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Q5HZJ0

- RNC_MOUSE

UniProt

Q5HZJ0 - RNC_MOUSE

Protein

Ribonuclease 3

Gene

Drosha

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
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    Functioni

    Ribonuclease III double-stranded (ds) RNA-specific endoribonuclease that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DROSHA cleaves the 3' and 5' strands of a stem-loop in pri-miRNAs (processing center 11 bp from the dsRNA-ssRNA junction) to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. Involved also in pre-rRNA processing. Cleaves double-strand RNA and does not cleave single-strand RNA. Involved in the formation of GW bodies By similarity.By similarity

    Catalytic activityi

    Endonucleolytic cleavage to 5'-phosphomonoester.

    Cofactori

    Magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1146 – 11461Magnesium or manganeseBy similarity
    Sitei1214 – 12141Important for activityBy similarity
    Metal bindingi1218 – 12181Magnesium or manganeseBy similarity
    Metal bindingi1221 – 12211Magnesium or manganeseBy similarity

    GO - Molecular functioni

    1. endoribonuclease activity Source: MGI
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. ribonuclease III activity Source: UniProtKB-EC
    5. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. miRNA metabolic process Source: MGI
    2. pre-miRNA processing Source: MGI
    3. regulation of gene expression Source: MGI
    4. ribosome biogenesis Source: UniProtKB-KW
    5. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    6. rRNA catabolic process Source: InterPro

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    Ribosome biogenesis

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_221178. MicroRNA (miRNA) biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease 3 (EC:3.1.26.3)
    Alternative name(s):
    Protein Drosha
    Ribonuclease III
    Short name:
    RNase III
    Gene namesi
    Name:Drosha
    Synonyms:Etohi2, Rn3, Rnasen
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1261425. Drosha.

    Subcellular locationi

    Nucleus By similarity. Nucleusnucleolus By similarity
    Note: A fraction is translocated to the nucleolus during the S phase of the cell cycle. Localized in GW bodies (GWBs), also known as P-bodies By similarity.By similarity

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13731373Ribonuclease 3PRO_0000384374Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei372 – 3721PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ5HZJ0.
    PRIDEiQ5HZJ0.

    PTM databases

    PhosphoSiteiQ5HZJ0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ5HZJ0.
    BgeeiQ5HZJ0.
    GenevestigatoriQ5HZJ0.

    Interactioni

    Subunit structurei

    Component of the microprocessor complex, or pri-miRNA processing protein complex, which is composed of DROSHA and DGCR8. The microprocessor complex may contain multiple subunit of DGCR8 and DROSHA. Interacts with DGCR8, SP1 and SNIP1 By similarity. Interacts with SRRT/ARS2.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi199531. 1 interaction.
    IntActiQ5HZJ0. 1 interaction.
    STRINGi10090.ENSMUSP00000087762.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5HZJ0.
    SMRiQ5HZJ0. Positions 961-1336.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini875 – 1055181RNase III 1Add
    BLAST
    Domaini1106 – 1232127RNase III 2Add
    BLAST
    Domaini1259 – 133375DRBMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni489 – 1373885Necessary for interaction with DGCR8 and pri-miRNA processing activityBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi28 – 211184Pro-richAdd
    BLAST
    Compositional biasi217 – 31599Arg-richAdd
    BLAST

    Domaini

    The 2 RNase III domains form an intramolecular dimer where the domain 1 cuts the 3'strand while the domain 2 cleaves the 5'strand of pri-miRNAs, independently of each other.By similarity

    Sequence similaritiesi

    Contains 2 RNase III domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0571.
    GeneTreeiENSGT00730000111052.
    HOGENOMiHOG000122291.
    InParanoidiQ5HZJ0.
    KOiK03685.
    OMAiESYYSND.
    OrthoDBiEOG773XF7.
    PhylomeDBiQ5HZJ0.
    TreeFamiTF314734.

    Family and domain databases

    Gene3Di1.10.1520.10. 3 hits.
    3.30.160.20. 1 hit.
    HAMAPiMF_00104. RNase_III.
    InterProiIPR014720. dsRNA-bd_dom.
    IPR011907. RNase_III.
    IPR000999. RNase_III_dom.
    [Graphical view]
    PANTHERiPTHR11207. PTHR11207. 1 hit.
    PfamiPF00035. dsrm. 1 hit.
    PF14622. Ribonucleas_3_3. 1 hit.
    PF00636. Ribonuclease_3. 1 hit.
    [Graphical view]
    SMARTiSM00358. DSRM. 1 hit.
    SM00535. RIBOc. 2 hits.
    [Graphical view]
    SUPFAMiSSF69065. SSF69065. 3 hits.
    PROSITEiPS50137. DS_RBD. 1 hit.
    PS00517. RNASE_3_1. 2 hits.
    PS50142. RNASE_3_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5HZJ0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQGNTCHRMS YHPGRGCPRG RGGHGARPSA PAFRPQNLRL LHPQQPPAQY     50
    QYEPPSAPSS SYSNSQAPSF MPPRPDFVPY PPPAAPSAQG PLPPCPVRPP 100
    YPNHQMRHPF PVPPCFPPMP PPMPCPNNPP ASGAPPGQGT FPFMVPPPSM 150
    PHPPPPPVMP QQVNYQYPPG YSHSFPPPGF NSYQNNSSSF PPSANSSSTP 200
    HFRHLPPYSL PKAQNERRSP ERLKHYDDHR HRDHSHGRGE RHRSLERRER 250
    GRSPERRRPE SRYRSDYDRG RTPPPRHRSY ERSRERDRER HRHREARRSP 300
    SLERSYKKEY KRSGRSYALP VAPEPAGCTP ELPGEMIKTT ESWAPPPENV 350
    NHRSPSREKK RARWEEEKDR WSDSQGSGKE KNYTSIKEKE AEEVPPEKTE 400
    EEEEELLKPV WIRCTHSESY YSSDPMDQVG DSTVVGTSRL RDLYDKFEEE 450
    LGNRQEKAKA ARPPWEPPKT KLDEDLESSS ESECETDDDS TCSSSSDSEV 500
    FDVIAEIKRK KAHPDRLHDE LWYNDPGQMN DGPLCKCSAK ARRTGIRHSI 550
    YPGEEAIKPC RPMTNNAGRL FHYRITVSPP TNFLTDRPTV IEYDDHEYIF 600
    EGFSMFAHAP LTNIPLCKVI RFNIDYTIHF IEEMMPENFC VKGLELFSLF 650
    LFRDILELYD WNLKGPLFED SPPCCPRFHF MPRFVRFLPD GGKEVLSMHQ 700
    ILLYLLRCSK ALVPEEEIAN MLQWEELEWQ KYAEECKGMI VTNPGTKPSS 750
    VRIDQLDREQ FNPEVITFPI IVHFGIRPAQ LSYAGDPQYQ KLWKSYVKLR 800
    HLLANSPKVK QTDKQKLAQR EEALQKIRQK NTMRREVTVE LSSQGFWKTG 850
    IRSDVCQHAM MLPVLTHHIR YHQCLMHLDK LIGYTFQDRC LLQLAMTHPS 900
    HHLNFGMNPD HARNSLSNCG IRQPKYGDRK VHHMHMRKKG INTLINIMSR 950
    LGQDDPTPSR INHNERLEFL GDAVVEFLTS VHLYYLFPSL EEGGLATYRT 1000
    AIVQNQHLAM LAKKLELDRF MLYAHGPDLC RESDLRHAMA NCFEALIGAV 1050
    YLEGSLEEAK QLFGRLLFND PDLREVWLNY PLHPLQLQEP NTDRQLIETS 1100
    PVLQKLTEFE EAIGVIFTHV RLLARAFTLR TVGFNHLTLG HNQRMEFLGD 1150
    SIMQLVATEY LFIHFPDHHE GHLTLLRSSL VNNRTQAKVA EELGMQEYAI 1200
    TNDKTKRPVA LRTKTLADLL ESFIAALYID KDLEYVHTFM NVCFFPRLKE 1250
    FILNQDWNDP KSQLQQCCLT LRTEGKEPDI PLYKTLQTVG PSHARTYTVA 1300
    VYFKGERIGC GKGPSIQQAE MGAAMDALEK YNFPQMAHQK RFIERKYRQE 1350
    LKEMRWEREH QEREPEEAED IKK 1373
    Length:1,373
    Mass (Da):158,828
    Last modified:February 15, 2005 - v1
    Checksum:iED1DBEE2FFD89A6B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK144147 mRNA. Translation: BAE25729.1.
    AK148640 mRNA. Translation: BAE28629.1.
    BC088999 mRNA. Translation: AAH88999.1.
    CCDSiCCDS49583.1.
    RefSeqiNP_001123621.1. NM_001130149.1.
    NP_081075.3. NM_026799.3.
    UniGeneiMm.293142.

    Genome annotation databases

    EnsembliENSMUST00000090292; ENSMUSP00000087762; ENSMUSG00000022191.
    ENSMUST00000169061; ENSMUSP00000129279; ENSMUSG00000022191.
    GeneIDi14000.
    KEGGimmu:14000.
    UCSCiuc007via.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK144147 mRNA. Translation: BAE25729.1 .
    AK148640 mRNA. Translation: BAE28629.1 .
    BC088999 mRNA. Translation: AAH88999.1 .
    CCDSi CCDS49583.1.
    RefSeqi NP_001123621.1. NM_001130149.1.
    NP_081075.3. NM_026799.3.
    UniGenei Mm.293142.

    3D structure databases

    ProteinModelPortali Q5HZJ0.
    SMRi Q5HZJ0. Positions 961-1336.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199531. 1 interaction.
    IntActi Q5HZJ0. 1 interaction.
    STRINGi 10090.ENSMUSP00000087762.

    PTM databases

    PhosphoSitei Q5HZJ0.

    Proteomic databases

    PaxDbi Q5HZJ0.
    PRIDEi Q5HZJ0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000090292 ; ENSMUSP00000087762 ; ENSMUSG00000022191 .
    ENSMUST00000169061 ; ENSMUSP00000129279 ; ENSMUSG00000022191 .
    GeneIDi 14000.
    KEGGi mmu:14000.
    UCSCi uc007via.2. mouse.

    Organism-specific databases

    CTDi 29102.
    MGIi MGI:1261425. Drosha.

    Phylogenomic databases

    eggNOGi COG0571.
    GeneTreei ENSGT00730000111052.
    HOGENOMi HOG000122291.
    InParanoidi Q5HZJ0.
    KOi K03685.
    OMAi ESYYSND.
    OrthoDBi EOG773XF7.
    PhylomeDBi Q5HZJ0.
    TreeFami TF314734.

    Enzyme and pathway databases

    Reactomei REACT_221178. MicroRNA (miRNA) biogenesis.

    Miscellaneous databases

    ChiTaRSi DROSHA. mouse.
    NextBioi 284892.
    PROi Q5HZJ0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5HZJ0.
    Bgeei Q5HZJ0.
    Genevestigatori Q5HZJ0.

    Family and domain databases

    Gene3Di 1.10.1520.10. 3 hits.
    3.30.160.20. 1 hit.
    HAMAPi MF_00104. RNase_III.
    InterProi IPR014720. dsRNA-bd_dom.
    IPR011907. RNase_III.
    IPR000999. RNase_III_dom.
    [Graphical view ]
    PANTHERi PTHR11207. PTHR11207. 1 hit.
    Pfami PF00035. dsrm. 1 hit.
    PF14622. Ribonucleas_3_3. 1 hit.
    PF00636. Ribonuclease_3. 1 hit.
    [Graphical view ]
    SMARTi SM00358. DSRM. 1 hit.
    SM00535. RIBOc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF69065. SSF69065. 3 hits.
    PROSITEi PS50137. DS_RBD. 1 hit.
    PS00517. RNASE_3_1. 2 hits.
    PS50142. RNASE_3_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryonic stem cell and Sympathetic ganglion.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Embryonic brain.
    3. "Ars2 links the nuclear cap-binding complex to RNA interference and cell proliferation."
      Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M., Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N., Dreyfuss G., Thompson C.B.
      Cell 138:328-339(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRRT.

    Entry informationi

    Entry nameiRNC_MOUSE
    AccessioniPrimary (citable) accession number: Q5HZJ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3