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Q9CQ01

- RNT2_MOUSE

UniProt

Q9CQ01 - RNT2_MOUSE

Protein

Ribonuclease T2

Gene

Rnaset2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Has ribonuclease activity, with higher activity at acidic pH. May play a role in cellular RNA catabolism. Probably is involved in lysosomal degradation of ribosomal RNA By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei69 – 691By similarity
    Active sitei118 – 1181By similarity
    Active sitei122 – 1221By similarity

    GO - Molecular functioni

    1. ribonuclease activity Source: UniProtKB
    2. ribonuclease T2 activity Source: InterPro
    3. RNA binding Source: InterPro

    GO - Biological processi

    1. RNA catabolic process Source: UniProtKB
    2. RNA phosphodiester bond hydrolysis Source: GOC

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease T2 (EC:3.1.27.-)
    Alternative name(s):
    Ribonuclease 6
    Gene namesi
    Name:Rnaset2
    Synonyms:Rnase6pl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1915445. Rnaset2.

    Subcellular locationi

    Secreted By similarity. Endoplasmic reticulum lumen By similarity. Lysosome lumen By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB
    2. extracellular space Source: UniProtKB
    3. lysosomal lumen Source: UniProtKB-SubCell
    4. lysosome Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Lysosome, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 259230Ribonuclease T2PRO_0000030988Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi53 ↔ 59By similarity
    Disulfide bondi79 ↔ 125By similarity
    Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi188 ↔ 244By similarity
    Disulfide bondi206 ↔ 217By similarity
    Glycosylationi216 – 2161N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9CQ01.
    PaxDbiQ9CQ01.
    PRIDEiQ9CQ01.

    PTM databases

    PhosphoSiteiQ9CQ01.

    Expressioni

    Gene expression databases

    BgeeiQ9CQ01.
    GenevestigatoriQ9CQ01.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000086519.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CQ01.
    SMRiQ9CQ01. Positions 39-254.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RNase T2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG285082.
    GeneTreeiENSGT00640000091563.
    HOGENOMiHOG000059657.
    HOVERGENiHBG050037.
    InParanoidiQ9CQ01.
    KOiK01166.
    OMAiILTHHWP.
    OrthoDBiEOG789CC3.
    PhylomeDBiQ9CQ01.
    TreeFamiTF315063.

    Family and domain databases

    Gene3Di3.90.730.10. 1 hit.
    InterProiIPR001568. RNase_T2-like.
    IPR018188. RNase_T2_AS.
    [Graphical view]
    PANTHERiPTHR11240. PTHR11240. 1 hit.
    PfamiPF00445. Ribonuclease_T2. 1 hit.
    [Graphical view]
    SUPFAMiSSF55895. SSF55895. 1 hit.
    PROSITEiPS00530. RNASE_T2_1. 1 hit.
    PS00531. RNASE_T2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9CQ01-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPAEARGAL PGWISVLGWG LALCSLCGAG PLWSGSHEWK KLILTQHWPP    50
    TVCKEVNSCQ DSLDYWTIHG LWPDRAEDCN QSWHFNLDEI KDLLRDMKIY 100
    WPDVIHRSSN RSQFWKHEWV KHGTCAAQVD ALNSEKKYFG KSLDLYKQID 150
    LNSVLQKFGI KPSINYYQLA DFKDALTRIY GVVPKIQCLM PEQGESVQTV 200
    GQIELCFTKE DLHLRNCTEP GEQLSSRQEA WLAMEASTHG MMVCEDGPIF 250
    YPPPTKTQH 259
    Length:259
    Mass (Da):29,609
    Last modified:June 1, 2001 - v1
    Checksum:iE0A1C1BBBEAA5033
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK018722 mRNA. Translation: BAB31368.1.
    AK019234 mRNA. Translation: BAB31616.1.
    AK029149 mRNA. Translation: BAC26326.1.
    BC031496 mRNA. Translation: AAH31496.1.
    CCDSiCCDS37433.1.
    RefSeqiNP_001077407.1. NM_001083938.2.
    NP_080887.1. NM_026611.2.
    UniGeneiMm.181237.
    Mm.426736.

    Genome annotation databases

    EnsembliENSMUST00000089119; ENSMUSP00000086519; ENSMUSG00000094724.
    ENSMUST00000097420; ENSMUSP00000095031; ENSMUSG00000095687.
    ENSMUST00000179728; ENSMUSP00000137303; ENSMUSG00000094724.
    GeneIDi100037283.
    68195.
    KEGGimmu:100037283.
    mmu:68195.
    UCSCiuc008aic.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK018722 mRNA. Translation: BAB31368.1 .
    AK019234 mRNA. Translation: BAB31616.1 .
    AK029149 mRNA. Translation: BAC26326.1 .
    BC031496 mRNA. Translation: AAH31496.1 .
    CCDSi CCDS37433.1.
    RefSeqi NP_001077407.1. NM_001083938.2.
    NP_080887.1. NM_026611.2.
    UniGenei Mm.181237.
    Mm.426736.

    3D structure databases

    ProteinModelPortali Q9CQ01.
    SMRi Q9CQ01. Positions 39-254.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000086519.

    PTM databases

    PhosphoSitei Q9CQ01.

    Proteomic databases

    MaxQBi Q9CQ01.
    PaxDbi Q9CQ01.
    PRIDEi Q9CQ01.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000089119 ; ENSMUSP00000086519 ; ENSMUSG00000094724 .
    ENSMUST00000097420 ; ENSMUSP00000095031 ; ENSMUSG00000095687 .
    ENSMUST00000179728 ; ENSMUSP00000137303 ; ENSMUSG00000094724 .
    GeneIDi 100037283.
    68195.
    KEGGi mmu:100037283.
    mmu:68195.
    UCSCi uc008aic.1. mouse.

    Organism-specific databases

    CTDi 100037283.
    68195.
    MGIi MGI:1915445. Rnaset2.

    Phylogenomic databases

    eggNOGi NOG285082.
    GeneTreei ENSGT00640000091563.
    HOGENOMi HOG000059657.
    HOVERGENi HBG050037.
    InParanoidi Q9CQ01.
    KOi K01166.
    OMAi ILTHHWP.
    OrthoDBi EOG789CC3.
    PhylomeDBi Q9CQ01.
    TreeFami TF315063.

    Miscellaneous databases

    NextBioi 326674.
    PROi Q9CQ01.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CQ01.
    Genevestigatori Q9CQ01.

    Family and domain databases

    Gene3Di 3.90.730.10. 1 hit.
    InterProi IPR001568. RNase_T2-like.
    IPR018188. RNase_T2_AS.
    [Graphical view ]
    PANTHERi PTHR11240. PTHR11240. 1 hit.
    Pfami PF00445. Ribonuclease_T2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55895. SSF55895. 1 hit.
    PROSITEi PS00530. RNASE_T2_1. 1 hit.
    PS00531. RNASE_T2_2. 1 hit.
    [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: Embryo, Kidney and Skin.
    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: FVB/N.
      Tissue: Mammary gland.

    Entry informationi

    Entry nameiRNT2_MOUSE
    AccessioniPrimary (citable) accession number: Q9CQ01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 102 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