ARL3

Protein-coding gene in the species Homo sapiens

ARL3

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1FZQ, 3BH6, 3BH7, 4GOJ

Identifiers

Aliases

ARL3, ARFL3, ADP ribosylation factor like GTPase 3, JBTS35, RP83

External IDs

OMIM: 604695; MGI: 1929699; HomoloGene: 48276; GeneCards: ARL3; OMA:ARL3 - orthologs

Gene location (Human)

Chr.	Chromosome 10 (human)^[1]

Band	10q24.32	Start	102,673,731 bp^[1]
Band	10q24.32	End	102,714,397 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 19 (mouse)^[2]

Band	19\|19 C3	Start	46,519,535 bp^[2]
Band	19\|19 C3	End	46,561,637 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

bronchial epithelial cell

mucosa of paranasal sinus

palpebral conjunctiva

retinal pigment epithelium

pons

Pars compacta

pars reticulata

tibia

epithelium of nasopharynx

external globus pallidus

Top expressed in

neural layer of retina

Epithelium of choroid plexus

epithelium of lens

retinal pigment epithelium

motor neuron

medullary collecting duct

fossa

substantia nigra

Rostral migratory stream

olfactory epithelium

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	nucleotide binding GDP binding microtubule binding GTP binding metal ion binding protein binding GTPase activity magnesium ion binding GTPase activating protein binding
Cellular component	cytoplasm centrosome Golgi apparatus cell projection membrane Golgi membrane spindle intracellular anatomical structure photoreceptor connecting cilium microtubule organizing center midbody spindle microtubule cytoplasmic microtubule extracellular exosome cytoskeleton nucleus cilium microtubule cytoskeleton
Biological process	cilium assembly kidney development intraciliary transport small GTPase mediated signal transduction photoreceptor cell development post-Golgi vesicle-mediated transport cell division protein transport cell cycle smoothened signaling pathway transport mitotic cytokinesis Golgi to plasma membrane transport protein localization to cilium protein localization to ciliary membrane
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


403


56350

Ensembl


ENSG00000138175


ENSMUSG00000025035

UniProt


P36405


Q9WUL7

RefSeq (mRNA)


NM_004311


NM_019718 NM_001355233

RefSeq (protein)


NP_004302


NP_062692 NP_001342162

Location (UCSC)

Chr 10: 102.67 – 102.71 Mb

Chr 19: 46.52 – 46.56 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

ADP-ribosylation factor-like protein 3 is a protein that in humans is encoded by the ARL3 gene.^[5]^[6]^[7]

Function

ADP-ribosylation factor-like 3 is a member of the ADP-ribosylation factor family of GTP-binding proteins. ARL3 binds guanine nucleotides but lacks ADP-ribosylation factor activity.^[7]

Interactions

ARL3 has been shown to interact with Protein unc-119 homolog.^[8]^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000138175 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025035 – 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.
^ Cavenagh MM, Breiner M, Schurmann A, Rosenwald AG, Terui T, Zhang C, Randazzo PA, Adams M, Joost HG, Kahn RA (August 1994). "ADP-ribosylation factor (ARF)-like 3, a new member of the ARF family of GTP-binding proteins cloned from human and rat tissues". J. Biol. Chem. 269 (29): 18937–42. doi:10.1016/S0021-9258(17)32257-3. PMID 8034651.
^ Kim HS (1998). "Assignment of the human ADP-ribosylation factor-like 3 (ARL3) gene to chromosome 10 band q23.3 by radiation hybrid mapping". Cytogenet. Cell Genet. 83 (3–4): 246. doi:10.1159/000015194. PMID 10072593. S2CID 35440803.
^ ^a ^b "Entrez Gene: ARL3 ADP-ribosylation factor-like 3".
^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
^ Van Valkenburgh H, Shern JF, Sharer JD, Zhu X, Kahn RA (June 2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins". J. Biol. Chem. 276 (25): 22826–37. doi:10.1074/jbc.M102359200. PMID 11303027.

External links

Human ARL3 genome location and ARL3 gene details page in the UCSC Genome Browser.

Adams MD, Kerlavage AR, Fleischmann RD, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O (1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence" (PDF). Nature. 377 (6547 Suppl): 3–174. PMID 7566098.
Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
Linari M, Hanzal-Bayer M, Becker J (1999). "The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner". FEBS Lett. 458 (1): 55–9. doi:10.1016/S0014-5793(99)01117-5. PMID 10518933. S2CID 23460401.
Hillig RC, Hanzal-Bayer M, Linari M, Becker J, Wittinghofer A, Renault L (2000). "Structural and biochemical properties show ARL3-GDP as a distinct GTP binding protein". Structure. 8 (12): 1239–45. doi:10.1016/S0969-2126(00)00531-1. PMID 11188688.
Bartolini F, Bhamidipati A, Thomas S, Schwahn U, Lewis SA, Cowan NJ (2002). "Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C". J. Biol. Chem. 277 (17): 14629–34. doi:10.1074/jbc.M200128200. PMID 11847227.
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.
Wistow G, Bernstein SL, Wyatt MK, Ray S, Behal A, Touchman JW, Bouffard G, Smith D, Peterson K (2002). "Expressed sequence tag analysis of human retina for the NEIBank Project: retbindin, an abundant, novel retinal cDNA and alternative splicing of other retina-preferred gene transcripts". Mol. Vis. 8: 196–204. PMID 12107411.
Grayson C, Bartolini F, Chapple JP, Willison KR, Bhamidipati A, Lewis SA, Luthert PJ, Hardcastle AJ, Cowan NJ, Cheetham ME (2002). "Localization in the human retina of the X-linked retinitis pigmentosa protein RP2, its homologue cofactor C and the RP2 interacting protein Arl3". Hum. Mol. Genet. 11 (24): 3065–74. doi:10.1093/hmg/11.24.3065. PMID 12417528.
Kühnel K, Veltel S, Schlichting I, Wittinghofer A (2006). "Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3". Structure. 14 (2): 367–78. doi:10.1016/j.str.2005.11.008. hdl:11858/00-001M-0000-0015-8B49-9. PMID 16472755.
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.