Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P70425

- RIT2_MOUSE

UniProt

P70425 - RIT2_MOUSE

Protein

GTP-binding protein Rit2

Gene

Rit2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Binds and exchanges GTP and GDP.

    Enzyme regulationi

    Alternates between an inactive form bound to GDP and an active form bound to GTP.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi27 – 348GTPBy similarity
    Nucleotide bindingi74 – 785GTPBy similarity
    Nucleotide bindingi133 – 1364GTPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. GTP catabolic process Source: InterPro
    2. small GTPase mediated signal transduction Source: InterPro

    Keywords - Ligandi

    Calmodulin-binding, GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTP-binding protein Rit2
    Alternative name(s):
    Ras-like protein expressed in neurons
    Ras-like without CAAX protein 2
    Gene namesi
    Name:Rit2
    Synonyms:Rin, Roc2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:108054. Rit2.

    Subcellular locationi

    Nucleus By similarity. Cell membrane
    Note: Colocalizes with PLXNB3 at the plasma membrane.By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi34 – 341S → N: Dominant negative. Loss of interaction with MLLT4, RLF and RALGDS. 1 Publication
    Mutagenesisi52 – 521T → A: Loss of interaction with MLLT4, RLF and RALGDS; when associated with L-78. 1 Publication
    Mutagenesisi78 – 781Q → L: Constitutively active. Dramatic reduction of the rate of GTP hydrolysis. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 217217GTP-binding protein Rit2PRO_0000082728Add
    BLAST

    Proteomic databases

    PaxDbiP70425.
    PRIDEiP70425.

    Expressioni

    Tissue specificityi

    Neuron-specific.

    Gene expression databases

    ArrayExpressiP70425.
    BgeeiP70425.
    CleanExiMM_RIT2.
    GenevestigatoriP70425.

    Interactioni

    Subunit structurei

    Interacts with PLXNB3 By similarity. Interacts with MLLT4, the C-terminal domain of RALGDS and RLF, but not with RIN1 and PIK3CA. RLF binds exclusively to the active GTP-bound form. Binds calmodulin.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RLFQ131292EBI-2649620,EBI-958266From a different organism.

    Protein-protein interaction databases

    BioGridi202893. 1 interaction.
    IntActiP70425. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP70425.
    SMRiP70425. Positions 33-183.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Ras family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    GeneTreeiENSGT00750000117416.
    HOVERGENiHBG009351.
    InParanoidiP70425.
    KOiK07833.
    OMAiVYKIVIL.
    PhylomeDBiP70425.
    TreeFamiTF315072.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR020849. Small_GTPase_Ras.
    [Graphical view]
    PANTHERiPTHR24070. PTHR24070. 1 hit.
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00173. RAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51421. RAS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P70425-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEVENEAHCC PGSSSGGSRE YKVVMLGAGG VGKSAVTMQF ISHQFPDYHD    50
    PTIEDAYKTQ VRIDNEPAYL DILDTAGQAE FTAMREQYMR GGEGFIICYS 100
    VTDRQSFQEA AKFKELIFQV RHTYEIPLVL VGNKIDLEQF RQVSTEEGMN 150
    LARDYNCAFF ETSAALRFGI DDAFQGLVRE IRRKESMLSL VERKLKRKDS 200
    LWKKIKASLK KKRENML 217
    Length:217
    Mass (Da):24,802
    Last modified:February 1, 1997 - v1
    Checksum:i189AA6DCCE75034F
    GO

    Sequence cautioni

    The sequence BAE23581.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31V → A in AAD13022. (PubMed:10545207)Curated
    Sequence conflicti150 – 1501N → T in AAD13022. (PubMed:10545207)Curated
    Sequence conflicti176 – 1761G → S in BAC32750. (PubMed:16141072)Curated
    Sequence conflicti217 – 2171L → I in AAD13022. (PubMed:10545207)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U71202 mRNA. Translation: AAB42212.1.
    AF084463 mRNA. Translation: AAD13022.1.
    AK040743 mRNA. Translation: BAC30690.1.
    AK046425 mRNA. Translation: BAC32724.1.
    AK046484 mRNA. Translation: BAC32750.1.
    AK138206 mRNA. Translation: BAE23581.1. Different initiation.
    AK139394 mRNA. Translation: BAE23992.1.
    AK140133 mRNA. Translation: BAE24250.1.
    AK140726 mRNA. Translation: BAE24457.1.
    AK162862 mRNA. Translation: BAE37088.1.
    AK162953 mRNA. Translation: BAE37131.1.
    BC018267 mRNA. Translation: AAH18267.1.
    CCDSiCCDS29108.1.
    RefSeqiNP_033091.1. NM_009065.2.
    UniGeneiMm.5163.

    Genome annotation databases

    EnsembliENSMUST00000153060; ENSMUSP00000114323; ENSMUSG00000057455.
    GeneIDi19762.
    KEGGimmu:19762.
    UCSCiuc008ehx.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U71202 mRNA. Translation: AAB42212.1 .
    AF084463 mRNA. Translation: AAD13022.1 .
    AK040743 mRNA. Translation: BAC30690.1 .
    AK046425 mRNA. Translation: BAC32724.1 .
    AK046484 mRNA. Translation: BAC32750.1 .
    AK138206 mRNA. Translation: BAE23581.1 . Different initiation.
    AK139394 mRNA. Translation: BAE23992.1 .
    AK140133 mRNA. Translation: BAE24250.1 .
    AK140726 mRNA. Translation: BAE24457.1 .
    AK162862 mRNA. Translation: BAE37088.1 .
    AK162953 mRNA. Translation: BAE37131.1 .
    BC018267 mRNA. Translation: AAH18267.1 .
    CCDSi CCDS29108.1.
    RefSeqi NP_033091.1. NM_009065.2.
    UniGenei Mm.5163.

    3D structure databases

    ProteinModelPortali P70425.
    SMRi P70425. Positions 33-183.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202893. 1 interaction.
    IntActi P70425. 3 interactions.

    Proteomic databases

    PaxDbi P70425.
    PRIDEi P70425.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000153060 ; ENSMUSP00000114323 ; ENSMUSG00000057455 .
    GeneIDi 19762.
    KEGGi mmu:19762.
    UCSCi uc008ehx.1. mouse.

    Organism-specific databases

    CTDi 6014.
    MGIi MGI:108054. Rit2.

    Phylogenomic databases

    eggNOGi COG1100.
    GeneTreei ENSGT00750000117416.
    HOVERGENi HBG009351.
    InParanoidi P70425.
    KOi K07833.
    OMAi VYKIVIL.
    PhylomeDBi P70425.
    TreeFami TF315072.

    Miscellaneous databases

    ChiTaRSi RIT2. mouse.
    NextBioi 297208.
    PROi P70425.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P70425.
    Bgeei P70425.
    CleanExi MM_RIT2.
    Genevestigatori P70425.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR020849. Small_GTPase_Ras.
    [Graphical view ]
    PANTHERi PTHR24070. PTHR24070. 1 hit.
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00173. RAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51421. RAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rin, a neuron-specific and calmodulin-binding small G-protein, and Rit define a novel subfamily of ras proteins."
      Lee C.H.J., Della N.G., Chew C.E., Zack D.J.
      J. Neurosci. 16:6784-6794(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
      Tissue: Retina.
    2. "Biochemical characterization of the Ras-related GTPases Rit and Rin."
      Shao H., Kadono-Okuda K., Finlin B.S., Andres D.A.
      Arch. Biochem. Biophys. 371:207-219(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INTERACTION WITH MLLT4; RP RALGDS AND RLF, MUTAGENESIS OF SER-34; THR-52 AND GLN-78.
    3. "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: Blood vessel, Brain cortex, Corpora quadrigemina, Corpus striatum, Hypothalamus and Spinal cord.
    4. "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].
      Tissue: Retina.

    Entry informationi

    Entry nameiRIT2_MOUSE
    AccessioniPrimary (citable) accession number: P70425
    Secondary accession number(s): Q3UST1
    , Q3UUP4, Q8BQT5, Q9QWX5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2003
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Shows rapid uncatalyzed guanine nucleotide dissociation rates, which are much faster than those of most Ras subfamily members.

    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