A0A915ABU5 · A0A915ABU5_PARUN

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.

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.

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TypeIDPosition(s)Description
Binding site257-264ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcentrosome
Cellular Componentcytoplasm
Cellular Componentmicrotubule
Cellular Componentspindle pole
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionisomerase activity
Molecular Functionmicrotubule binding
Molecular Functionmicrotubule severing ATPase activity
Biological Processcell division
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
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Spirurina > Ascaridomorpha > Ascaridoidea > Ascarididae > Parascaris

Accessions

  • Primary accession
    A0A915ABU5

Proteomes

Subcellular Location

Cytoplasm
Note: Predominantly cytoplasmic. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1.

Keywords

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.

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region88-185Disordered
Compositional bias94-108Pro residues
Compositional bias109-152Polar residues
Compositional bias161-185Basic and acidic residues
Domain249-386AAA+ ATPase

Sequence similarities

Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    494
  • Mass (Da)
    54,848
  • Last updated
    2023-02-22 v1
  • Checksum
    B1D1E54E285E4384
MDIGLLAENCQMARESALVGNYERASVFYQSAIAQISRHLNKITFDDPRRCQWSQSKSILQNELDSVNSLASASCQLRQLALGAIATSPVDAPPTDPDVWPPPTPLPRKSTLSARSKTVVRKPASSQSADNKAKKSVMRKSASQSGIEHGASSKRASSVGRVAKVELHEESIPDEKETDKKECKEEEKVFDGRGYDKELIEAIERDIVQQQPDVRWCDIAGLEDAKKLLKEAVVLPSVIPQFFKGIRRPWRGVCMVGPPGTGKTLLAKAVATECRTTFFCVSSSTMTSKYRGESEKLVRILFDMARFYAPSTIFIDEIDSLCSRRGAQTEHEASRRVKSELLIQMDGCSADTSRMVLVLAATNFPWDLDEALRRRLEKRIYIPLPDRTDRLTLLKLALAEVVVAEDVDLGKVADRLEGYSGADITNVCREAAMMSMRARIANLTADEIKALTHEEIDLPITSEDFASAIEHTSPSVSLDDIHKYEQWMHDFGAA

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A915AC78A0A915AC78_PARUNKATNA1488

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias94-108Pro residues
Compositional bias109-152Polar residues
Compositional bias161-185Basic and acidic residues

Keywords

Genome annotation databases

Similar Proteins

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