A0A034W584 · A0A034W584_BACDO

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.

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.

1813100200300400500600700800
TypeIDPosition(s)Description
Binding site578-585ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcentrosome
Cellular Componentchromosome
Cellular Componentcytoplasm
Cellular Componentlipid droplet
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 Processcell differentiation
Biological Processcell division
Biological Processmicrotubule severing
Biological Processnervous system development
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

    • Name
      SPAST
    • Synonyms
      LOC105227605

Organism names

  • Taxonomic identifier
  • Strain
    • Punador
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Tephritoidea > Tephritidae > Bactrocera > Bactrocera

Accessions

  • Primary accession
    A0A034W584

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, transmembrane, intramembrane.

TypeIDPosition(s)Description
Topological domain1-119Cytoplasmic
Transmembrane113-135Helical
Intramembrane120-140Helical
Topological domain141-813Cytoplasmic

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 compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-85Polar residues
Region1-105Disordered
Compositional bias221-238Polar residues
Region221-252Disordered
Domain250-328MIT
Compositional bias392-464Polar residues
Region392-506Disordered
Compositional bias472-506Polar residues
Domain570-707AAA+ ATPase

Sequence similarities

Belongs to the AAA ATPase family. Spastin subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    813
  • Mass (Da)
    89,015
  • Last updated
    2014-07-09 v1
  • Checksum
    4A41E5920FC76ED9
MVRNKTQSTSSSSSGNASGSASNSSSSTKSPIRQNSASSNNINSGARTHRKSSSTCSVALADDSKPASSSSRRSQPQSNNNTSSHTDEETDVEYDRTPTDGAPSISSVHKQNLYIVSFPIIFLFNILRSLIYQLFCIFRYVYGASTKVIYRPHKRECNIEIVVGSNKSFQNSRNENSLISESDKNQLVQYHSRNSSLATYPLAGGTGIGVGNNSTVSGQQRYRSAQQLDMSGRGNPSSSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWERAQRLHDKMQTNLSMARDRLHFLELREEELKLHALKLSDCDEQTNKVLVVPPMVVNGTEYKNSATSRTSLTKTDSRLPSYNIQNKLRTTKKSTTDSHKSISCASTTTGGKVSSTASGRKLTVSSKRPGNLAVINKSQTLPRNLGSKNASSTAVQRQPVKTAATPPAVRRQFTSGRNTPPQRARTPINTSSNYGNQSSGSGTAAAVTVKGVEQKLVQIILDEIVEGGAKVEWSDIAGQEVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVAREMQPSIIFIDEVDSLLSERSSNEHEASRRLKTEFLVEFDGLPGNPEGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDIDTRELLLSRLLEKQGSPLSTEALRRLAKLTDGYSGSDLTALAKDAALEPIRELNMEQVKCLDISAMRSITENDFHNSLKRIRRSVASQSLNSYEKWSQEYGDITI

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-85Polar residues
Compositional bias221-238Polar residues
Compositional bias392-464Polar residues
Compositional bias472-506Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GAKP01009677
EMBL· GenBank· DDBJ
JAC49275.1
EMBL· GenBank· DDBJ
Transcribed RNA

Genome annotation databases

Similar Proteins

Disclaimer

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