Short=RNase K6;
DE EC=3.1.27.- {ECO:0000269|PubMed:3926759};
DE AltName: Full=K6b;
DE AltName: Full=Ribonuclease K2;
DE Short=RNase K2;
DE Flags: Precursor;
GN Name=RNASE6; Synonyms=RK6B, RNS6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spinal cord;
RX PubMed=11092753; DOI=10.3109/10425170009033257;
RA Pietrowski D., Forster M.;
RT "Complete cDNA sequence and amino acid analysis of a bovine ribonuclease K6
RT gene.";
RL DNA Seq. 11:365-371(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 28-154.
RX PubMed=3182769; DOI=10.1093/oxfordjournals.jbchem.a122460;
RA Irie M., Nitta R., Ohgi K., Niwata Y., Watanabe H., Iwama M.,
RA Beintema J.J., Sanda A., Takizawa Y.;
RT "Primary structure of a non-secretory ribonuclease from bovine kidney.";
RL J. Biochem. 104:289-296(1988).
RN [4]
RP PROTEIN SEQUENCE OF 28-57, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=3926759; DOI=10.1093/oxfordjournals.jbchem.a135134;
RA Niwata Y., Ohgi K., Sanda A., Takizawa Y., Irie M.;
RT "Purification and properties of bovine kidney ribonucleases.";
RL J. Biochem. 97:923-934(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-129.
RX PubMed=8836175; DOI=10.1093/nar/24.18.3507;
RA Rosenberg H.F., Dyer K.D.;
RT "Molecular cloning and characterization of a novel human ribonuclease
RT (RNase k6): increasing diversity in the enlarging ribonuclease gene
RT family.";
RL Nucleic Acids Res. 24:3507-3513(1996).
CC -!- FUNCTION: Ribonuclease which shows a preference for the pyrimidines
CC uridine and cytosine (PubMed:3926759). Has potent antimicrobial
CC activity against a range of Gram-positive and Gram-negative bacteria,
CC including P.aeruginosa, A.baumanii, M.luteus, S.aureus, E.faecalis,
CC E.faecium, S.saprophyticus and E.coli (By similarity). Causes loss of
CC bacterial membrane integrity, and also promotes agglutination of Gram-
CC negative bacteria (By similarity). Probably contributes to urinary
CC tract sterility (By similarity). Bactericidal activity is independent
CC of RNase activity (By similarity). {ECO:0000250|UniProtKB:Q93091,
CC ECO:0000269|PubMed:3926759}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:3926759};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. Activity declines with
CC increasing temperature, with loss of stability at 90 degrees Celsius.
CC {ECO:0000269|PubMed:3926759};
CC -!- SUBUNIT: Interacts (via N-terminus) with bacterial lipopolysaccharide
CC (LPS). {ECO:0000250|UniProtKB:Q93091}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q93091}. Lysosome
CC {ECO:0000250|UniProtKB:Q93091}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q93091}.
CC -!- TISSUE SPECIFICITY: Kidney (at protein level).
CC {ECO:0000269|PubMed:3926759}.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; AF164025; AAD44349.1; -; mRNA.
DR EMBL; BC109812; AAI09813.1; -; mRNA.
DR EMBL; U64997; AAC48633.1; -; Genomic_DNA.
DR PIR; A05315; A05315.
DR PIR; S72363; S72363.
DR RefSeq; NP_777019.1; NM_174594.2.
DR RefSeq; XP_010807378.1; XM_010809076.1.
DR AlphaFoldDB; P08904; -.
DR SMR; P08904; -.
DR STRING; 9913.ENSBTAP00000011585; -.
DR PaxDb; P08904; -.
DR Ensembl; ENSBTAT00000011585; ENSBTAP00000011585; ENSBTAG00000008792.
DR GeneID; 282341; -.
DR KEGG; bta:282341; -.
DR CTD; 6039; -.
DR VEuPathDB; HostDB:ENSBTAG00000008792; -.
DR VGNC; VGNC:33999; RNASE6.
DR eggNOG; ENOG502TDZ3; Eukaryota.
DR GeneTree; ENSGT00940000161733; -.
DR HOGENOM; CLU_117006_0_1_1; -.
DR InParanoid; P08904; -.
DR OMA; LTKAHWF; -.
DR OrthoDB; 1549558at2759; -.
DR TreeFam; TF333393; -.
DR Reactome; R-BTA-6803157; Antimicrobial peptides.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000008792; Expressed in neutrophil and 108 other tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR Gene3D; 3.10.130.10; -; 1.
DR InterPro; IPR001427; RNaseA.
DR InterPro; IPR036816; RNaseA-like_dom_sf.
DR InterPro; IPR023411; RNaseA_AS.
DR InterPro; IPR023412; RNaseA_domain.
DR PANTHER; PTHR11437; PTHR11437; 1.
DR Pfam; PF00074; RnaseA; 1.
DR PRINTS; PR00794; RIBONUCLEASE.
DR SMART; SM00092; RNAse_Pc; 1.
DR SUPFAM; SSF54076; SSF54076; 1.
DR PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Endonuclease; Glycoprotein; Hydrolase; Lysosome; Nuclease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:3182769,
FT ECO:0000269|PubMed:3926759"
FT CHAIN 28..154
FT /note="Ribonuclease K6"
FT /id="PRO_0000030888"
FT ACT_SITE 42
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q64438"
FT ACT_SITE 149
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q64438"
FT BINDING 65..69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 63
FT /note="Facilitates cleavage of polynucleotide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q93091"
FT SITE 65
FT /note="Critical for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E1"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..108
FT /evidence="ECO:0000250|UniProtKB:Q93091"
FT DISULFID 64..118
FT /evidence="ECO:0000250|UniProtKB:Q93091"
FT DISULFID 82..133
FT /evidence="ECO:0000250|UniProtKB:Q93091"
FT DISULFID 89..96
FT /evidence="ECO:0000250|UniProtKB:Q93091"
FT CONFLICT 45..51
FT /note="PRLLQCN -> SRIIPCS (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="K -> N (in Ref. 5; AAC48633)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="H -> N (in Ref. 2; AAI09813)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..154
FT /note="VV -> YF (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 17661 MW; 9325DF841EF39C11 CRC64;
MGPHLLGRSS LLLLLLGMWW SVRPLCAVPK GLTKARWFEI QHIQPRLLQC NKAMSGVNNY
TQHCKPENTF LHNVFQDVTA VCDMPNIICK NGRHNCHQSP KPVNLTQCNF IAGRYPDCRY
HDDAQYKFFI VACDPPQKTD PPYHLVPVHL DKVV
