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P36405 (ARL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 3
Gene names
Name:ARL3
Synonyms:ARFL3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length182 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). Required for normal cytokinesis and cilia signaling. Requires assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms. Required for targeting proteins such as NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from UNC119B cargo adapter into the cilium. Does not act as an allosteric activator of the cholera toxin catalytic subunit. Ref.13 Ref.15 Ref.18

Subunit structure

Interacts with RP2. The GTP-bound form interacts with PDE6D. Found in a complex with ARL3, RP2 and UNC119 (or UNC119B); RP2 induces hydrolysis of GTP ARL3 in the complex, leading to the release of UNC119 (or UNC119B). Interacts with SYS1. The GTP-bound form interacts with ARL2BP and PDE6D. Interacts with RP2; interaction is direct and stimulated with the activated GTP-bound form of ARL3. Microtubule-associated protein. Does not interact with TBCC. May interact with GOLGA4. Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15

Subcellular location

Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeletonspindle. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasm. Cell projectioncilium. Note: Detected predominantly in the photoreceptor connecting cilium. Present on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. Ref.10 Ref.12 Ref.13 Ref.15

Tissue specificity

Expressed in the retina. Strongly expressed in connecting cilium, the myoid region of the inner segments (IS) and in cone photoreceptors (at protein level). Ref.10

Sequence similarities

Belongs to the small GTPase superfamily. Arf family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Protein transport
Transport
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcilium morphogenesis

Inferred from mutant phenotype Ref.18. Source: UniProtKB

cytokinesis

Inferred from mutant phenotype Ref.13. Source: UniProtKB

intraciliary transport

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from sequence or structural similarity. Source: UniProtKB

photoreceptor cell development

Inferred from sequence or structural similarity. Source: UniProtKB

post-Golgi vesicle-mediated transport

Inferred from mutant phenotype PubMed 20106869. Source: MGI

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

small GTPase mediated signal transduction

Inferred from direct assay Ref.18. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.13. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

centrosome

Inferred from direct assay Ref.13. Source: UniProtKB

cytoplasmic microtubule

Inferred from direct assay Ref.10. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

midbody

Inferred from direct assay Ref.13. Source: UniProtKB

nucleus

Inferred from direct assay Ref.13. Source: UniProtKB

photoreceptor connecting cilium

Inferred from direct assay Ref.10. Source: UniProtKB

primary cilium

Inferred from direct assay Ref.13. Source: UniProtKB

spindle microtubule

Inferred from direct assay Ref.13. Source: UniProtKB

   Molecular_functionGDP binding

Inferred from direct assay Ref.15. Source: UniProtKB

GTP binding

Inferred from direct assay Ref.15Ref.18. Source: UniProtKB

GTPase activity

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule binding

Inferred from direct assay Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11Ref.18. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDE6DO439242EBI-712710,EBI-712685
UNC119Q134325EBI-712710,EBI-711260

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 182181ADP-ribosylation factor-like protein 3
PRO_0000207456

Regions

Nucleotide binding24 – 318GTP By similarity
Nucleotide binding67 – 715GTP By similarity
Nucleotide binding126 – 1294GTP By similarity
Nucleotide binding159 – 1613GTP By similarity

Sites

Metal binding311Magnesium By similarity
Metal binding481Magnesium By similarity
Binding site481GTP By similarity
Binding site701GTP; via amide nitrogen By similarity

Amino acid modifications

Modified residue51Phosphoserine Ref.16
Lipidation21N-myristoyl glycine Potential

Natural variations

Natural variant341L → M. Ref.4
Corresponds to variant rs1141895 [ dbSNP | Ensembl ].
VAR_014869

Experimental info

Mutagenesis311T → N: Enhances the interaction with RP2. Ref.11 Ref.18
Mutagenesis711Q → L: Enhances the interaction with RP2. Does not induce a mitotic arrest resulting from the loss of the microtubule-based mitotic spindle. Induces release of myristoylated proteins from UNC119. Interacts with ARL2BP, GOLGA4, PDE6D and UNC119. Ref.9 Ref.11 Ref.13 Ref.18

Sequences

Sequence LengthMass (Da)Tools
P36405 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: E5C1ACAD0BD55537

FASTA18220,456
        10         20         30         40         50         60 
MGLLSILRKL KSAPDQEVRI LLLGLDNAGK TTLLKQLASE DISHITPTQG FNIKSVQSQG 

        70         80         90        100        110        120 
FKLNVWDIGG QRKIRPYWKN YFENTDILIY VIDSADRKRF EETGQELAEL LEEEKLSCVP 

       130        140        150        160        170        180 
VLIFANKQDL LTAAPASEIA EGLNLHTIRD RVWQIQSCSA LTGEGVQDGM NWVCKNVNAK 


KK 

« Hide

References

« Hide 'large scale' references
[1]"ADP-ribosylation factor (ARF)-like 3, a new member of the ARF family of GTP-binding proteins cloned from human and rat tissues."
Cavenagh M.A., Breiner M., Schurmann A., Rosenwald A.G., Terui T., Zhang C.-J., Randoazzo P.A., Adams M., Joost H.-G., Kahn R.A.
J. Biol. Chem. 269:18937-18942(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thalamus.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-34.
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Skin.
[7]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 80-97 AND 128-149, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[8]"ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin."
Bhamidipati A., Lewis S.A., Cowan N.J.
J. Cell Biol. 149:1087-1096(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ABSENCE OF INTERACTION WITH TBCC.
[9]"ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins."
Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.
J. Biol. Chem. 276:22826-22837(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARL2BP; GOLGA4; PDE6D AND UNC119, MUTAGENESIS OF GLN-71.
[10]"Localization in the human retina of the X-linked retinitis pigmentosa protein RP2, its homologue cofactor C and the RP2 interacting protein Arl3."
Grayson C., Bartolini F., Chapple J.P., Willison K.R., Bhamidipati A., Lewis S.A., Luthert P.J., Hardcastle A.J., Cowan N.J., Cheetham M.E.
Hum. Mol. Genet. 11:3065-3074(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[11]"Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C."
Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A., Cowan N.J.
J. Biol. Chem. 277:14629-14634(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RP2 AND ARL2BP, MUTAGENESIS OF THR-31 AND GLN-71.
[12]"Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p."
Behnia R., Panic B., Whyte J.R.C., Munro S.
Nat. Cell Biol. 6:405-413(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYS1, SUBCELLULAR LOCATION.
[13]"Arl2 and Arl3 regulate different microtubule-dependent processes."
Zhou C., Cunningham L., Marcus A.I., Li Y., Kahn R.A.
Mol. Biol. Cell 17:2476-2487(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLN-71, SUBCELLULAR LOCATION.
[14]"Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3."
Kuehnel K., Veltel S., Schlichting I., Wittinghofer A.
Structure 14:367-378(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RP2.
[15]"Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-GAP complex."
Veltel S., Kravchenko A., Ismail S., Wittinghofer A.
FEBS Lett. 582:2501-2507(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, GTP/GDP BINDING, IDENTIFICATION IN A COMPLEX WITH UNC119 AND RP2, SUBCELLULAR LOCATION.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the primary cilium."
Wright K.J., Baye L.M., Olivier-Mason A., Mukhopadhyay S., Sang L., Kwong M., Wang W., Pretorius P.R., Sheffield V.C., Sengupta P., Slusarski D.C., Jackson P.K.
Genes Dev. 25:2347-2360(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF THR-31 AND GLN-71.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U07151 mRNA. Translation: AAA21654.1.
AF493889 mRNA. Translation: AAM12603.1.
AK312525 mRNA. Translation: BAG35424.1.
CR407637 mRNA. Translation: CAG28565.1.
AL391121 Genomic DNA. Translation: CAI40862.1.
BC009841 mRNA. Translation: AAH09841.1.
CCDSCCDS7538.1.
PIRA54869.
RefSeqNP_004302.1. NM_004311.3.
UniGeneHs.182215.

3D structure databases

ProteinModelPortalP36405.
SMRP36405. Positions 2-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106896. 11 interactions.
IntActP36405. 10 interactions.
MINTMINT-1368863.
STRING9606.ENSP00000260746.

PTM databases

PhosphoSiteP36405.

Polymorphism databases

DMDM543851.

2D gel databases

REPRODUCTION-2DPAGEIPI00003327.
UCD-2DPAGEP36405.

Proteomic databases

MaxQBP36405.
PaxDbP36405.
PeptideAtlasP36405.
PRIDEP36405.

Protocols and materials databases

DNASU403.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260746; ENSP00000260746; ENSG00000138175.
GeneID403.
KEGGhsa:403.
UCSCuc001kwa.3. human.

Organism-specific databases

CTD403.
GeneCardsGC10M104423.
HGNCHGNC:694. ARL3.
HPAHPA036292.
MIM604695. gene.
neXtProtNX_P36405.
PharmGKBPA24987.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000163691.
HOVERGENHBG002073.
InParanoidP36405.
KOK07944.
OMALECEEFQ.
OrthoDBEOG7M98HG.
PhylomeDBP36405.
TreeFamTF105463.

Gene expression databases

BgeeP36405.
CleanExHS_ARL3.
GenevestigatorP36405.

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

GeneWikiARL3.
GenomeRNAi403.
NextBio1689.
PROP36405.
SOURCESearch...

Entry information

Entry nameARL3_HUMAN
AccessionPrimary (citable) accession number: P36405
Secondary accession number(s): B2R6C7, Q53X83, Q5JSM2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM