A0A061IIZ4 · A0A061IIZ4_CRIGR
- ProteinKatanin p60 ATPase-containing subunit A1
- GeneKATNA1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids506 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth.
Catalytic activity
Activity regulation
ATPase activity is stimulated by microtubules, which promote homooligomerization. ATP-dependent microtubule severing is stimulated by interaction with KATNB1.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | cytoplasm | |
Cellular Component | microtubule | |
Cellular Component | midbody | |
Cellular Component | spindle pole | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | isomerase activity | |
Molecular Function | microtubule binding | |
Molecular Function | microtubule severing ATPase activity | |
Biological Process | cell division | |
Biological Process | microtubule severing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKatanin p60 ATPase-containing subunit A1
- EC number
- Short namesKatanin p60 subunit A1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Cricetidae > Cricetinae > Cricetulus
Accessions
- Primary accessionA0A061IIZ4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Predominantly cytoplasmic. Localized diffusely in the cytoplasm during the interphase. During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase and telophase is localized at the midbody region. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1. Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 51 | Phosphoserine; by DYRK2 | ||||
Sequence: S | ||||||
Modified residue | 118 | Phosphoserine; by DYRK2 | ||||
Sequence: S |
Post-translational modification
Phosphorylation by DYRK2 triggers ubiquitination and subsequent degradation.
Ubiquitinated by the BCR(KLHL42) E3 ubiquitin ligase complex, leading to its proteasomal degradation. Ubiquitinated by the EDVP E3 ligase complex and subsequently targeted for proteasomal degradation.
Keywords
- PTM
Interaction
Subunit
Can homooligomerize into hexameric rings, which may be promoted by interaction with microtubules. Interacts with KATNB1, which may serve as a targeting subunit. Interacts with ASPM; the katanin complex formation KATNA1:KATNB1 is required for the association of ASPM. Interacts with dynein and NDEL1. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP complex). Interacts with KLHL42 (via the kelch domains). Interacts with CUL3; the interaction is enhanced by KLHL42. Interacts with KATNB1 and KATNBL1. Interacts with CAMSAP2 and CAMSAP3; leading to regulate the length of CAMSAP-decorated microtubule stretches.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 106-197 | Disordered | ||||
Sequence: VWSLPVPVERRPSPGPRKRQSSQYHDPKPHSNRPGTGVRAHRPSAQSLHNDRGKAVRSREKKEQSKGREEKKRALDPNKSPAAVTEQEANKF | ||||||
Compositional bias | 117-131 | Basic and acidic residues | ||||
Sequence: PSPGPRKRQSSQYHD | ||||||
Compositional bias | 150-182 | Basic and acidic residues | ||||
Sequence: AQSLHNDRGKAVRSREKKEQSKGREEKKRALDP | ||||||
Domain | 256-398 | AAA+ ATPase | ||||
Sequence: PWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPS |
Domain
The N-terminus is sufficient for interaction with microtubules, although high affinity binding to microtubules also requires an intact C-terminal domain and ATP, which promotes oligomerization.
Sequence similarities
Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length506
- Mass (Da)57,561
- Last updated2014-09-03 v1
- Checksum69019816C41F0487
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 117-131 | Basic and acidic residues | ||||
Sequence: PSPGPRKRQSSQYHD | ||||||
Compositional bias | 150-182 | Basic and acidic residues | ||||
Sequence: AQSLHNDRGKAVRSREKKEQSKGREEKKRALDP |