ARL2

Protein-coding gene in the species Homo sapiens

ARL2

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
3DOE, 3DOF

Identifiers

Aliases

ARL2, ARFL2, ADP ribosylation factor like GTPase 2, MRCS1

External IDs

OMIM: 601175; MGI: 1928393; HomoloGene: 1260; GeneCards: ARL2; OMA:ARL2 - orthologs

Gene location (Human)

Chr.	Chromosome 11 (human)^[1]

Band	11q13.1	Start	65,014,160 bp^[1]
Band	11q13.1	End	65,022,184 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 19 (mouse)^[2]

Band	19\|19 A	Start	6,184,404 bp^[2]
Band	19\|19 A	End	6,191,578 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

C1 segment

nucleus accumbens

apex of heart

caudate nucleus

putamen

tibial nerve

right frontal lobe

left coronary artery

ascending aorta

right auricle

Top expressed in

muscle of thigh

right ventricle

yolk sac

superior frontal gyrus

dentate gyrus of hippocampal formation granule cell

right kidney

saccule

primary visual cortex

otic placode

otic vesicle

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	nucleotide binding GTP binding GTPase inhibitor activity protein binding GTPase activity GDP binding
Cellular component	cytoplasm centrosome lateral plasma membrane mitochondrial intermembrane space intracellular anatomical structure microtubule organizing center mitochondrial matrix mitochondrion cytoskeleton nucleus nucleolus Golgi apparatus cytosol focal adhesion cilium microtubule cytoskeleton
Biological process	tubulin complex assembly regulation of insulin secretion negative regulation of GTPase activity regulation of microtubule polymerization bicellular tight junction assembly positive regulation of microtubule polymerization cell cycle maintenance of protein location in nucleus positive regulation of cell-substrate adhesion centrosome cycle
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


402


56327

Ensembl


ENSG00000213465


ENSMUSG00000024944

UniProt


P36404


Q9D0J4

RefSeq (mRNA)


NM_001667 NM_001199745


NM_019722

RefSeq (protein)


NP_001186674 NP_001658


NP_062696

Location (UCSC)

Chr 11: 65.01 – 65.02 Mb

Chr 19: 6.18 – 6.19 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

ADP-ribosylation factor-like protein 2 is a protein that in humans is encoded by the ARL2 gene.^[5]^[6]^[7]

Function

The ADP-ribosylation factor (ARF) genes are small GTP-binding proteins of the RAS superfamily. ARL2 is a member of a functionally distinct group of ARF-like genes.^[7]
In photoreceptors, ARL2 participates in the trafficking of lipidated membrane-associated proteins.^[8]
There is an evidence that increased activity of ARL2 protein is strongly correlated with increased mitochondria fusion, while loss of ARL2 activity results in a decreased rate of fusion.^[9]

Interactions

ARL2 has been shown to interact with Protein unc-119 homolog,^[10] TBCD^[11]^[12] and PDE6D.^[13]^[14]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000213465 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000024944 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Clark J, Moore L, Krasinskas A, Way J, Battey J, Tamkun J, Kahn RA (November 1993). "Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: cloning of additional human and Drosophila ARF-like genes". Proc. Natl. Acad. Sci. U.S.A. 90 (19): 8952–6. Bibcode:1993PNAS...90.8952C. doi:10.1073/pnas.90.19.8952. PMC 47479. PMID 8415637.
^ Guru SC, Agarwal SK, Manickam P, Olufemi SE, Crabtree JS, Weisemann JM, Kester MB, Kim YS, Wang Y, Emmert-Buck MR, Liotta LA, Spiegel AM, Boguski MS, Roe BA, Collins FS, Marx SJ, Burns L, Chandrasekharappa SC (September 1997). "A transcript map for the 2.8-Mb region containing the multiple endocrine neoplasia type 1 locus". Genome Res. 7 (7): 725–35. doi:10.1101/gr.7.7.725. PMC 310681. PMID 9253601.
^ ^a ^b "Entrez Gene: ARL2 ADP-ribosylation factor-like 2".
^ Hanke-Gogokhia, C.; Zhang, H.; Frederick, J. M.; Baehr, W. (2016). "The Function of Arf-like Proteins ARL2 and ARL3 in Photoreceptors". Retinal Degenerative Diseases. Advances in Experimental Medicine and Biology. Vol. 854. pp. 655–661. doi:10.1007/978-3-319-17121-0_87. ISBN 978-3-319-17120-3. PMID 26427472.
^ Newman, L. E.; Schiavon, C. R.; Turn, R. E.; Kahn, R. A. (2017). "The ARL2 GTPase regulates mitochondrial fusion from the intermembrane space". Cellular Logistics. 7 (3): e1340104. doi:10.1080/21592799.2017.1340104. PMC 5602422. PMID 28944094.
^ Kobayashi A, Kubota S, Mori N, McLaren MJ, Inana G (January 2003). "Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain". FEBS Lett. 534 (1–3): 26–32. Bibcode:2003FEBSL.534...26K. doi:10.1016/S0014-5793(02)03766-3. PMID 12527357. S2CID 22603052.
^ Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA (October 2003). "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. doi:10.1074/jbc.M308678200. PMID 12912990.
^ Bhamidipati A, Lewis SA, Cowan NJ (May 2000). "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. doi:10.1083/jcb.149.5.1087. PMC 2174823. PMID 10831612.
^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
^ Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (May 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". EMBO J. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981. PMID 11980706.

External links

Human ARL2 genome location and ARL2 gene details page in the UCSC Genome Browser.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Bhamidipati A, Lewis SA, Cowan NJ (2000). "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. doi:10.1083/jcb.149.5.1087. PMC 2174823. PMID 10831612.
Sharer JD, Shern JF, Van Valkenburgh H, Wallace DC, Kahn RA (2002). "ARL2 and BART enter mitochondria and bind the adenine nucleotide transporter". Mol. Biol. Cell. 13 (1): 71–83. doi:10.1091/mbc.01-05-0245. PMC 65073. PMID 11809823.
Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (2002). "The complex of Arl2-GTP and PDE delta: from structure to function". EMBO J. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981. PMID 11980706.
Antoshechkin I, Han M (2002). "The C. elegans evl-20 gene is a homolog of the small GTPase ARL2 and regulates cytoskeleton dynamics during cytokinesis and morphogenesis". Dev. Cell. 2 (5): 579–91. doi:10.1016/S1534-5807(02)00146-6. PMID 12015966.
Kobayashi A, Kubota S, Mori N, McLaren MJ, Inana G (2003). "Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain". FEBS Lett. 534 (1–3): 26–32. Bibcode:2003FEBSL.534...26K. doi:10.1016/S0014-5793(02)03766-3. PMID 12527357. S2CID 22603052.
Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA (2003). "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. doi:10.1074/jbc.M308678200. PMID 12912990.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Zhou C, Cunningham L, Marcus AI, Li Y, Kahn RA (2006). "Arl2 and Arl3 regulate different microtubule-dependent processes". Mol. Biol. Cell. 17 (5): 2476–87. doi:10.1091/mbc.E05-10-0929. PMC 1446103. PMID 16525022.
Beghin A, Honore S, Messana C, Matera EL, Aim J, Burlinchon S, Braguer D, Dumontet C (2007). "ADP ribosylation factor like 2 (Arl2) protein influences microtubule dynamics in breast cancer cells". Exp. Cell Res. 313 (3): 473–85. doi:10.1016/j.yexcr.2006.10.024. PMID 17188265.