Q640N2 · AR13B_MOUSE

  • Protein
    ADP-ribosylation factor-like protein 13B
  • Gene
    Arl13b
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Cilium-specific protein required to control the microtubule-based, ciliary axoneme structure. May act by maintaining the association between IFT subcomplexes A and B. Binds GTP but is not able to hydrolyze it; the GTPase activity remains unclear. Required to pattern the neural tube. Involved in cerebral cortex development: required for the initial formation of a polarized radial glial scaffold, the first step in the construction of the cerebral cortex, by regulating ciliary signaling (PubMed:23817546).
Regulates the migration and placement of postmitotic interneurons in the developing cerebral cortex (PubMed:23153492).
Plays a role in ciliar trafficking of phosphatidylinositol phosphatase INPP5E in ciliogenesis (By similarity).
May regulate ARF6- and RAB22A-dependent endocytic recycling traffic (By similarity).

Miscellaneous

Used as a ciliary marker because of its specific localization to microtubule doublets of the ciliary axoneme. Frequently used to study cilium signaling, since in contrast to most cilia null mutants, deletion of Arl13b impairs without destroying cilia and their downstream pathways (PubMed:23817546).

Features

Showing features for binding site.

142750100150200250300350400
TypeIDPosition(s)Description
Binding site28-35GTP (UniProtKB | ChEBI)
Binding site71-75GTP (UniProtKB | ChEBI)
Binding site130-133GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentaxoneme
Cellular Componentciliary membrane
Cellular Componentcilium
Cellular Componentcytosol
Cellular Componentmotile cilium
Cellular Componentnon-motile cilium
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Biological Processcilium assembly
Biological Processdetermination of left/right symmetry
Biological Processdorsal/ventral pattern formation
Biological Processformation of radial glial scaffolds
Biological Processheart looping
Biological Processinterneuron migration from the subpallium to the cortex
Biological Processleft/right axis specification
Biological Processneural tube patterning
Biological Processnon-motile cilium assembly
Biological Processreceptor localization to non-motile cilium
Biological Processsmoothened signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ADP-ribosylation factor-like protein 13B
  • Alternative names
    • ADP-ribosylation factor-like protein 2-like 1 (ARL2-like protein 1)
    • Protein hennin

Gene names

    • Name
      Arl13b
    • Synonyms
      Arl2l1

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q640N2
  • Secondary accessions
    • G3X9K5

Proteomes

Organism-specific databases

Subcellular Location

Cell projection, cilium membrane
; Lipid-anchor
Note: Associates with the cilium membrane via palmitoylation. Localizes to proximal ciliary membranes, to an inversin-like subciliary membrane compartment, excluding the transition zone.

Keywords

Phenotypes & Variants

Disruption phenotype

Impaired cilium's ability to convey critical extracellular signals such as Shh, without destroying cilia and their downstream pathways. Mice show a constitutive low-level of Shh activity owing to loss of modulation of Gli2 activator, corresponding to the specification of progenitors of motoneurons through most of the neural tube. In contrast to other mouse mutants that disrupt cilia, Gli3 repressor activity is unaffected in mutants (PubMed:17488627).
Mutants show abnormal cilia in which components of Shh signaling are not regulated properly: Ptch1 and Smo localize to cilia regardless of Shh stimulation, and there is no Gli enrichment in cilia upon Shh stimulation (PubMed:21976698).
Conditional deletion disrupts interneuronal placement, but not postmigratory differentiation in the developing cerebral cortex (PubMed:23153492).
Early neuroepithelial-specific deletion in cortical progenitors induces a reversal of the apical-basal polarity of radial progenitors and aberrant neuronal placement (PubMed:23817546).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis8-9Abolishes palmitoylation and localization to the cilium membrane.
Mutagenesis358Abolishes localization to cilium.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 29 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, lipidation, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002511381-427ADP-ribosylation factor-like protein 13B
Lipidation8S-palmitoyl cysteine
Lipidation9S-palmitoyl cysteine
Modified residue328Phosphoserine

Post-translational modification

Sumoylation is required for PKD2 entry into cilium.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Cilium-specific protein. Expressed in neuroepithelial cells and developing radial glia of the developing cerebral cortex: present in both neuroepithelial and radial progenitor cells. In radial progenitors, found in the apical, cell soma domains of these cells (at protein level). Expressed in the primary cilia of postmitotic cortical neurons during embryonic and postnatal development.

Gene expression databases

Interaction

Subunit

Monomer. Interacts with IFT complex B components IFT46 and IFT74 (By similarity).
Interacts with CIMAP3 (By similarity) (PubMed:20643351).
Interacts with EXOC2; regulates ARL13B localization to the cilium membrane (PubMed:26582389).
Interacts with actin; the interaction mediates colocalization of ARL13B and microtubules (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for coiled coil, compositional bias, region.

TypeIDPosition(s)Description
Coiled coil194-285
Compositional bias207-238Basic and acidic residues
Region207-250Disordered
Compositional bias269-297Basic and acidic residues
Region269-427Disordered
Compositional bias313-345Basic and acidic residues
Compositional bias367-384Pro residues

Domain

The C-terminal domain is required for localization to microtubules and the cell membrane.

Sequence similarities

Belongs to the small GTPase superfamily. Arf family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    427
  • Mass (Da)
    48,144
  • Last updated
    2012-10-03 v2
  • Checksum
    AC131D386B999ABB
MFSLMANCCNLFKRWREPVRKVTLVMVGLDNAGKTATAKGIQGEHPEDVAPTVGFSKIDLRQGKFQVTIFDLGGGKRIRGIWKNYYAESYGVIFVVDSSDEERMEETKETMSEVLRHPRISGKPILVLANKQDKEGALGEADVIECLSLEKLVNEHKCLCQIEPCSAVLGYGKKIDKSIKKGLYWLLHIIAKDFDALSERIQKDTTEQRALEEQEKRERAERVRKLREEREREQTELDGTSGLAEIDSGPVLANPFQPIAAVIIENEKKQEKEKKKQTVEKDSDVGLLEHKVEPEQAAPQSEADCCLQNPDERVVDSYREALSQQLDSEDEQDQRGSESGENSKKKTKKLRMKRSHRVEPVNTDESTPKSPTPPQPPPPVGWGTPKVTRLPKLEPLGETRHNDFYGKPLPPLAVRQRPNGDAQDTIS

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A338P6Z3A0A338P6Z3_MOUSEArl13b126

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias207-238Basic and acidic residues
Compositional bias269-297Basic and acidic residues
Compositional bias313-345Basic and acidic residues
Sequence conflict356in Ref. 3; AAH82574
Compositional bias367-384Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC154309
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH466521
EMBL· GenBank· DDBJ
EDK98235.1
EMBL· GenBank· DDBJ
Genomic DNA
BC082574
EMBL· GenBank· DDBJ
AAH82574.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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