P09052 · VASA1_DROME
- ProteinATP-dependent RNA helicase vasa
- Genevas
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids661 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in translational control mechanisms operating in early stages of oogenesis. Required maternally in many stages of oogenesis, including cystocyte differentiation, oocyte differentiation, and specification of anterior-posterior polarity in the developing cysts. Essential for the formation and/or structural integrity of perinuclear nuage particles during germ cell formation. Required for gus, Fsn and aub accumulation at the posterior pole of the embryo. Required for the localization of vas to the perinuclear region of nurse cells. May have a role in production of piwi-interacting RNA (piRNA) (PubMed:17428915).
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | germ cell nucleus | |
Cellular Component | nucleus | |
Cellular Component | P granule | |
Cellular Component | posterior cell cortex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | mRNA binding | |
Molecular Function | RNA helicase activity | |
Biological Process | cell differentiation | |
Biological Process | gamete generation | |
Biological Process | germ cell development | |
Biological Process | oogenesis | |
Biological Process | protein localization | |
Biological Process | secondary piRNA processing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent RNA helicase vasa
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP09052
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Component of the perinuclear meiotic nuage (also known as germline granule or P granule), a germline-specific membraneless ribonucleoprotein biocondensate involved in post-transcriptional regulation of transposons and mRNAs (PubMed:14588248, PubMed:17428915, PubMed:26295961, PubMed:28945271, PubMed:3052853, PubMed:8026330).
Localization to the nuage is dependent on spn-E (PubMed:17428915).
During late stages of oogenesis seen in the pole plasm at the posterior end of the oocyte (PubMed:14588248, PubMed:17428915, PubMed:28945271, PubMed:8026330).
Localization to the nuage is dependent on spn-E (PubMed:17428915).
During late stages of oogenesis seen in the pole plasm at the posterior end of the oocyte (PubMed:14588248, PubMed:17428915, PubMed:28945271, PubMed:8026330).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Defective growth of germline cysts. Fails to efficiently accumulate many localized RNAs, such as Bic-D, orb, osk and nanos (nos), but still accumulates grk RNA.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 184 | Decreases interaction with gus. | ||||
Sequence: D → A | ||||||
Mutagenesis | 184-188 | Enhances protein stability. Does not affect protein distribution in the oocyte. | ||||
Sequence: DINNN → AAAAA | ||||||
Mutagenesis | 185 | Decreases interaction with gus. | ||||
Sequence: I → A | ||||||
Mutagenesis | 186-188 | Abolishes interaction with gus. | ||||
Sequence: NNN → AAA | ||||||
Mutagenesis | 186-189 | Strongly decreases interaction with gus. | ||||
Sequence: NNNN → ANNA | ||||||
Mutagenesis | 187 | Strongly decreases interaction with gus. | ||||
Sequence: N → A | ||||||
Mutagenesis | 188 | Strongly decreases interaction with gus. | ||||
Sequence: N → A | ||||||
Mutagenesis | 189 | Does not affect interaction with gus. | ||||
Sequence: N → A | ||||||
Mutagenesis | 256 | Fails to bind and unwind RNA. | ||||
Sequence: I → N | ||||||
Mutagenesis | 271 | Fails to bind and unwind RNA. | ||||
Sequence: I → M | ||||||
Mutagenesis | 328 | Reduction in RNA-binding, reduced RNA-dependent ATPase and unwinding activities. | ||||
Sequence: R → A | ||||||
Mutagenesis | 329 | Increase in RNA-binding and no significant change to RNA-dependent ATPase or unwinding activities. | ||||
Sequence: E → A | ||||||
Mutagenesis | 333 | Reduction in RNA-binding, drastic reduction in unwinding activities, no significant change to RNA-dependent ATPase activity. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 378 | Reduction in RNA-binding, significantly reduced RNA-dependent ATPase and unwinding activities. | ||||
Sequence: R → A | ||||||
Mutagenesis | 381 | Increase in RNA-binding. | ||||
Sequence: D → A | ||||||
Mutagenesis | 525 | Reduction in RNA-binding, abolished unwinding activities and no significant change to RNA-dependent ATPase activity. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 528 | Reduction in RNA-binding, barely detectable RNA-dependent ATPase activity and completely defective unwinding activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 546 | Moderately decreased the RNA binding, abolished both the RNA-dependent ATPase and unwinding activities. | ||||
Sequence: T → A | ||||||
Mutagenesis | 551 | Reduction in RNA-binding, drastic reduction in unwinding activities and no significant change to RNA-dependent ATPase activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 552 | Fails to unwind RNA. | ||||
Sequence: G → E | ||||||
Mutagenesis | 554 | No change to RNA-binding, abolished unwinding activities and no significant change to RNA-dependent ATPase activity. | ||||
Sequence: D → A |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000054976 | 1-661 | ATP-dependent RNA helicase vasa | |||
Sequence: MSDDWDDEPIVDTRGARGGDWSDDEDTAKSFSGEAEGDGVGGSGGEGGGYQGGNRDVFGRIGGGRGGGAGGYRGGNRDGGGFHGGRREGERDFRGGEGGFRGGQGGSRGGQGGSRGGQGGFRGGEGGFRGRLYENEDGDERRGRLDREERGGERRGRLDREERGGERGERGDGGFARRRRNEDDINNNNNIVEDVERKREFYIPPEPSNDAIEIFSSGIASGIHFSKYNNIPVKVTGSDVPQPIQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGRPQVVIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMRRIMTHVTMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFVAIGIVGGACSDVKQTIYEVNKYAKRSKLIEILSEQADGTIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIKNIKHVINYDMPSKIDDYVHRIGRTGRVGNNGRATSFFDPEKDRAIAADLVKILEGSGQTVPDFLRTCGAGGDGGYSNQNFGGVDVRGRGNYVGDATNVEEEEQWD | ||||||
Modified residue | 22 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 27 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Ubiquitinated during oogenesis. Deubiquitinated by faf, which protects this protein from proteasome-mediated degradation.
Keywords
- PTM
PTM databases
Expression
Tissue specificity
Abundantly expressed in the female germline (PubMed:12479811, PubMed:14588248, PubMed:17428915, PubMed:3052853, PubMed:3140040, PubMed:9521895).
Gus and faf are required for vas expression in the posterior pole of the oocyte
Gus and faf are required for vas expression in the posterior pole of the oocyte
Developmental stage
Expressed both maternally and zygotically.
Gene expression databases
Interaction
Subunit
Interacts with eIF5B and faf. Interacts with gus (via B30.2/SPRY domain) and Fsn (via B30.2/SPRY domain). Interacts with aub, me31B, eIF-4a and TER94. Interacts with piwi; this interaction is RNA independent. Interacts with Dcr-1 and Fmr1; these interactions occur in the polar granules.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P09052 | Fsn Q9V6L9 | 2 | EBI-134067, EBI-126933 | |
BINARY | P09052 | gus A1Z6E0 | 5 | EBI-134067, EBI-75338 | |
XENO | P09052 | SPSB1 Q96BD6 | 2 | EBI-134067, EBI-2659201 | |
XENO | P09052 | SPSB2 Q99619 | 2 | EBI-134067, EBI-2323209 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-186 | Disordered | ||||
Sequence: MSDDWDDEPIVDTRGARGGDWSDDEDTAKSFSGEAEGDGVGGSGGEGGGYQGGNRDVFGRIGGGRGGGAGGYRGGNRDGGGFHGGRREGERDFRGGEGGFRGGQGGSRGGQGGSRGGQGGFRGGEGGFRGRLYENEDGDERRGRLDREERGGERRGRLDREERGGERGERGDGGFARRRRNEDDIN | ||||||
Compositional bias | 7-32 | Basic and acidic residues | ||||
Sequence: DEPIVDTRGARGGDWSDDEDTAKSFS | ||||||
Compositional bias | 80-97 | Basic and acidic residues | ||||
Sequence: GGFHGGRREGERDFRGGE | ||||||
Repeat | 93-99 | 1 | ||||
Sequence: FRGGEGG | ||||||
Region | 93-127 | 5 X 7 AA tandem repeats of [FS]-R-G-G-[EQ]-G-G | ||||
Sequence: FRGGEGGFRGGQGGSRGGQGGSRGGQGGFRGGEGG | ||||||
Repeat | 100-106 | 2 | ||||
Sequence: FRGGQGG | ||||||
Repeat | 107-113 | 3 | ||||
Sequence: SRGGQGG | ||||||
Repeat | 114-120 | 4 | ||||
Sequence: SRGGQGG | ||||||
Repeat | 121-127 | 5 | ||||
Sequence: FRGGEGG | ||||||
Compositional bias | 129-186 | Basic and acidic residues | ||||
Sequence: RGRLYENEDGDERRGRLDREERGGERRGRLDREERGGERGERGDGGFARRRRNEDDIN | ||||||
Motif | 184-188 | B30.2/SPRY domain-binding motif | ||||
Sequence: DINNN | ||||||
Region | 184-203 | Required for posterior localization in oocyte | ||||
Sequence: DINNNNNIVEDVERKREFYI | ||||||
Motif | 245-273 | Q motif | ||||
Sequence: QHFTSADLRDIIIDNVNKSGYKIPTPIQK | ||||||
Domain | 276-453 | Helicase ATP-binding | ||||
Sequence: IPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGRPQVVIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMRRIMTHVTMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFV | ||||||
Motif | 399-402 | DEAD box | ||||
Sequence: DEAD | ||||||
Domain | 477-624 | Helicase C-terminal | ||||
Sequence: KRSKLIEILSEQADGTIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIKNIKHVINYDMPSKIDDYVHRIGRTGRVGNNGRATSFFDPEKDRAIAADLVKILEGSGQTVPDFLRTCG |
Domain
The B30.2/SPRY domain-binding motif mediates recognition by proteins containing a B30.2/SPRY domain.
Sequence similarities
Belongs to the DEAD box helicase family. DDX4/VASA subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P09052-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Namevas
- SynonymsA
- Length661
- Mass (Da)72,331
- Last updated2000-12-01 v3
- Checksum8617C25CCB3130B9
B6JUP5-1
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- Namesolo
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M9PBB5 | M9PBB5_DROME | vas | 661 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 7-32 | Basic and acidic residues | ||||
Sequence: DEPIVDTRGARGGDWSDDEDTAKSFS | ||||||
Sequence conflict | 35 | in Ref. 3; AAA29013 | ||||
Sequence: A → R | ||||||
Compositional bias | 80-97 | Basic and acidic residues | ||||
Sequence: GGFHGGRREGERDFRGGE | ||||||
Compositional bias | 129-186 | Basic and acidic residues | ||||
Sequence: RGRLYENEDGDERRGRLDREERGGERRGRLDREERGGERGERGDGGFARRRRNEDDIN | ||||||
Sequence conflict | 153-165 | in Ref. 3; AAA29013 | ||||
Sequence: Missing | ||||||
Sequence conflict | 192 | in Ref. 1; CAA31405 and 3; AAA29013 | ||||
Sequence: V → A | ||||||
Sequence conflict | 265 | in Ref. 1; CAA31405 | ||||
Sequence: Y → F | ||||||
Sequence conflict | 322 | in Ref. 3; AAA29013 | ||||
Sequence: V → C | ||||||
Sequence conflict | 452 | in Ref. 1; CAA31405 | ||||
Sequence: F → S | ||||||
Sequence conflict | 582 | in Ref. 1; CAA31405 | ||||
Sequence: R → C | ||||||
Sequence conflict | 594 | in Ref. 3; AAA29013 | ||||
Sequence: D → H |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X12945 EMBL· GenBank· DDBJ | CAA31405.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X12946 EMBL· GenBank· DDBJ | CAA31405.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M23560 EMBL· GenBank· DDBJ | AAA29013.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014134 EMBL· GenBank· DDBJ | AAF53438.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY084126 EMBL· GenBank· DDBJ | AAL89864.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |