RNK_MOUSE
ID RNK_MOUSE Reviewed; 98 AA.
AC Q8K3C0; Q3TAB4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ribonuclease kappa;
DE Short=RNase K;
DE Short=RNase kappa;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q6P5S7};
DE AltName: Full=V-type proton ATPase subunit f {ECO:0000250|UniProtKB:Q6P5S7};
DE Short=V-ATPase subunit f {ECO:0000250|UniProtKB:Q6P5S7};
GN Name=Rnasek; Synonyms=D11Bwg0434e;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Liver, and Mammary tumor;
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).
CC -!- FUNCTION: Endoribonuclease which preferentially cleaves ApU and ApG
CC phosphodiester bonds. Hydrolyzes UpU bonds at a lower rate (By
CC similarity). Regulates the activity of vacuolar (H+)-ATPase (V-ATPase)
CC which is responsible for acidifying and maintaining the pH of
CC intracellular compartments (By similarity). Required at an early stage
CC of receptor-mediated endocytosis (By similarity).
CC {ECO:0000250|UniProtKB:Q6P5S7}.
CC -!- SUBUNIT: Interacts with the proton translocation complex V0 of the V-
CC ATPase (By similarity). Interacts with ATP6AP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q6P5S7}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:Q6P5S7}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000250|UniProtKB:Q3ZC23}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the RNase K family. {ECO:0000305}.
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DR EMBL; AK009592; BAC25261.1; -; mRNA.
DR EMBL; AK171975; BAE42755.1; -; mRNA.
DR EMBL; AL669869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR933731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466596; EDL12546.1; -; Genomic_DNA.
DR EMBL; BC021602; AAH21602.2; -; mRNA.
DR EMBL; BC021603; AAH21603.2; -; mRNA.
DR EMBL; BC024417; AAH24417.1; -; mRNA.
DR CCDS; CCDS36204.1; -.
DR RefSeq; NP_776103.1; NM_173742.3.
DR AlphaFoldDB; Q8K3C0; -.
DR SMR; Q8K3C0; -.
DR STRING; 10090.ENSMUSP00000048271; -.
DR PhosphoSitePlus; Q8K3C0; -.
DR SwissPalm; Q8K3C0; -.
DR PaxDb; Q8K3C0; -.
DR PeptideAtlas; Q8K3C0; -.
DR PRIDE; Q8K3C0; -.
DR ProteomicsDB; 260991; -.
DR DNASU; 52898; -.
DR Ensembl; ENSMUST00000040428; ENSMUSP00000048271; ENSMUSG00000093989.
DR Ensembl; ENSMUST00000176268; ENSMUSP00000135088; ENSMUSG00000040904.
DR GeneID; 52898; -.
DR KEGG; mmu:52898; -.
DR UCSC; uc007jui.2; mouse.
DR CTD; 440400; -.
DR MGI; MGI:106369; Rnasek.
DR VEuPathDB; HostDB:ENSMUSG00000040904; -.
DR VEuPathDB; HostDB:ENSMUSG00000093989; -.
DR eggNOG; ENOG502S351; Eukaryota.
DR GeneTree; ENSGT00390000009664; -.
DR HOGENOM; CLU_140554_1_0_1; -.
DR InParanoid; Q8K3C0; -.
DR OMA; RQVGINC; -.
DR OrthoDB; 1615928at2759; -.
DR PhylomeDB; Q8K3C0; -.
DR TreeFam; TF300182; -.
DR BioGRID-ORCS; 52898; 25 hits in 71 CRISPR screens.
DR ChiTaRS; Rnasek; mouse.
DR PRO; PR:Q8K3C0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K3C0; protein.
DR Bgee; ENSMUSG00000040904; Expressed in bone marrow and 63 other tissues.
DR ExpressionAtlas; Q8K3C0; baseline and differential.
DR Genevisible; Q8K3C0; MM.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0048388; P:endosomal lumen acidification; ISS:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; ISS:UniProtKB.
DR InterPro; IPR026770; RNase_K.
DR PANTHER; PTHR31733; PTHR31733; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle; Endocytosis; Endonuclease; Hydrogen ion transport;
KW Hydrolase; Ion transport; Membrane; Nuclease; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..98
FT /note="Ribonuclease kappa"
FT /id="PRO_0000344222"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 96
FT /note="M -> I (in Ref. 1; BAE42755)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 98 AA; 10992 MW; B6B39A5CFDDB87EB CRC64;
MASLLCCGPK LAACGIVLSA WGVIMLIMLG IFFNVHSAVL IEDVPFTEKD FENGPQNIYN
LYEQVSYNCF IAAGLYLLLG GFSFCQVRLN KRKEYMVR
