M3WEU7 · M3WEU7_FELCA

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

  • n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
    EC:5.6.1.1 (UniProtKB | ENZYME | Rhea)

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.

TypeIDPosition(s)Description
Binding site249-256ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcentrosome
Cellular Componentcytoplasm
Cellular Componentkatanin complex
Cellular Componentmicrotubule
Cellular Componentmicrotubule cytoskeleton
Cellular Componentmidbody
Cellular Componentmitotic spindle pole
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionisomerase activity
Molecular Functionmicrotubule binding
Molecular Functionmicrotubule severing ATPase activity
Molecular Functionprotein heterodimerization activity
Biological Processcell division
Biological Processcytoplasmic microtubule organization
Biological Processmicrotubule severing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Katanin p60 ATPase-containing subunit A1
  • EC number
  • Short names
    Katanin p60 subunit A1
  • Alternative names
    • p60 katanin

Gene names

    • Name
      KATNA1

Organism names

  • Taxonomic identifier
  • Strain
    • Abyssinian
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Feliformia > Felidae > Felinae > Felis

Accessions

  • Primary accession
    M3WEU7

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Midbody
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

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue42Phosphoserine; by DYRK2
Modified residue109Phosphoserine; by DYRK2
Modified residue133Phosphothreonine; by DYRK2

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

Proteomic databases

Expression

Gene expression databases

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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region97-185Disordered
Compositional bias121-139Polar residues
Compositional bias140-172Basic and acidic residues
Domain241-383AAA+ ATPase

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    491
  • Mass (Da)
    55,969
  • Last updated
    2013-05-01 v1
  • Checksum
    DB7A0A402C1E9FB3
MSLLMISENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTYLQQKWQQVWQEINVEAKHVKDIMKTLESFKLDHTPLKAAQHELPASEGEVWSLPVPVERRPSPGPRKRQSPQYGDPKPHSNRPNTTARVHRSSAHSLHNDRGKAVRCREKKEQNKGREEKNKSPAAVTEPETSKFDSTGYDKDLVEALERDIISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLSKEEMHMPTTMEDFEMALKKVSKSVSAADIERYEKWIFEFGSC

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A337S2M9A0A337S2M9_FELCAKATNA1311

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias121-139Polar residues
Compositional bias140-172Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AANG04000169
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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