Q640N2 · AR13B_MOUSE
- ProteinADP-ribosylation factor-like protein 13B
- GeneArl13b
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids427 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axoneme | |
Cellular Component | ciliary membrane | |
Cellular Component | cilium | |
Cellular Component | cytosol | |
Cellular Component | motile cilium | |
Cellular Component | non-motile cilium | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Biological Process | cilium assembly | |
Biological Process | determination of left/right symmetry | |
Biological Process | dorsal/ventral pattern formation | |
Biological Process | formation of radial glial scaffolds | |
Biological Process | heart looping | |
Biological Process | interneuron migration from the subpallium to the cortex | |
Biological Process | left/right axis specification | |
Biological Process | neural tube patterning | |
Biological Process | non-motile cilium assembly | |
Biological Process | receptor localization to non-motile cilium | |
Biological Process | smoothened signaling pathway |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameADP-ribosylation factor-like protein 13B
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ640N2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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
- Cellular component
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 8-9 | Abolishes palmitoylation and localization to the cilium membrane. | ||||
Sequence: CC → SS | ||||||
Mutagenesis | 358 | Abolishes localization to cilium. | ||||
Sequence: V → A |
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.
PTM/Processing
Features
Showing features for chain, lipidation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000251138 | 1-427 | ADP-ribosylation factor-like protein 13B | |||
Sequence: MFSLMANCCNLFKRWREPVRKVTLVMVGLDNAGKTATAKGIQGEHPEDVAPTVGFSKIDLRQGKFQVTIFDLGGGKRIRGIWKNYYAESYGVIFVVDSSDEERMEETKETMSEVLRHPRISGKPILVLANKQDKEGALGEADVIECLSLEKLVNEHKCLCQIEPCSAVLGYGKKIDKSIKKGLYWLLHIIAKDFDALSERIQKDTTEQRALEEQEKRERAERVRKLREEREREQTELDGTSGLAEIDSGPVLANPFQPIAAVIIENEKKQEKEKKKQTVEKDSDVGLLEHKVEPEQAAPQSEADCCLQNPDERVVDSYREALSQQLDSEDEQDQRGSESGENSKKKTKKLRMKRSHRVEPVNTDESTPKSPTPPQPPPPVGWGTPKVTRLPKLEPLGETRHNDFYGKPLPPLAVRQRPNGDAQDTIS | ||||||
Lipidation | 8 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 9 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 328 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Sumoylation is required for PKD2 entry into cilium.
Keywords
- PTM
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 194-285 | |||||
Sequence: FDALSERIQKDTTEQRALEEQEKRERAERVRKLREEREREQTELDGTSGLAEIDSGPVLANPFQPIAAVIIENEKKQEKEKKKQTVEKDSDV | ||||||
Compositional bias | 207-238 | Basic and acidic residues | ||||
Sequence: EQRALEEQEKRERAERVRKLREEREREQTELD | ||||||
Region | 207-250 | Disordered | ||||
Sequence: EQRALEEQEKRERAERVRKLREEREREQTELDGTSGLAEIDSGP | ||||||
Compositional bias | 269-297 | Basic and acidic residues | ||||
Sequence: KQEKEKKKQTVEKDSDVGLLEHKVEPEQA | ||||||
Region | 269-427 | Disordered | ||||
Sequence: KQEKEKKKQTVEKDSDVGLLEHKVEPEQAAPQSEADCCLQNPDERVVDSYREALSQQLDSEDEQDQRGSESGENSKKKTKKLRMKRSHRVEPVNTDESTPKSPTPPQPPPPVGWGTPKVTRLPKLEPLGETRHNDFYGKPLPPLAVRQRPNGDAQDTIS | ||||||
Compositional bias | 313-345 | Basic and acidic residues | ||||
Sequence: RVVDSYREALSQQLDSEDEQDQRGSESGENSKK | ||||||
Compositional bias | 367-384 | Pro residues | ||||
Sequence: TPKSPTPPQPPPPVGWGT |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length427
- Mass (Da)48,144
- Last updated2012-10-03 v2
- ChecksumAC131D386B999ABB
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A338P6Z3 | A0A338P6Z3_MOUSE | Arl13b | 126 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 207-238 | Basic and acidic residues | ||||
Sequence: EQRALEEQEKRERAERVRKLREEREREQTELD | ||||||
Compositional bias | 269-297 | Basic and acidic residues | ||||
Sequence: KQEKEKKKQTVEKDSDVGLLEHKVEPEQA | ||||||
Compositional bias | 313-345 | Basic and acidic residues | ||||
Sequence: RVVDSYREALSQQLDSEDEQDQRGSESGENSKK | ||||||
Sequence conflict | 356 | in Ref. 3; AAH82574 | ||||
Sequence: H → Q | ||||||
Compositional bias | 367-384 | Pro residues | ||||
Sequence: TPKSPTPPQPPPPVGWGT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |