A0A182DXM0 · A0A182DXM0_ONCOC

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.
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.

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)

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NUBP1 and two labile, bridging clusters between subunits of the NUBP1-NUBP2 heterotetramer.

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 site375-382ATP (UniProtKB | ChEBI)
Binding site824[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site838[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site841[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site847[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site878-885ATP (UniProtKB | ChEBI)
Binding site1052[4Fe-4S] cluster 2 (UniProtKB | ChEBI); ligand shared with heterodimeric partner
Binding site1055[4Fe-4S] cluster 2 (UniProtKB | ChEBI); ligand shared with heterodimeric partner

GO annotations

AspectTerm
Cellular Componentcell projection
Cellular Componentcentrosome
Cellular Componentcytoplasm
Cellular Componentmicrotubule
Cellular Componentspindle pole
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionacyltransferase activity
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent FeS chaperone activity
Molecular Functionisomerase activity
Molecular Functionmetal ion binding
Molecular Functionmicrotubule binding
Molecular Functionmicrotubule severing ATPase activity
Biological Processcell division
Biological ProcessDNA repair
Biological Processiron-sulfur cluster assembly
Biological Processmicrotubule severing

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Katanin p60 ATPase-containing subunit A1
  • EC number
  • Short names
    Katanin p60 subunit A1
  • Alternative names
    • p60 katanin
  • Recommended name
    Cytosolic Fe-S cluster assembly factor NUBP1 homolog

Gene names

    • Name
      KATNA1
    • ORF names
      NOO_LOCUS399

Organism names

Accessions

  • Primary accession
    A0A182DXM0

Proteomes

Subcellular Location

Cell projection
Cytoplasm, cytoskeleton
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.
Heterotetramer of 2 NUBP1 and 2 NUBP2 chains.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region224-308Disordered
Compositional bias255-283Polar residues
Compositional bias286-308Basic and acidic residues
Domain1128-1514Ketosynthase family 3 (KS3)

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,518
  • Mass (Da)
    166,883
  • Last updated
    2016-09-07 v1
  • Checksum
    FA5B97953B04122A
MGDRWQSARKVGPACEEMGGVAIAHWLSLDDGMNAKRLMIGKSCPACIALWGWDIDFHSLISYSISCLQSAFLRFPGKSCEMFCFDRLVLIFVLAPIFDDWLPPEWHMDRLPKQRTIVKKAQMEWEISESYRAAKEAALRRKYDQSALFLRTALSLIERRLNSISVDDPNKDQLVKVKSVLKLNVERMNGIADVVSQMRQMAGVTISSSPIDAPPSDPDVWPLPPLTKKTSAIPSPKSAAKKQTYSRVDNKTKKSSVGKSPCTSAGCRNITKRANSLGRASMSELSEVTPKEEGDNNSNEKGGNEKVFDDRGFDKELVEIIERDIMQKRPDVHWNDIAGLDEAKKLLKEAVILPSVMPNFFKGIRRPWRGVCMVGPPGTGKTMLAKAVATESQTTFFCVSSATLTSKYRGDSEKLVQLLFKMARFYAPSTIFIDEIDSLCSRRGADSEHEASRRVKSELLTQMDGCSPDVSRVLVLAATNFPWDLDEALRRRLEKRIYIPLPDKTNRFQLLKLALAEVSIDEEVNLETVADSLDGYSGADITNVCREAAMMSMRVRIANLTAEEIKALKQEEVDLPITSNDFSQAIQNTSPSVSSTDVQNEIVSGMEISNPNKSGAALLNSKLVINRKRQEGNPVLKYIRNVPFEWADIKADFEAGKEMGILYLSLKWHKLHPNYIETRINSDGIGYAIKVLLVLVNVEPRHILRELNLFCYRTGWTLMLCYSAEEAAEYLENLHISRNRNEQSVVNAMQERKRKRLCLSDDDSKLQQAIKFLSVIRSLTVSDAQRLIATFGNIQKIANADIDRLLLCPGLAMNDIPENANENCPGATSADAGKATSCAGCPNQVLCASGETKKLDADLSAIADRLKNVKHKILILSGKGGVGKSAVAANLARALAKNDKIQVGLLDVDICGPSQARIMGVEQESVHESGDGWCPIVVKDNLIMMSIAFLLQNKSEAVIWRGARKNTLIKQFLKDVDWGSLDYLLIDTPPGTSDEHISIVQFLLQAGSVDGAIVITTPQEISLLDVRKEINFCRRTKINILGVIENMSSFICPCCSKLSQLFPRTTGGAETMCSELSVPLLVSLPFDGRMAGCADAGEDYFEKYYDSPVAKEFEKLAQLISSDVINSMKRVVITGIGIVSPFGVGKRLLFDNLLANNVALQHDEKLKIIVGRVSKYGENGLDLTSWSSRELKRMSRGSVLAVVAAEEAVKDAGLKECHMEETGVNVGMGIADLELIYDVGKQIAEGKGRRVTPFFIPRILTNMPAGHVSIKFGMRGPQLSSCTACATGLHSVGDSATFIRMGRAKRMLAGATEACVNSIAVIGFSQMRALTMTCSRPFDKRRDGFVLSEGAAILVLEEMEEALKRKANIYAEVLGYGVAGDAYHLTVPSEDGIGAFLSMERCLTDSSINPEQVTYVNAHATSTVLGDRFESLAIARLFPGHIGHTLAAAGAIETAITAMCVKESKLVGNVGLEESDIKENLRFLKQSEGWNNERVALVNSFGFGGSHATLCLSAIEKP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias255-283Polar residues
Compositional bias286-308Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
UYRW01000038
EMBL· GenBank· DDBJ
VDK62061.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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