RNAS6_MOUSE
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 03-AUG-2022, entry version 129.
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.ENSMUSP00000093613; -.
DR GlyGen; Q9D244; 2 sites.
DR PaxDb; Q9D244; -.
DR PRIDE; Q9D244; -.
DR ProteomicsDB; 260985; -.
DR DNASU; 78416; -.
DR GeneID; 78416; -.
DR KEGG; mmu:78416; -.
DR CTD; 6039; -.
DR MGI; MGI:1925666; Rnase6.
DR eggNOG; ENOG502TDZ3; Eukaryota.
DR InParanoid; Q9D244; -.
DR OrthoDB; 1549558at2759; -.
DR PhylomeDB; Q9D244; -.
DR Reactome; R-MMU-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 78416; 1 hit in 71 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:ribonuclease 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 GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; ISO:MGI.
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; 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
