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Q9D0J4

- ARL2_MOUSE

UniProt

Q9D0J4 - ARL2_MOUSE

Protein

ADP-ribosylation factor-like protein 2

Gene

Arl2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca2+-dependent release of acetylcholine. Required for normal progress through the cell cycle.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei68 – 681GTP; via amide nitrogen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi23 – 308GTP1 Publication
    Nucleotide bindingi66 – 705GTP1 Publication
    Nucleotide bindingi125 – 1284GTP1 Publication

    GO - Molecular functioni

    1. GDP binding Source: UniProtKB
    2. GTPase activity Source: UniProtKB
    3. GTP binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. centrosome organization Source: UniProtKB
    3. GTP catabolic process Source: GOC
    4. maintenance of protein location in nucleus Source: UniProtKB
    5. negative regulation of GTPase activity Source: UniProtKB
    6. positive regulation of cell-substrate adhesion Source: UniProtKB
    7. positive regulation of microtubule polymerization Source: UniProtKB
    8. regulation of microtubule polymerization Source: UniProtKB
    9. small GTPase mediated signal transduction Source: InterPro
    10. tight junction assembly Source: UniProtKB

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ADP-ribosylation factor-like protein 2
    Gene namesi
    Name:Arl2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1928393. Arl2.

    Subcellular locationi

    Mitochondrion intermembrane space. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Nucleus. Cytoplasm
    Note: The complex formed with ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules By similarity. The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria.By similarity

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. lateral plasma membrane Source: UniProtKB
    4. mitochondrial intermembrane space Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi30 – 301T → L: Reduces affinity to GTP and GDP. Inhibits interaction with PDE6D. 1 Publication
    Mutagenesisi70 – 701Q → L: Does not reduce affinity fo GTP and GDP. Enhances interaction with PDE6D. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedSequence Analysis
    Chaini2 – 184183ADP-ribosylation factor-like protein 2PRO_0000207454Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineSequence Analysis
    Cross-linki71 – 71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Not N-myristoylated.

    Keywords - PTMi

    Isopeptide bond, Lipoprotein, Myristate, Ubl conjugation

    Proteomic databases

    MaxQBiQ9D0J4.
    PaxDbiQ9D0J4.
    PRIDEiQ9D0J4.

    PTM databases

    PhosphoSiteiQ9D0J4.

    Expressioni

    Tissue specificityi

    Expressed in brain, lung, cerebellum, liver, kidney, hippocampus, spleen, cortex and heart (at protein level).1 Publication

    Gene expression databases

    BgeeiQ9D0J4.
    CleanExiMM_ARL2.
    GenevestigatoriQ9D0J4.

    Interactioni

    Subunit structurei

    Found in a complex with ARL2, ARL2BP and SLC25A6. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with ELMOD2. The GTP-bound form interacts with ARL2BP. Interacts with TBCD; the GDP-bound form interacts preferentially with TBCD. Interacts with UNC119 By similarity. Found in a complex with ARL2, ARL2BP and SLC25A4. The GTP-bound form interacts with PDE6D.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDE6DO439246EBI-1033319,EBI-712685From a different organism.
    UNC119Q134322EBI-1033319,EBI-711260From a different organism.

    Protein-protein interaction databases

    BioGridi207906. 2 interactions.
    DIPiDIP-36659N.
    IntActiQ9D0J4. 5 interactions.
    MINTiMINT-236357.
    STRINGi10090.ENSMUSP00000025893.

    Structurei

    Secondary structure

    1
    184
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 1211
    Beta strandi17 – 226
    Helixi29 – 368
    Beta strandi48 – 5710
    Beta strandi60 – 678
    Helixi71 – 744
    Helixi75 – 806
    Beta strandi85 – 928
    Helixi96 – 983
    Helixi99 – 11012
    Helixi113 – 1153
    Beta strandi119 – 1257
    Helixi135 – 1417
    Helixi144 – 1463
    Beta strandi152 – 1565
    Turni159 – 1613
    Helixi165 – 17713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KSGX-ray2.30A1-184[»]
    1KSHX-ray1.80A1-184[»]
    1KSJX-ray2.60A1-184[»]
    4GOKX-ray2.60A/B17-184[»]
    ProteinModelPortaliQ9D0J4.
    SMRiQ9D0J4. Positions 1-179.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9D0J4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Arf family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    GeneTreeiENSGT00750000117257.
    HOGENOMiHOG000163691.
    HOVERGENiHBG002073.
    InParanoidiQ9D0J4.
    KOiK07943.
    OMAiEMRILFL.
    OrthoDBiEOG7M98HG.
    PhylomeDBiQ9D0J4.
    TreeFamiTF105462.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR024156. Small_GTPase_ARF.
    IPR006689. Small_GTPase_ARF/SAR.
    [Graphical view]
    PfamiPF00025. Arf. 1 hit.
    [Graphical view]
    PRINTSiPR00328. SAR1GTPBP.
    SMARTiSM00177. ARF. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51417. ARF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9D0J4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED VDTISPTLGF    50
    NIKTLEHRGF KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ 100
    DCQRELQSLL VEERLAGATL LIFANKQDLP GALSCNAIQE ALELDSIRSH 150
    HWRIQGCSAV TGEDLLPGID WLLDDISSRV FTAD 184
    Length:184
    Mass (Da):20,864
    Last modified:June 1, 2001 - v1
    Checksum:i8B3741700BFED3F8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331L → S in AAD33908. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF143680 mRNA. Translation: AAD33908.1.
    AK011366 mRNA. Translation: BAB27572.1.
    BC060259 mRNA. Translation: AAH60259.1.
    CCDSiCCDS29496.1.
    RefSeqiNP_062696.2. NM_019722.3.
    UniGeneiMm.21071.

    Genome annotation databases

    EnsembliENSMUST00000025893; ENSMUSP00000025893; ENSMUSG00000024944.
    GeneIDi56327.
    KEGGimmu:56327.
    UCSCiuc008gho.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF143680 mRNA. Translation: AAD33908.1 .
    AK011366 mRNA. Translation: BAB27572.1 .
    BC060259 mRNA. Translation: AAH60259.1 .
    CCDSi CCDS29496.1.
    RefSeqi NP_062696.2. NM_019722.3.
    UniGenei Mm.21071.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KSG X-ray 2.30 A 1-184 [» ]
    1KSH X-ray 1.80 A 1-184 [» ]
    1KSJ X-ray 2.60 A 1-184 [» ]
    4GOK X-ray 2.60 A/B 17-184 [» ]
    ProteinModelPortali Q9D0J4.
    SMRi Q9D0J4. Positions 1-179.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207906. 2 interactions.
    DIPi DIP-36659N.
    IntActi Q9D0J4. 5 interactions.
    MINTi MINT-236357.
    STRINGi 10090.ENSMUSP00000025893.

    PTM databases

    PhosphoSitei Q9D0J4.

    Proteomic databases

    MaxQBi Q9D0J4.
    PaxDbi Q9D0J4.
    PRIDEi Q9D0J4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025893 ; ENSMUSP00000025893 ; ENSMUSG00000024944 .
    GeneIDi 56327.
    KEGGi mmu:56327.
    UCSCi uc008gho.1. mouse.

    Organism-specific databases

    CTDi 402.
    MGIi MGI:1928393. Arl2.

    Phylogenomic databases

    eggNOGi COG1100.
    GeneTreei ENSGT00750000117257.
    HOGENOMi HOG000163691.
    HOVERGENi HBG002073.
    InParanoidi Q9D0J4.
    KOi K07943.
    OMAi EMRILFL.
    OrthoDBi EOG7M98HG.
    PhylomeDBi Q9D0J4.
    TreeFami TF105462.

    Miscellaneous databases

    ChiTaRSi ARL2. mouse.
    EvolutionaryTracei Q9D0J4.
    NextBioi 312306.
    PROi Q9D0J4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9D0J4.
    CleanExi MM_ARL2.
    Genevestigatori Q9D0J4.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR024156. Small_GTPase_ARF.
    IPR006689. Small_GTPase_ARF/SAR.
    [Graphical view ]
    Pfami PF00025. Arf. 1 hit.
    [Graphical view ]
    PRINTSi PR00328. SAR1GTPBP.
    SMARTi SM00177. ARF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51417. ARF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of Mus musculus arf like protein 2 (ARL2)."
      Linari M., Hanzal-Bayer M., Becker J.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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.
    3. "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: Brain.
    4. "ARL2 and BART enter mitochondria and bind the adenine nucleotide transporter."
      Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A.
      Mol. Biol. Cell 13:71-83(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH SLC25A4 AND ARL2BP, TISSUE SPECIFICITY.
    5. "Properties of the interaction of Arf-like protein 2 with PDEdelta."
      Hanzal-Bayer M., Linari M., Wittinghofer A.
      J. Mol. Biol. 350:1074-1082(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDE6D, GTP/GDP-BINDING, MUTAGENESIS OF THR-30 AND GLN-70.
    6. "The complex of Arl2-GTP and PDE delta: from structure to function."
      Hanzal-Bayer M., Renault L., Roversi P., Wittinghofer A., Hillig R.C.
      EMBO J. 21:2095-2106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH HUMAN PDE6D AND GTP.

    Entry informationi

    Entry nameiARL2_MOUSE
    AccessioniPrimary (citable) accession number: Q9D0J4
    Secondary accession number(s): Q9WUM1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 116 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