A0A034W584 · A0A034W584_BACDO
- ProteinSpastin
- GeneSPAST
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids813 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | chromosome | |
Cellular Component | cytoplasm | |
Cellular Component | lipid droplet | |
Cellular Component | membrane | |
Cellular Component | microtubule | |
Cellular Component | spindle | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | isomerase activity | |
Molecular Function | microtubule binding | |
Molecular Function | microtubule severing ATPase activity | |
Biological Process | cell differentiation | |
Biological Process | cell division | |
Biological Process | microtubule severing | |
Biological Process | nervous system development | |
Biological Process | positive regulation of microtubule depolymerization | |
Biological Process | protein hexamerization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSpastin
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Tephritoidea > Tephritidae > Bactrocera > Bactrocera
Accessions
- Primary accessionA0A034W584
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Peripheral membrane protein
Note: Forms an intramembrane hairpin-like structure in the membrane.
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-119 | Cytoplasmic | ||||
Sequence: MVRNKTQSTSSSSSGNASGSASNSSSSTKSPIRQNSASSNNINSGARTHRKSSSTCSVALADDSKPASSSSRRSQPQSNNNTSSHTDEETDVEYDRTPTDGAPSISSVHKQNLYIVSFP | ||||||
Transmembrane | 113-135 | Helical | ||||
Sequence: LYIVSFPIIFLFNILRSLIYQLF | ||||||
Intramembrane | 120-140 | Helical | ||||
Sequence: IIFLFNILRSLIYQLFCIFRY | ||||||
Topological domain | 141-813 | Cytoplasmic | ||||
Sequence: VYGASTKVIYRPHKRECNIEIVVGSNKSFQNSRNENSLISESDKNQLVQYHSRNSSLATYPLAGGTGIGVGNNSTVSGQQRYRSAQQLDMSGRGNPSSSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWERAQRLHDKMQTNLSMARDRLHFLELREEELKLHALKLSDCDEQTNKVLVVPPMVVNGTEYKNSATSRTSLTKTDSRLPSYNIQNKLRTTKKSTTDSHKSISCASTTTGGKVSSTASGRKLTVSSKRPGNLAVINKSQTLPRNLGSKNASSTAVQRQPVKTAATPPAVRRQFTSGRNTPPQRARTPINTSSNYGNQSSGSGTAAAVTVKGVEQKLVQIILDEIVEGGAKVEWSDIAGQEVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVAREMQPSIIFIDEVDSLLSERSSNEHEASRRLKTEFLVEFDGLPGNPEGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDIDTRELLLSRLLEKQGSPLSTEALRRLAKLTDGYSGSDLTALAKDAALEPIRELNMEQVKCLDISAMRSITENDFHNSLKRIRRSVASQSLNSYEKWSQEYGDITI |
Keywords
- Cellular component
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.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-85 | Polar residues | ||||
Sequence: MVRNKTQSTSSSSSGNASGSASNSSSSTKSPIRQNSASSNNINSGARTHRKSSSTCSVALADDSKPASSSSRRSQPQSNNNTSSH | ||||||
Region | 1-105 | Disordered | ||||
Sequence: MVRNKTQSTSSSSSGNASGSASNSSSSTKSPIRQNSASSNNINSGARTHRKSSSTCSVALADDSKPASSSSRRSQPQSNNNTSSHTDEETDVEYDRTPTDGAPSI | ||||||
Compositional bias | 221-238 | Polar residues | ||||
Sequence: RYRSAQQLDMSGRGNPSS | ||||||
Region | 221-252 | Disordered | ||||
Sequence: RYRSAQQLDMSGRGNPSSSPGPGDPLLAKQKH | ||||||
Domain | 250-328 | MIT | ||||
Sequence: QKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWERAQRLHDKMQTNLSMARDRLHF | ||||||
Compositional bias | 392-464 | Polar residues | ||||
Sequence: LRTTKKSTTDSHKSISCASTTTGGKVSSTASGRKLTVSSKRPGNLAVINKSQTLPRNLGSKNASSTAVQRQPV | ||||||
Region | 392-506 | Disordered | ||||
Sequence: LRTTKKSTTDSHKSISCASTTTGGKVSSTASGRKLTVSSKRPGNLAVINKSQTLPRNLGSKNASSTAVQRQPVKTAATPPAVRRQFTSGRNTPPQRARTPINTSSNYGNQSSGSG | ||||||
Compositional bias | 472-506 | Polar residues | ||||
Sequence: AVRRQFTSGRNTPPQRARTPINTSSNYGNQSSGSG | ||||||
Domain | 570-707 | AAA+ ATPase | ||||
Sequence: PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVAREMQPSIIFIDEVDSLLSERSSNEHEASRRLKTEFLVEFDGLPGNPEGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPD |
Sequence similarities
Belongs to the AAA ATPase family. Spastin subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length813
- Mass (Da)89,015
- Last updated2014-07-09 v1
- Checksum4A41E5920FC76ED9
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-85 | Polar residues | ||||
Sequence: MVRNKTQSTSSSSSGNASGSASNSSSSTKSPIRQNSASSNNINSGARTHRKSSSTCSVALADDSKPASSSSRRSQPQSNNNTSSH | ||||||
Compositional bias | 221-238 | Polar residues | ||||
Sequence: RYRSAQQLDMSGRGNPSS | ||||||
Compositional bias | 392-464 | Polar residues | ||||
Sequence: LRTTKKSTTDSHKSISCASTTTGGKVSSTASGRKLTVSSKRPGNLAVINKSQTLPRNLGSKNASSTAVQRQPV | ||||||
Compositional bias | 472-506 | Polar residues | ||||
Sequence: AVRRQFTSGRNTPPQRARTPINTSSNYGNQSSGSG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GAKP01009677 EMBL· GenBank· DDBJ | JAC49275.1 EMBL· GenBank· DDBJ | Transcribed RNA |