ID   RNAS6_MOUSE             Reviewed;         153 AA.
AC   Q9D244; A2RTT6; Q6QDX5;
DT   19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   24-JAN-2024, entry version 135.
DE   RecName: Full=Ribonuclease K6;
DE            Short=RNase K6;
DE            EC=3.1.27.- {ECO:0000269|PubMed:15693621};
DE   Flags: Precursor;
GN   Name=Rnase6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND TISSUE SPECIFICITY.
RX   PubMed=15693621; DOI=10.1007/s00239-004-2657-0;
RA   Dyer K.D., Rosenberg H.F., Zhang J.;
RT   "Isolation, characterization, and evolutionary divergence of mouse RNase 6:
RT   evidence for unusual evolution in rodents.";
RL   J. Mol. Evol. 59:657-665(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=25075772; DOI=10.1038/ki.2014.268;
RA   Becknell B., Eichler T.E., Beceiro S., Li B., Easterling R.S.,
RA   Carpenter A.R., James C.L., McHugh K.M., Hains D.S., Partida-Sanchez S.,
RA   Spencer J.D.;
RT   "Ribonucleases 6 and 7 have antimicrobial function in the human and murine
RT   urinary tract.";
RL   Kidney Int. 87:151-161(2015).
CC   -!- FUNCTION: Ribonuclease which shows a preference for the pyrimidines
CC       uridine and cytosine (PubMed:15693621). 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 (PubMed:15693621,
CC       PubMed:25075772). Causes loss of bacterial membrane integrity, and also
CC       promotes agglutination of Gram-negative bacteria (By similarity).
CC       Probably contributes to urinary tract sterility (PubMed:25075772).
CC       Bactericidal activity is independent of RNase activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q93091, ECO:0000269|PubMed:15693621,
CC       ECO:0000269|PubMed:25075772}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.1 uM for tRNA {ECO:0000269|PubMed:15693621};
CC   -!- SUBUNIT: Interacts (via N-terminus) with bacterial lipopolysaccharide
CC       (LPS). {ECO:0000250|UniProtKB:Q93091}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25075772}. Lysosome
CC       {ECO:0000305|PubMed:25075772}. Cytoplasmic granule
CC       {ECO:0000269|PubMed:25075772}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in spleen (at protein level)
CC       (PubMed:15693621, PubMed:25075772). Has little or no expression in
CC       healthy kidneys (at protein level) (PubMed:25075772). Detected at high
CC       levels in infected kidneys (at protein level) (PubMed:25075772).
CC       Expressed at low levels in bladder (PubMed:15693621, PubMed:25075772).
CC       Also detected in skeletal muscle, heart and bone marrow
CC       (PubMed:15693621). {ECO:0000269|PubMed:15693621}.
CC   -!- INDUCTION: Up-regulated in bone marrow derived macrophages in response
CC       to the uropathogenic E.coli strain CFT073.
CC       {ECO:0000269|PubMed:25075772}.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AY545655; AAS48640.1; -; mRNA.
DR   EMBL; AK020595; BAB32143.1; -; mRNA.
DR   EMBL; BC094892; AAH94892.1; -; mRNA.
DR   EMBL; BC132632; AAI32633.1; -; mRNA.
DR   CCDS; CCDS27037.1; -.
DR   RefSeq; NP_084374.2; NM_030098.2.
DR   RefSeq; XP_006519761.1; XM_006519698.2.
DR   AlphaFoldDB; Q9D244; -.
DR   SMR; Q9D244; -.
DR   STRING; 10090.ENSMUSP00000154125; -.
DR   GlyCosmos; Q9D244; 2 sites, No reported glycans.
DR   GlyGen; Q9D244; 2 sites.
DR   PaxDb; 10090-ENSMUSP00000093613; -.
DR   ProteomicsDB; 260985; -.
DR   DNASU; 78416; -.
DR   GeneID; 78416; -.
DR   KEGG; mmu:78416; -.
DR   AGR; MGI:1925666; -.
DR   CTD; 6039; -.
DR   MGI; MGI:1925666; Rnase6.
DR   eggNOG; ENOG502TDZ3; Eukaryota.
DR   InParanoid; Q9D244; -.
DR   OrthoDB; 4593516at2759; -.
DR   PhylomeDB; Q9D244; -.
DR   Reactome; R-MMU-6803157; Antimicrobial peptides.
DR   BioGRID-ORCS; 78416; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Rnase6; mouse.
DR   PRO; PR:Q9D244; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9D244; Protein.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
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:RNA nuclease activity; ISO:MGI.
DR   GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR   CDD; cd06265; RNase_A_canonical; 1.
DR   Gene3D; 3.10.130.10; Ribonuclease A-like domain; 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; RIBONUCLEASE; 1.
DR   PANTHER; PTHR11437:SF4; RIBONUCLEASE K6; 1.
DR   Pfam; PF00074; RnaseA; 1.
DR   PRINTS; PR00794; RIBONUCLEASE.
DR   SMART; SM00092; RNAse_Pc; 1.
DR   SUPFAM; SSF54076; RNase A-like; 1.
DR   PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Disulfide bond; Endonuclease; Glycoprotein;
KW   Hydrolase; Lysosome; Nuclease; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..153
FT                   /note="Ribonuclease K6"
FT                   /id="PRO_0000030900"
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        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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        42
FT                   /note="I -> V (in Ref. 2; BAB32143)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   153 AA;  17675 MW;  84A6C788AEE7CA05 CRC64;
     MVVDLPRYLP LLLLLELWEP MYLLCSQPKG LSRAHWFEIQ HIQTSRQPCN TAMRGVNNYT
     QHCKQINTFL HESFQNVAAT CSLHNITCKN GRKNCHESAE PVKMTDCSHT GGAYPNCRYS
     SDKQYKFFIV ACEHPKKEDP PYQLVPVHLD KIV
//