ARL2

ARL2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesARL2, ARFL2, ADP ribosylation factor like GTPase 2, MRCS1
External IDsOMIM: 601175; MGI: 1928393; HomoloGene: 1260; GeneCards: ARL2; OMA:ARL2 - orthologs
Orthologs
SpeciesHumanMouse
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 MbChr 19: 6.18 – 6.19 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000213465 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024944 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ 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.
  7. ^ a b "Entrez Gene: ARL2 ADP-ribosylation factor-like 2".
  8. ^ 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.
  9. ^ 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.
  10. ^ 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.
  11. ^ 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.
  12. ^ 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.
  13. ^ 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.
  14. ^ 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.

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