A0A974HAG9 · A0A974HAG9_XENLA
- ProteinArf-GAP with coiled-coil, ANK repeat and PH domain-containing protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids867 (go to sequence)
- Protein existencePredicted
- Annotation score2/5
Function
function
GTPase-activating protein for the ADP ribosylation factor family.
Activity regulation
GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid.
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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Aspect | Term | |
---|---|---|
Cellular Component | endosome membrane | |
Molecular Function | GTPase activator activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameArf-GAP with coiled-coil, ANK repeat and PH domain-containing protein
- Short namesCnt-b
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionA0A974HAG9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endosome membrane ; Peripheral membrane protein
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 264-359 | PH | ||||
Sequence: GVVMEGYLFKRASNAFKTWNRRWFSIQNSQLVYQKKLKDVLTVVVEDLRLCTVKPCEDIERRFCFEVVSPSKSCMLQADSEKLRQSWIQAVQASIA | ||||||
Domain | 399-521 | Arf-GAP | ||||
Sequence: ESILQRVQSIAGNDQCCDCGQTDPRWASINLGITLCIECSGIHRSLGVHFSKVRSLTLDSWEPELLKLMCELGNSTINQIYEAKCEHLGLKKPTSGCSRQNKEIWIKAKYVEKKFLKRLGTVE | ||||||
Region | 537-564 | Disordered | ||||
Sequence: HRNNSTTKVPSTRRKFRHEMGSASPAML | ||||||
Region | 616-646 | Disordered | ||||
Sequence: TGSGAEPGGSAMPFLRDGGLSSDSGLGGSTD | ||||||
Compositional bias | 664-684 | Acidic residues | ||||
Sequence: EECEVSEDSSGEAETEQEPSD | ||||||
Region | 664-690 | Disordered | ||||
Sequence: EECEVSEDSSGEAETEQEPSDPEDLRE | ||||||
Repeat | 727-759 | ANK | ||||
Sequence: ESKTPLIQAVLGGSLIACEFLLQNGADVNQTDM | ||||||
Repeat | 760-792 | ANK | ||||
Sequence: RGRAPIHHATYLGHTGQVCLFLKRGANQHAVDE |
Domain
PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate protein binding to PIP2 or PIP3 containing membranes.
The BAR domain mediates homodimerization, it can neither bind membrane nor impart curvature, but instead requires the neighboring PH domain to achieve these functions.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length867
- Mass (Da)97,823
- Last updated2023-02-22 v1
- ChecksumECF4A6537B9A7D7B
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 664-684 | Acidic residues | ||||
Sequence: EECEVSEDSSGEAETEQEPSD |