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RNT2B_MOUSE
ID   RNT2B_MOUSE             Reviewed;         259 AA.
AC   C0HKG6; Q9CQ01;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Ribonuclease T2-B {ECO:0000312|MGI:MGI:3702087};
DE            EC=4.6.1.19 {ECO:0000255|PROSITE-ProRule:PRU10045};
DE   AltName: Full=Ribonuclease 6-B {ECO:0000305};
DE   Flags: Precursor;
GN   Name=Rnaset2b {ECO:0000312|MGI:MGI:3702087};
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 {ECO:0000312|EMBL:BAC26326.1};
RC   TISSUE=Skin {ECO:0000312|EMBL:BAC26326.1};
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Ribonuclease that plays an essential role in innate immune
CC       response by recognizing and degrading RNAs from microbial pathogens
CC       that are subsequently sensed by TLR8. Cleaves preferentially single-
CC       stranded RNA molecules between purine and uridine residues, which
CC       critically contributes to the supply of catabolic uridine and the
CC       generation of purine-2',3'-cyclophosphate-terminated
CC       oligoribonucleotides. In turn, RNase T2 degradation products promote
CC       the RNA-dependent activation of TLR8. Also plays a key role in
CC       degradation of mitochondrial RNA and processing of non-coding RNA
CC       imported from the cytosol into mitochondria. Participates as well in
CC       degradation of mitochondrion-associated cytosolic rRNAs.
CC       {ECO:0000250|UniProtKB:O00584}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-
CC         phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA +
CC         H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-
CC         COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284,
CC         ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10045};
CC   -!- ACTIVITY REGULATION: Inhibited by Zn(2+) and Cu(2+).
CC       {ECO:0000250|UniProtKB:O00584}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O00584}. Lysosome
CC       lumen {ECO:0000250|UniProtKB:O00584}. Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:O00584}. Mitochondrion intermembrane space
CC       {ECO:0000250|UniProtKB:O00584}.
CC   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR   EMBL; AK029149; BAC26326.1; -; mRNA.
DR   CCDS; CCDS37429.1; -.
DR   RefSeq; NP_001077407.1; NM_001083938.2.
DR   RefSeq; NP_080887.1; NM_026611.2.
DR   AlphaFoldDB; C0HKG6; -.
DR   SMR; C0HKG6; -.
DR   GlyGen; C0HKG6; 3 sites.
DR   jPOST; C0HKG6; -.
DR   DNASU; 68195; -.
DR   Ensembl; ENSMUST00000089119; ENSMUSP00000086519; ENSMUSG00000094724.
DR   Ensembl; ENSMUST00000097420; ENSMUSP00000095031; ENSMUSG00000095687.
DR   Ensembl; ENSMUST00000179728; ENSMUSP00000137303; ENSMUSG00000094724.
DR   Ensembl; ENSMUST00000231550; ENSMUSP00000156290; ENSMUSG00000116876.
DR   Ensembl; ENSMUST00000231927; ENSMUSP00000156083; ENSMUSG00000095687.
DR   Ensembl; ENSMUST00000232307; ENSMUSP00000156372; ENSMUSG00000116988.
DR   GeneID; 100037283; -.
DR   GeneID; 68195; -.
DR   KEGG; mmu:100037283; -.
DR   KEGG; mmu:68195; -.
DR   CTD; 100037283; -.
DR   CTD; 68195; -.
DR   MGI; MGI:3702087; Rnaset2b.
DR   VEuPathDB; HostDB:ENSMUSG00000094724; -.
DR   VEuPathDB; HostDB:ENSMUSG00000095687; -.
DR   VEuPathDB; HostDB:ENSMUSG00000116876; -.
DR   VEuPathDB; HostDB:ENSMUSG00000116988; -.
DR   GeneTree; ENSGT00640000091563; -.
DR   OMA; DMRRYWP; -.
DR   OrthoDB; 994722at2759; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   ChiTaRS; Rnaset2b; mouse.
DR   PRO; PR:C0HKG6; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; C0HKG6; protein.
DR   Bgee; ENSMUSG00000094724; Expressed in right kidney and 109 other tissues.
DR   ExpressionAtlas; C0HKG6; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; ISO:MGI.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0004540; F:ribonuclease activity; ISO:MGI.
DR   GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006401; P:RNA catabolic process; ISO:MGI.
DR   CDD; cd01061; RNase_T2_euk; 1.
DR   Gene3D; 3.90.730.10; -; 1.
DR   InterPro; IPR033697; Ribonuclease_T2_eukaryotic.
DR   InterPro; IPR001568; RNase_T2-like.
DR   InterPro; IPR036430; RNase_T2-like_sf.
DR   InterPro; IPR018188; RNase_T2_His_AS_1.
DR   InterPro; IPR033130; RNase_T2_His_AS_2.
DR   PANTHER; PTHR11240; PTHR11240; 1.
DR   Pfam; PF00445; Ribonuclease_T2; 1.
DR   SUPFAM; SSF55895; SSF55895; 1.
DR   PROSITE; PS00530; RNASE_T2_1; 1.
DR   PROSITE; PS00531; RNASE_T2_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Endonuclease; Endoplasmic reticulum; Glycoprotein;
KW   Hydrolase; Immunity; Innate immunity; Lyase; Lysosome; Mitochondrion;
KW   Nuclease; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..259
FT                   /note="Ribonuclease T2-B"
FT                   /id="PRO_0000440153"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT   ACT_SITE        118
FT                   /evidence="ECO:0000250|UniProtKB:P08056"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..59
FT                   /evidence="ECO:0000250|UniProtKB:O00584"
FT   DISULFID        79..125
FT                   /evidence="ECO:0000250|UniProtKB:O00584"
FT   DISULFID        188..244
FT                   /evidence="ECO:0000250|UniProtKB:O00584"
FT   DISULFID        206..217
FT                   /evidence="ECO:0000250|UniProtKB:O00584"
SQ   SEQUENCE   259 AA;  29609 MW;  E0A1C1BBBEAA5033 CRC64;
     MAPAEARGAL PGWISVLGWG LALCSLCGAG PLWSGSHEWK KLILTQHWPP TVCKEVNSCQ
     DSLDYWTIHG LWPDRAEDCN QSWHFNLDEI KDLLRDMKIY WPDVIHRSSN RSQFWKHEWV
     KHGTCAAQVD ALNSEKKYFG KSLDLYKQID LNSVLQKFGI KPSINYYQLA DFKDALTRIY
     GVVPKIQCLM PEQGESVQTV GQIELCFTKE DLHLRNCTEP GEQLSSRQEA WLAMEASTHG
     MMVCEDGPIF YPPPTKTQH
 
 
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