A0A644F0Y1 · TBG_GIAIC
- ProteinTubulin gamma chain
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids472 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tubulin is the major constituent of microtubules (Potential). The gamma chain is found at microtubule organizing centers (MTOC) such as the centrosome (PubMed:30318753).
Component of the gamma-tubulin small complex (gamma-TuSC) involved in microtubule nucleation for the formation of median bodies and in the biogenesis of flagella (PubMed:30318753).
Gamma-TuSC may be required for the correct positioning of EB1 within the trophozoites (PubMed:30318753).
Component of the gamma-tubulin small complex (gamma-TuSC) involved in microtubule nucleation for the formation of median bodies and in the biogenesis of flagella (PubMed:30318753).
Gamma-TuSC may be required for the correct positioning of EB1 within the trophozoites (PubMed:30318753).
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameTubulin gamma chain
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metamonada > Diplomonadida > Hexamitidae > Giardiinae > Giardia
Accessions
- Primary accessionA0A644F0Y1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes mainly to basal bodies of trophozoites during interface (PubMed:30318753).
Localizes as four dots at the basis of posterolateral and ventral flagellar pairs in interphase (PubMed:10928459).
Localizes also to axonemes and median body in over half of the interphase cells (PubMed:30318753).
Colocalizes with microtubules in the median bodies of the interphase cells (PubMed:30318753).
Localizes to basal bodies and median bodies in dividing stages of the trophozoites (PubMed:30318753).
The four dots are absent in late prophase and early metaphase, but reappear as tiny dots at the perikinetosomal areas of the separated parent flagella in anaphase (PubMed:10928459).
Localizes transiently to the centers of the mitotic spindles in anaphase (PubMed:30318753).
The four dots localize at the basal body regions of each daughter karyomastigont in telophase (PubMed:10928459).
Colocalizes with centrin outside the two nuclei in telophase (PubMed:30318753).
Localizes to basal bodies and axonemes of the two daughter cells during cytokinesis (PubMed:30318753).
Does not localize at the spindle poles of the dividing nuclei (PubMed:10928459).
Localizes as four dots at the basis of posterolateral and ventral flagellar pairs in interphase (PubMed:10928459).
Localizes also to axonemes and median body in over half of the interphase cells (PubMed:30318753).
Colocalizes with microtubules in the median bodies of the interphase cells (PubMed:30318753).
Localizes to basal bodies and median bodies in dividing stages of the trophozoites (PubMed:30318753).
The four dots are absent in late prophase and early metaphase, but reappear as tiny dots at the perikinetosomal areas of the separated parent flagella in anaphase (PubMed:10928459).
Localizes transiently to the centers of the mitotic spindles in anaphase (PubMed:30318753).
The four dots localize at the basal body regions of each daughter karyomastigont in telophase (PubMed:10928459).
Colocalizes with centrin outside the two nuclei in telophase (PubMed:30318753).
Localizes to basal bodies and axonemes of the two daughter cells during cytokinesis (PubMed:30318753).
Does not localize at the spindle poles of the dividing nuclei (PubMed:10928459).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Knockdown of expression by morpholino results in an arrest of cytokinesis, leading to reduced growth rate and increased number of cells with four nuclei. Knockdown has various defects including increased number of disorganized cells impertinent for cytokinesis and increased number of cells without furrow. However, knockdown does not have an effect on the number of cells defective in cytokinesis or abscission. Knockdown has reduced formation and volume of median bodies, increased number of posterolateral and ventral axonemes without central pair of flagellar microtubules (MTs), and reduced length of the caudal flagella. Knockdown does not affect central pair of flagellar MTs in anterior and caudal axonemes.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000459116 | 1-472 | Tubulin gamma chain | |||
Sequence: MPREVITIQCGQCGNQIGEVFWNRLCTEHGINPDGTLRPEAYTFNDRKDVFFYQSDDEHYVPRAILLDTEPGVISHIRNGPIKELINPENVYIDSTGGGAGNIWTKGFQCGEAGFEKIVEIIDREADGADSLAGFSLTHSIAGGTGSGMGSFLLDRLSDRYPKALLQTYSVFPNTTADIIVQPYNSILTLQRLALCADAVVVLDNTALDRIITNHIPNELLTNPFEHVNSLVSTVMAASTSTLRLPGFMSNDLLSLVSSLVPTPRLHFLMSSYTPITSSSLNVKEHTKDQEAGSGAVAGAAAGATRRQVHTDSIVQLVKRLLHPTNGMVSCGRDGKYISLLNIVQGEAESNQLYKSLQQIKEGRDVKFIDWGPSNMQMALSKRSPFTNEAHKVSGLMLANHTAIRKIFDNINNTFTQLFSKRAYLQNYIDSMVTGGEPEILEQFTDAQAVCTSLSKEYEAAESKDYLEYIGM |
Interaction
Subunit
Component of the gamma-tubulin small complex (gamma-TuSC) composed of tubulin gamma chain, gamma-tubulin complex protein 2 (GCP2) and gamma-tubulin complex protein 3 (GCP3) (PubMed:30318753).
Interacts with GCP2 and GCP3 (PubMed:30318753).
Interacts with EB1 (PubMed:30318753).
Interacts with GCP2 and GCP3 (PubMed:30318753).
Interacts with EB1 (PubMed:30318753).
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length472
- Mass (Da)51,870
- Last updated2020-04-22 v1
- ChecksumB5D2977F0EA7F4B3
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AACB02000033 EMBL· GenBank· DDBJ | EDO77838.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
AACB03000004 EMBL· GenBank· DDBJ | KAE8302020.1 EMBL· GenBank· DDBJ | Genomic DNA |