A0A7L2ACG1 · A0A7L2ACG1_9GRUI
- ProteinTubulin alpha chain
- GeneTuba1b_0
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids395 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Catalytic activity
- GTP + H2O = GDP + H+ + phosphateThis reaction proceeds in the forward direction.
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | microtubule | |
Molecular Function | GTP binding | |
Molecular Function | hydrolase activity | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | mitotic cell cycle |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameTubulin alpha chain
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Gruiformes > Heliornithidae > Heliornis
Accessions
- Primary accessionA0A7L2ACG1
Proteomes
Subcellular Location
Interaction
Subunit
Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-196 | Tubulin/FtsZ GTPase | ||||
Sequence: TFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDG | ||||||
Domain | 198-343 | Tubulin/FtsZ 2-layer sandwich | ||||
Sequence: LNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDH |
Sequence similarities
Belongs to the tubulin family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length395
- Mass (Da)44,098
- Last updated2021-04-07 v1
- Checksum47CCD4B4543F15F1
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: T | ||||||
Non-terminal residue | 395 | |||||
Sequence: E |
Keywords
- Technical term