RNAS6_PIG
ID RNAS6_PIG Reviewed; 153 AA.
AC P81649; D0PSF9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Ribonuclease K3;
DE Short=RNase K3;
DE EC=3.1.27.- {ECO:0000269|PubMed:7764367};
DE Flags: Precursor;
GN Name=RNASE6; Synonyms=RNS6;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=19247805; DOI=10.1007/s11033-009-9471-0;
RA Bai X., Liang Z., Zhao S., Liu X., Zhu M., Wu Z., Yu M.;
RT "The porcine ANG, RNASE1 and RNASE6 genes: molecular cloning, polymorphism
RT detection and the association with haematological parameters.";
RL Mol. Biol. Rep. 36:2405-2411(2009).
RN [2]
RP PROTEIN SEQUENCE OF 27-152, FUNCTION, CATALYTIC ACTIVITY, AND GLYCOSYLATION
RP AT ASN-30; ASN-58 AND ASN-85.
RC TISSUE=Kidney;
RX PubMed=7764367; DOI=10.1271/bbb.57.2133;
RA Iwama M., Sanda A., Ohgi K., Hofsteenge J., Irie M.;
RT "Purification and primary structure of a porcine kidney non-secretory
RT ribonuclease.";
RL Biosci. Biotechnol. Biochem. 57:2133-2138(1993).
CC -!- FUNCTION: Ribonuclease which shows a preference for the pyrimidines
CC uridine and cytosine (PubMed:7764367). Has potent antibacterial
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:7764367}.
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.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; EU814502; ACJ26823.1; -; mRNA.
DR PIR; JC2034; JC2034.
DR RefSeq; NP_001161128.1; NM_001167656.1.
DR AlphaFoldDB; P81649; -.
DR SMR; P81649; -.
DR STRING; 9823.ENSSSCP00000027994; -.
DR iPTMnet; P81649; -.
DR PeptideAtlas; P81649; -.
DR GeneID; 100312981; -.
DR KEGG; ssc:100312981; -.
DR CTD; 6039; -.
DR eggNOG; ENOG502TDZ3; Eukaryota.
DR InParanoid; P81649; -.
DR OrthoDB; 1549558at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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: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..26
FT /evidence="ECO:0000269|PubMed:19247805"
FT CHAIN 27..153
FT /note="Ribonuclease K3"
FT /id="PRO_0000057163"
FT ACT_SITE 41
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q64438"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q64438"
FT BINDING 64..68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 62
FT /note="Facilitates cleavage of polynucleotide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q93091"
FT SITE 64
FT /note="Critical for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E1"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7764367"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7764367"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7764367"
FT DISULFID 49..107
FT /evidence="ECO:0000250|UniProtKB:Q93091"
FT DISULFID 63..117
FT /evidence="ECO:0000250|UniProtKB:Q93091"
FT DISULFID 81..132
FT /evidence="ECO:0000250|UniProtKB:Q93091"
FT DISULFID 88..95
FT /evidence="ECO:0000250|UniProtKB:Q93091"
FT CONFLICT 55
FT /note="S -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="S -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 17350 MW; DE6D7B9327F3B091 CRC64;
MGPDLRCFPL LLLLLGLWWS VRPLCAIPKN LTRAQWFTIQ HIQPSPLQCN KAMNSVNNYT
WHCKPQNTFL HDSFQDVATA CNLPNITCKN GQNNCHQSAK PVSLTQCSFT GGNYPNCRYK
DAAQYKFFIV ACDPPQKGDP PYPFVPVHLD KII
