A0A8S1AMV4 · A0A8S1AMV4_ARCPL

Function

function

ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the microtubule organizing center following nucleation.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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)

Features

Showing features for binding site.

159450100150200250300350400450500550
TypeIDPosition(s)Description
Binding site358-365ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcentrosome
Cellular Componentcytoplasm
Cellular Componentmembrane
Cellular Componentmicrotubule
Cellular Componentspindle
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionisomerase activity
Molecular Functionmicrotubule binding
Molecular Functionmicrotubule severing ATPase activity
Biological Processmicrotubule severing
Biological Processpositive regulation of microtubule depolymerization
Biological Processprotein hexamerization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Spastin
  • EC number

Gene names

    • ORF names
      APLA_LOCUS10835

Organism names

Accessions

  • Primary accession
    A0A8S1AMV4

Proteomes

Subcellular Location

Membrane
; Peripheral membrane protein
Cytoplasm, cytoskeleton
Note: Forms an intramembrane hairpin-like structure in the membrane.

Features

Showing features for topological domain.

TypeIDPosition(s)Description
Topological domain1-31Cytoplasmic
Topological domain45-594Cytoplasmic

Keywords

Interaction

Subunit

Homohexamer. The homohexamer is stabilized by ATP-binding. The homohexamer may adopt a ring conformation through which microtubules pass prior to being severed. Interacts with microtubules.

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-20Disordered
Domain61-139MIT
Compositional bias152-178Basic and acidic residues
Region152-291Disordered
Compositional bias179-194Polar residues
Compositional bias215-244Polar residues
Compositional bias256-289Polar residues
Domain350-486AAA+ ATPase

Sequence similarities

Belongs to the AAA ATPase family. Spastin subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    594
  • Mass (Da)
    64,723
  • Last updated
    2022-10-12 v1
  • Checksum
    6143FA5E87A00342
MVSGDDSNGGRLSRKTTRSPNRECNLEVVVKDGIVSTELAASEEMSHIHNVGPGDPLLAKQKHHHRKAFEYISKALKIDEENEGQKELAIELYKKGIYELERGIAVDCWGGRGDAWQRAQRLHDKMKTNLGMAKDRLHFLANLVALSKLGVESEADRSDKKPTESPLKARRPLEKSKTTLLAHTESNSGQTKPPNEVAGRKLTTAGRRVPSSGGGPLMKSQTLPRSMGRSSSQPNNTNGGYNRYPMKPVSTPPAVKRQLSVPSNGSPVRRVVSGGSQRGTPTRSRTPQPALSVRGVDPKLVQLILDEIVEGGPKVQWDDIAGQDAAKQALKEMVVLPSLRPELFTGLRSPAKGLLLFGPPGNGKTLLARCVAAECSATFFSISAATLTSKYVGEGEKMVRALFQVARELQPSIIFVDEVDSLLCERSSGEHEASRRLKTEFLVEFDGLPAAGADRLIVMAATNRPQELDEAALRRFPKRVYVSLPDMRTRMSLVRGMLARGAAAASLIDDELARLAALTDGYSGSDLAALCRDAALGPIRELDPEEVKCLDLSLVRSITYQDFIDALKRIRPSVSPHSLAAYEKWSVQYGDLGL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias152-178Basic and acidic residues
Compositional bias179-194Polar residues
Compositional bias215-244Polar residues
Compositional bias256-289Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CADEBC010000525
EMBL· GenBank· DDBJ
CAB3246340.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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