O88987 · AKAP3_MOUSE
- ProteinA-kinase anchor protein 3
- GeneAkap3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids864 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Structural component of sperm fibrous sheath (PubMed:31969357).
Required for the formation of the subcellular structure of the sperm flagellum, sperm motility and male fertility (PubMed:31969357).
Required for the formation of the subcellular structure of the sperm flagellum, sperm motility and male fertility (PubMed:31969357).
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 | acrosomal vesicle | |
Cellular Component | cytoplasm | |
Cellular Component | motile cilium | |
Cellular Component | sperm fibrous sheath | |
Cellular Component | sperm midpiece | |
Cellular Component | sperm principal piece | |
Molecular Function | protein kinase A binding | |
Biological Process | blastocyst hatching | |
Biological Process | cell surface receptor protein serine/threonine kinase signaling pathway | |
Biological Process | establishment of protein localization | |
Biological Process | flagellated sperm motility | |
Biological Process | protein localization |
Names & Taxonomy
Protein names
- Recommended nameA-kinase anchor protein 3
- Short namesAKAP-3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO88987
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Male mice are sterile due to sperm morphology abnormalities (PubMed:31969357).
The absence of Akap3 affects the integrity of sperm structure, causing mislocalizations of sperm proteins (PubMed:31969357).
The absence of Akap3 affects the integrity of sperm structure, causing mislocalizations of sperm proteins (PubMed:31969357).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 51 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000064527 | 1-864 | A-kinase anchor protein 3 | |||
Sequence: MADRVDWLQSQSGVCKVGVYSPGDNQHQDWKMDTSTDPVRVLSWLRKDLEKSTAGFQDSRFKPGESSFVEEVAYPVDQRKGFCVDYYNTTNKGSPGRLHFEMSHKENPSQGLISHVGNGGSIDEVSFYANRLTNLVIAMARKEINEKIHGAENKCVHQSLYMGDEPTPHKSLSTVASELVNETVTACSKNISSDKAPGSGDRASGSSQAPGLRYTSTLKIKESTKEGKCPDDKPGTKKSFFYKEVFESRNAGDAKEGGRSLPGDQKLFRTSPDNRPDDFSNSISQGIMTYANSVVSDMMVSIMKTLKIQVKDTTIATILLKKVLMKHAKEVVSDLIDSFMKNLHGVTGSLMTDTDFVSAVKRSFFSHGSQKATDIMDAMLGKLYNVMFAKKFPENIRRARDKSESYSLISTKSRAGDPKLSNLNFAMKSESKLKENLFSTCKLEKEKTCAETLGEHIIKEGLHMWHKSQQKSPGLERAAKLGNAPQEVSFECPDPCEANPPHQPQPPENFANFMCDSDSWAKDLIVSALLLIQYHLAQGGKMDAQSFLEAAASTNFPTNKPPPPSPVVQDECKLKSPPHKICDQEQTEKKDLMSVIFNFIRNLLSETIFKSSRNCESNVHEQNTQEEEIHPCERPKTPCERPITPPAPKFCEDEEATGGALSGLTKMVANQLDNCMNGQMVEHLMDSVMKLCLIIAKSCDSPLSELGEEKCGDASRPNSAFPDNLYECLPVKGTGTAEALLQNAYLTIHNELRGLSGQPPEGCEIPKVIVSNHNLADTVQNKQLQAVLQWVAASELNVPILYFAGDDEGIQEKLLQLSATAVEKGRSVGEVLQSVLRYEKERQLDEAVGNVTRLQLLDWLMANL | ||||||
Modified residue | 12 | Phosphoserine; by STK33 | ||||
Sequence: S | ||||||
Modified residue | 206 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 405 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 406 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Phosphorylated by STK33 during sperm flagella assembly (PubMed:37146716).
Phosphorylated on tyrosine (By similarity).
Phosphorylated on tyrosine (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with ROPN1 and ROPN1L. Interacts with QRICH2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O88987 | Brap Q99MP8 | 3 | EBI-9033539, EBI-10818333 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 125-138 | PKA-RII subunit binding domain | ||||
Sequence: VSFYANRLTNLVIA | ||||||
Compositional bias | 190-218 | Polar residues | ||||
Sequence: NISSDKAPGSGDRASGSSQAPGLRYTSTL | ||||||
Region | 190-235 | Disordered | ||||
Sequence: NISSDKAPGSGDRASGSSQAPGLRYTSTLKIKESTKEGKCPDDKPG | ||||||
Compositional bias | 219-235 | Basic and acidic residues | ||||
Sequence: KIKESTKEGKCPDDKPG | ||||||
Region | 251-281 | Disordered | ||||
Sequence: AGDAKEGGRSLPGDQKLFRTSPDNRPDDFSN | ||||||
Region | 619-638 | Disordered | ||||
Sequence: VHEQNTQEEEIHPCERPKTP | ||||||
Compositional bias | 620-637 | Basic and acidic residues | ||||
Sequence: HEQNTQEEEIHPCERPKT |
Domain
RII-binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.
Sequence similarities
Belongs to the AKAP110 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length864
- Mass (Da)95,556
- Last updated2011-06-28 v2
- Checksum3E24E63327BC4E78
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 190-218 | Polar residues | ||||
Sequence: NISSDKAPGSGDRASGSSQAPGLRYTSTL | ||||||
Sequence conflict | 215 | in Ref. 1; AAC63369 | ||||
Sequence: T → M | ||||||
Compositional bias | 219-235 | Basic and acidic residues | ||||
Sequence: KIKESTKEGKCPDDKPG | ||||||
Compositional bias | 620-637 | Basic and acidic residues | ||||
Sequence: HEQNTQEEEIHPCERPKT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF093406 EMBL· GenBank· DDBJ | AAC63369.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466523 EMBL· GenBank· DDBJ | EDK99845.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC100458 EMBL· GenBank· DDBJ | AAI00459.1 EMBL· GenBank· DDBJ | mRNA |