ID   RNAS6_GORGO             Reviewed;         150 AA.
AC   O46532;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Ribonuclease K6;
DE            Short=RNase K6;
DE            EC=3.1.27.-;
DE   Flags: Precursor;
GN   Name=RNASE6;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9647635; DOI=10.1101/gr.8.6.599;
RA   Deming M.S., Dyer K.D., Bankier A.T., Piper M.B., Dear P.H.,
RA   Rosenberg H.F.;
RT   "Ribonuclease k6: chromosomal mapping and divergent rates of evolution
RT   within the RNase A gene superfamily.";
RL   Genome Res. 8:599-607(1998).
CC   -!- FUNCTION: Ribonuclease which shows a preference for the pyrimidines
CC       uridine and cytosine. Has potent antibacterial activity against a range
CC       of Gram-positive and Gram-negative bacteria, including P.aeruginosa,
CC       A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus
CC       and E.coli. Causes loss of bacterial membrane integrity, and also
CC       promotes agglutination of Gram-negative bacteria. Probably contributes
CC       to urinary tract sterility. Bactericidal activity is independent of
CC       RNase activity. {ECO:0000250|UniProtKB:Q93091}.
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   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AF037088; AAB94750.1; -; Genomic_DNA.
DR   AlphaFoldDB; O46532; -.
DR   SMR; O46532; -.
DR   STRING; 9593.ENSGGOP00000027666; -.
DR   eggNOG; ENOG502TDZ3; Eukaryota.
DR   InParanoid; O46532; -.
DR   Proteomes; UP000001519; 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   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Disulfide bond; Endonuclease; Glycoprotein;
KW   Hydrolase; Lysosome; Nuclease; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..150
FT                   /note="Ribonuclease K6"
FT                   /id="PRO_0000030891"
FT   ACT_SITE        38
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q64438"
FT   ACT_SITE        145
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q64438"
FT   BINDING         61..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            59
FT                   /note="Facilitates cleavage of polynucleotide substrates"
FT                   /evidence="ECO:0000250|UniProtKB:Q93091"
FT   SITE            61
FT                   /note="Critical for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H1E1"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..104
FT                   /evidence="ECO:0000250|UniProtKB:Q93091"
FT   DISULFID        60..114
FT                   /evidence="ECO:0000250|UniProtKB:Q93091"
FT   DISULFID        78..129
FT                   /evidence="ECO:0000250|UniProtKB:Q93091"
FT   DISULFID        85..92
FT                   /evidence="ECO:0000250|UniProtKB:Q93091"
SQ   SEQUENCE   150 AA;  17222 MW;  D33EA034CD487E71 CRC64;
     MVLCFPLLLL LLVLWGPVCP LHAWPKRLTK AHWFEIQHIQ PSPLQCNRAM IGINNYTQHC
     KHQNTFLHDS FQNVAAVCDL LSIVCKNRRH NCHQSSKPVN MTDCRLTSGK YPQCRYSAAA
     QYKFFIVACD PPQKSDPPYK LVPVHLDSIL