SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9D0J4

- ARL2_MOUSE

UniProt

Q9D0J4 - ARL2_MOUSE

(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)

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

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 nitrogen

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. cell cycle Source: UniProtKB-KW
  3. centrosome organization Source: UniProtKB
  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
Complete GO annotation...

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.

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
Complete GO annotation...

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 – 11Removed Reviewed prediction
Chaini2 – 184183ADP-ribosylation factor-like protein 2
PRO_0000207454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine Reviewed prediction
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.2 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

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.

Miscellaneous databases

EvolutionaryTraceiQ9D0J4.

Family & Domainsi

Sequence similaritiesi

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

Sequence conflict

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

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 115 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

Similar proteinsi