Q9D0J4 (ARL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ADP-ribosylation factor-like protein 2

Gene names

Name:

Arl2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	184 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › centrosome. 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 process	Cell cycle
Cellular component	Cytoplasm Cytoskeleton Mitochondrion Nucleus
Ligand	GTP-binding Nucleotide-binding
PTM	Isopeptide bond Lipoprotein Myristate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro tight junction assembly Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	centrosome 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_function	GDP 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
PDE6D	O43924	3	EBI-1033319,EBI-712685	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 184

184

ADP-ribosylation factor-like protein 2

PRO_0000207454

Regions

Nucleotide binding

23 – 30

8

GTP

Nucleotide binding

66 – 70

5

GTP

Nucleotide binding

125 – 128

4

GTP

Sites

Binding site

68

1

GTP; via amide nitrogen

Amino acid modifications

Modified residue

45

1

Phosphoserine By similarity

Lipidation

2

1

N-myristoyl glycine Potential

Cross-link

71

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis

30

1

T → L: Reduces affinity to GTP and GDP. Inhibits interaction with PDE6D. Ref.5

Mutagenesis

70

1

Q → L: Does not reduce affinity fo GTP and GDP. Enhances interaction with PDE6D. Ref.5

Sequence conflict

33

1

L → S in AAD33908. Ref.1

Secondary structure

1

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184

Helix Strand Turn

Details...

Helix

2 – 12

11

Beta strand

17 – 22

6

Helix

29 – 36

8

Beta strand

48 – 57

10

Beta strand

60 – 67

8

Helix

71 – 74

4

Helix

75 – 80

6

Beta strand

85 – 92

8

Helix

96 – 98

3

Helix

99 – 110

12

Helix

113 – 115

3

Beta strand

119 – 125

7

Helix

135 – 141

7

Helix

144 – 146

3

Beta strand

152 – 156

5

Turn

159 – 161

3

Helix

165 – 177

13

Sequences

	Sequence		Length	Mass (Da)
	Q9D0J4 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 8B3741700BFED3F8	FASTA	184	20,864
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00315504.

RefSeq

NP_062696.2. NM_019722.3.

UniGene

Mm.21071.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9D0J4.

SMR

Q9D0J4. Positions 1-179.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36659N.

IntAct

Q9D0J4. 1 interaction.

MINT

MINT-236357.

STRING

10090.ENSMUSP00000025893.

PTM databases

PhosphoSite

Q9D0J4.

Proteomic databases

PaxDb

Q9D0J4.

PRIDE

Q9D0J4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000025893; ENSMUSP00000025893; ENSMUSG00000024944.

GeneID

56327.

KEGG

mmu:56327.

UCSC

uc008gho.1. mouse.

Organism-specific databases

CTD

402.

MGI

MGI:1928393. Arl2.

Phylogenomic databases

eggNOG

COG1100.

GeneTree

ENSGT00700000104039.

HOGENOM

HOG000163691.

HOVERGEN

HBG002073.

InParanoid

Q9D0J4.

KO

K07943.

OMA

RNYFECT.

OrthoDB

EOG4K0QPF.

Gene expression databases

Bgee

Q9D0J4.

CleanEx

MM_ARL2.

Genevestigator

Q9D0J4.

GermOnline

ENSMUSG00000024944. Mus musculus.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]

Pfam

PF00025. Arf. 1 hit.
[Graphical view]

PRINTS

PR00328. SAR1GTPBP.

SMART

SM00177. ARF. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51417. ARF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ARL2. mouse.

EvolutionaryTrace

Q9D0J4.

NextBio

312306.

SOURCE

Search...

Entry information

Entry name

ARL2_MOUSE

Accession

Primary (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 3, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program