A0A9D3X688 · A0A9D3X688_9SAUR
- ProteinSpastin
- GeneSPAST
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids620 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. Also plays a role in axon growth and the formation of axonal branches.
Catalytic activity
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | centrosome | |
Cellular Component | membrane | |
Cellular Component | microtubule | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
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 | axonogenesis | |
Biological Process | cytokinetic process | |
Biological Process | endoplasmic reticulum to Golgi vesicle-mediated transport | |
Biological Process | microtubule severing | |
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 > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Testudinata > Testudines > Cryptodira > Durocryptodira > Testudinoidea > Geoemydidae > Geoemydinae > Mauremys
Accessions
- Primary accessionA0A9D3X688
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, intramembrane, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-65 | Cytoplasmic | ||||
Sequence: MNSPGGRGKKKGSAGSSSPPQVPGASPSSPAGPAPPLQQQQQQQAAAGAAAASPHKRNLYYFSYP | ||||||
Intramembrane | 66-86 | Helical | ||||
Sequence: LFAAFALLRFVAFQLGLLFAW | ||||||
Transmembrane | 66-87 | Helical | ||||
Sequence: LFAAFALLRFVAFQLGLLFAWL | ||||||
Topological domain | 87-620 | Cytoplasmic | ||||
Sequence: LCERLSRGALMAAKGRAGAGDAPEPGGAPETVRACHKRAFECISVALRIDEEERAGQKEQAVEWYKKGIEELEKGIAVLVIGQGDQCERARRLQSKMMTNLAMAKDRLQLLEKLQAVLQIPKPQMEVYNDSTNLACRNGHLQSECGAVPKKKDPLAHTSNSLPRSKTVAVAKTGSTGLSGHHRTPSYSGISTFSVSRQGVNPATSTHKATSKNSRTNKPSTPTTAARKKKDLKIFRNVDSNLANLILNEIVDNGPAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPPRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSSGEDRILVMGATNRPQELDDAVLRRFTKRVYVSLPNEETRLILLKNLLSKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSLSPQTLDAYIRWNKDFGDTTV |
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 region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-49 | Disordered | ||||
Sequence: MNSPGGRGKKKGSAGSSSPPQVPGASPSSPAGPAPPLQQQQQQQAAAGA | ||||||
Domain | 118-196 | MIT | ||||
Sequence: VRACHKRAFECISVALRIDEEERAGQKEQAVEWYKKGIEELEKGIAVLVIGQGDQCERARRLQSKMMTNLAMAKDRLQL | ||||||
Region | 233-254 | Disordered | ||||
Sequence: AVPKKKDPLAHTSNSLPRSKTV | ||||||
Compositional bias | 282-309 | Polar residues | ||||
Sequence: SRQGVNPATSTHKATSKNSRTNKPSTPT | ||||||
Region | 282-314 | Disordered | ||||
Sequence: SRQGVNPATSTHKATSKNSRTNKPSTPTTAARK | ||||||
Domain | 378-514 | AAA+ ATPase | ||||
Sequence: PPRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSSGEDRILVMGATNRPQELDDAVLRRFTKRVYVSLPN |
Sequence similarities
Belongs to the AAA ATPase family. Spastin subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length620
- Mass (Da)67,409
- Last updated2023-05-03 v1
- Checksum849E42CC284B0BC6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 282-309 | Polar residues | ||||
Sequence: SRQGVNPATSTHKATSKNSRTNKPSTPT |
Keywords
- Technical term