W8C8D8 · W8C8D8_CERCA

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.

1723100200300400500600700
TypeIDPosition(s)Description
Binding site488-495ATP (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 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

Organism names

Accessions

  • Primary accession
    W8C8D8

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.

Type
IDPosition(s)Description
Topological domain1-120Cytoplasmic
Transmembrane114-136Helical
Intramembrane121-141Helical
Topological domain142-723Cytoplasmic

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.

Type
IDPosition(s)Description
Compositional bias1-86Polar residues
Region1-104Disordered
Compositional bias230-244Polar residues
Region230-253Disordered
Domain251-329MIT
Compositional bias352-374Polar residues
Region352-414Disordered
Compositional bias382-414Polar residues
Domain480-617AAA+ ATPase

Sequence similarities

Belongs to the AAA ATPase family. Spastin subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    723
  • Mass (Da)
    79,026
  • Last updated
    2014-04-16 v1
  • Checksum
    BAECB9FBEC2D6C0B
MVRNKTQSTSSSSSGNASGSASNSSSSTKSPIRQNSASNNNINSGARTHRKSSSTCSVALADDSKPTSSSSSRRSQPQVNTNTTTHTDEETDGEYDRTPTGGAPSISSVHKQNLYIVSFPIIFLFNILRSLIYQLFCIFRYVYGASTKVIYRPHKRECNIEIVVGSNNSFKNSQNENNLTNDIDKNQLVQYQSRNSALATYPLVGSAGIGIGNIAAVGGQQRFRSAQQLDMSGRGNTSSSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWERAQRLHDKMQTNLSMARDRLHFLASGRKLTVSSKRPGNLAVINKSQTLPRNLGSKNASSTAVQRQPVKTAATPPAVRRQFSSGRNTPPQRARTPINTSSNYSGQSSSSASAAAVTVKGVEQKLVQIILDEIVEGGAKVEWSDIAGQEVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVAREMQPSIIFIDEVDSLLSERSSNEHEASRRLKTEFLVEFDGLPGNPEGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDLDTRELLLSRLLEKQGSPLGTEALRRLAKLTDGYSGSDLTALAKDAALEPIRELNMEQVKCLDISAMRPITENDFHNSLKRIRRSVASQSLNSYEKWSQEYGDITI

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-86Polar residues
Compositional bias230-244Polar residues
Compositional bias352-374Polar residues
Compositional bias382-414Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GAMC01007521
EMBL· GenBank· DDBJ
JAB99034.1
EMBL· GenBank· DDBJ
mRNA
GAMC01007519
EMBL· GenBank· DDBJ
JAB99036.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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