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Q9D0J4 (ARL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ADP-ribosylation factor-like protein 2
Gene names
Name:Arl2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.4 Ref.5

Subcellular location

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.

Tissue specificity

Expressed in brain, lung, cerebellum, liver, kidney, hippocampus, spleen, cortex and heart (at protein level). Ref.4

Post-translational modification

Not N-myristoylated.

Sequence similarities

Belongs to the small GTPase superfamily. Arf family.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Cytoskeleton
Mitochondrion
Nucleus
   LigandGTP-binding
Nucleotide-binding
   PTMIsopeptide bond
Lipoprotein
Myristate
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from sequence or structural similarity. Source: GOC

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

centrosome organization

Inferred from sequence or structural similarity. Source: UniProtKB

maintenance of protein location in nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell-substrate adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of microtubule polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of microtubule polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

tight junction assembly

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

lateral plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial intermembrane space

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGDP binding

Inferred from direct assay Ref.5. Source: UniProtKB

GTP binding

Inferred from direct assay Ref.5. Source: UniProtKB

GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDE6DO439246EBI-1033319,EBI-712685From a different organism.
UNC119Q134322EBI-1033319,EBI-711260From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 184183ADP-ribosylation factor-like protein 2
PRO_0000207454

Regions

Nucleotide binding23 – 308GTP
Nucleotide binding66 – 705GTP
Nucleotide binding125 – 1284GTP

Sites

Binding site681GTP; via amide nitrogen

Amino acid modifications

Lipidation21N-myristoyl glycine Potential
Cross-link71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis301T → L: Reduces affinity to GTP and GDP. Inhibits interaction with PDE6D. Ref.5
Mutagenesis701Q → L: Does not reduce affinity fo GTP and GDP. Enhances interaction with PDE6D. Ref.5
Sequence conflict331L → S in AAD33908. Ref.1

Secondary structure

................................. 184
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9D0J4 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8B3741700BFED3F8

FASTA18420,864
        10         20         30         40         50         60 
MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED VDTISPTLGF NIKTLEHRGF 

        70         80         90        100        110        120 
KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL 

       130        140        150        160        170        180 
LIFANKQDLP GALSCNAIQE ALELDSIRSH HWRIQGCSAV TGEDLLPGID WLLDDISSRV 


FTAD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF143680 mRNA. Translation: AAD33908.1.
AK011366 mRNA. Translation: BAB27572.1.
BC060259 mRNA. Translation: AAH60259.1.
RefSeqNP_062696.2. NM_019722.3.
UniGeneMm.21071.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KSGX-ray2.30A1-184[»]
1KSHX-ray1.80A1-184[»]
1KSJX-ray2.60A1-184[»]
4GOKX-ray2.60A/B17-184[»]
ProteinModelPortalQ9D0J4.
SMRQ9D0J4. Positions 1-179.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207906. 1 interaction.
DIPDIP-36659N.
IntActQ9D0J4. 5 interactions.
MINTMINT-236357.
STRING10090.ENSMUSP00000025893.

PTM databases

PhosphoSiteQ9D0J4.

Proteomic databases

PaxDbQ9D0J4.
PRIDEQ9D0J4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025893; ENSMUSP00000025893; ENSMUSG00000024944.
GeneID56327.
KEGGmmu:56327.
UCSCuc008gho.1. mouse.

Organism-specific databases

CTD402.
MGIMGI:1928393. Arl2.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00750000117257.
HOGENOMHOG000163691.
HOVERGENHBG002073.
InParanoidQ9D0J4.
KOK07943.
OMAEMRILFL.
OrthoDBEOG7M98HG.
PhylomeDBQ9D0J4.
TreeFamTF105462.

Gene expression databases

BgeeQ9D0J4.
CleanExMM_ARL2.
GenevestigatorQ9D0J4.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
PfamPF00025. Arf. 1 hit.
[Graphical view]
PRINTSPR00328. SAR1GTPBP.
SMARTSM00177. ARF. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51417. ARF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARL2. mouse.
EvolutionaryTraceQ9D0J4.
NextBio312306.
PROQ9D0J4.
SOURCESearch...

Entry information

Entry nameARL2_MOUSE
AccessionPrimary (citable) accession number: Q9D0J4
Secondary accession number(s): Q9WUM1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot