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P61588

- RND3_MOUSE

UniProt

P61588 - RND3_MOUSE

Protein

Rho-related GTP-binding protein RhoE

Gene

Rnd3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (24 May 2004)
      Previous versions | rss
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    Functioni

    Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi30 – 378GTPBy similarity
    Nucleotide bindingi77 – 815GTPBy similarity
    Nucleotide bindingi135 – 1384GTPBy similarity

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. small GTPase mediated signal transduction Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho-related GTP-binding protein RhoE
    Alternative name(s):
    Rho family GTPase 3
    Rnd3
    Gene namesi
    Name:Rnd3
    Synonyms:Arhe, Rhoe
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1921444. Rnd3.

    Subcellular locationi

    Golgi apparatus membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 241241Rho-related GTP-binding protein RhoEPRO_0000198879Add
    BLAST
    Propeptidei242 – 2443Removed in mature formBy similarityPRO_0000281231

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei241 – 2411Cysteine methyl esterBy similarity
    Lipidationi241 – 2411S-farnesyl cysteineBy similarity

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    PRIDEiP61588.

    PTM databases

    PhosphoSiteiP61588.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP61588.
    BgeeiP61588.
    CleanExiMM_RND3.
    GenevestigatoriP61588.

    Interactioni

    Subunit structurei

    Interacts with UBXD5 By similarity. Binds ROCK1.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARHGAP5Q130172EBI-6930266,EBI-7237884From a different organism.
    Rock1P703357EBI-6930266,EBI-989293
    YWHABP319465EBI-6930266,EBI-359815From a different organism.
    YWHAEP622582EBI-6930266,EBI-356498From a different organism.
    YWHAGP619812EBI-6930266,EBI-359832From a different organism.
    YWHAHQ049172EBI-6930266,EBI-306940From a different organism.
    YWHAQP273482EBI-6930266,EBI-359854From a different organism.
    YWHAZP631043EBI-6930266,EBI-347088From a different organism.

    Protein-protein interaction databases

    IntActiP61588. 9 interactions.

    Structurei

    Secondary structure

    1
    244
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 319
    Helixi36 – 4510
    Beta strandi56 – 7823
    Helixi82 – 843
    Turni85 – 873
    Helixi88 – 914
    Beta strandi96 – 1038
    Helixi107 – 1159
    Helixi117 – 1248
    Beta strandi129 – 1357
    Helixi137 – 1415
    Helixi143 – 1508
    Turni151 – 1533
    Helixi159 – 16911
    Beta strandi172 – 1765
    Turni179 – 1813
    Helixi183 – 19917

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GWNX-ray2.10A/C16-200[»]
    ProteinModelPortaliP61588.
    SMRiP61588. Positions 22-200.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61588.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi52 – 609Effector regionSequence Analysis

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rho family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    GeneTreeiENSGT00700000104387.
    HOGENOMiHOG000233974.
    HOVERGENiHBG009351.
    InParanoidiP61588.
    KOiK07859.
    OMAiLACINKS.
    OrthoDBiEOG71P2BH.
    PhylomeDBiP61588.
    TreeFamiTF330887.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003578. Small_GTPase_Rho.
    [Graphical view]
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00174. RHO. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51420. RHO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P61588-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKERRASQKL SSKSIMDPNQ NVKCKIVVVG DSQCGKTALL HVFAKDCFPE    50
    NYVPTVFENY TASFEIDTQR IELSLWDTSG SPYYDNVRPL SYPDSDAVLI 100
    CFDISRPETL DSVLKKWKGE IQEFCPNTKM LLVGCKSDLR TDVSTLVELS 150
    NHRQTPVSYD QGANMAKQIG AATYIECSAL QSENSVRDIF HVATLACVNK 200
    TNKNVKRNKS QRATKRISHM PSRPELSAVA TDLRKDKAKS CTVM 244
    Length:244
    Mass (Da):27,368
    Last modified:May 24, 2004 - v1
    Checksum:iDD2D4021CD42BACC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK011442 mRNA. Translation: BAB27622.1.
    AK035195 mRNA. Translation: BAC28975.1.
    BC009002 mRNA. Translation: AAH09002.1.
    CCDSiCCDS16028.1.
    RefSeqiNP_083086.1. NM_028810.2.
    UniGeneiMm.46497.

    Genome annotation databases

    EnsembliENSMUST00000017288; ENSMUSP00000017288; ENSMUSG00000017144.
    GeneIDi74194.
    KEGGimmu:74194.
    UCSCiuc008jqf.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK011442 mRNA. Translation: BAB27622.1 .
    AK035195 mRNA. Translation: BAC28975.1 .
    BC009002 mRNA. Translation: AAH09002.1 .
    CCDSi CCDS16028.1.
    RefSeqi NP_083086.1. NM_028810.2.
    UniGenei Mm.46497.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GWN X-ray 2.10 A/C 16-200 [» ]
    ProteinModelPortali P61588.
    SMRi P61588. Positions 22-200.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P61588. 9 interactions.

    PTM databases

    PhosphoSitei P61588.

    Proteomic databases

    PRIDEi P61588.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000017288 ; ENSMUSP00000017288 ; ENSMUSG00000017144 .
    GeneIDi 74194.
    KEGGi mmu:74194.
    UCSCi uc008jqf.1. mouse.

    Organism-specific databases

    CTDi 390.
    MGIi MGI:1921444. Rnd3.

    Phylogenomic databases

    eggNOGi COG1100.
    GeneTreei ENSGT00700000104387.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    InParanoidi P61588.
    KOi K07859.
    OMAi LACINKS.
    OrthoDBi EOG71P2BH.
    PhylomeDBi P61588.
    TreeFami TF330887.

    Miscellaneous databases

    EvolutionaryTracei P61588.
    NextBioi 1627.
    PROi P61588.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61588.
    Bgeei P61588.
    CleanExi MM_RND3.
    Genevestigatori P61588.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003578. Small_GTPase_Rho.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00174. RHO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51420. RHO. 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.
    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].
    3. "RhoE binds to ROCK I and inhibits downstream signaling."
      Riento K., Guasch R.M., Garg R., Jin B., Ridley A.J.
      Mol. Cell. Biol. 23:4219-4229(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROCK1, SUBCELLULAR LOCATION.
    4. "Crystal structure of the core domain of RhoE/Rnd3: a constitutively activated small G protein."
      Garavini H., Riento K., Phelan J.P., McAlister M.S., Ridley A.J., Keep N.H.
      Biochemistry 41:6303-6310(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 14-200.

    Entry informationi

    Entry nameiRND3_MOUSE
    AccessioniPrimary (citable) accession number: P61588
    Secondary accession number(s): P52199, Q6ZWS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: May 24, 2004
    Last modified: October 1, 2014
    This is version 106 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

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3