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Protein

ATP-dependent RNA helicase vasa, isoform A

Gene

vas

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.11 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Cofactori

Mg2+1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi289 – 2968ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: UniProtKB
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • multicellular organism development Source: UniProtKB-KW
  • oogenesis Source: UniProtKB-KW
  • protein localization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Helicase, Hydrolase

Keywords - Biological processi

Differentiation, Oogenesis

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase vasa, isoform A (EC:3.6.4.13)
Alternative name(s):
Antigen Mab46F11
Gene namesi
Name:vas
ORF Names:CG3506
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0262526. vas.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Defective growth of germline cysts. Fails to efficiently accumulate many localized RNAs, such as Bic-D, orb, osk and nos, but still accumulates grk RNA.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi184 – 1885DINNN → AAAAA: Enhances protein stability. Does not affect protein distribution in the oocyte. 1 Publication
Mutagenesisi184 – 1841D → A: Decreases interaction with gus. 2 Publications
Mutagenesisi185 – 1851I → A: Decreases interaction with gus. 1 Publication
Mutagenesisi186 – 1894NNNN → ANNA: Strongly decreases interaction with gus. 1 Publication
Mutagenesisi186 – 1883NNN → AAA: Abolishes interaction with gus. 1 Publication
Mutagenesisi187 – 1871N → A: Strongly decreases interaction with gus. 2 Publications
Mutagenesisi188 – 1881N → A: Strongly decreases interaction with gus. 2 Publications
Mutagenesisi189 – 1891N → A: Does not affect interaction with gus. 2 Publications
Mutagenesisi256 – 2561I → N: Fails to bind and unwind RNA. 1 Publication
Mutagenesisi271 – 2711I → M: Fails to bind and unwind RNA. 1 Publication
Mutagenesisi328 – 3281R → A: Reduction in RNA-binding, reduced RNA-dependent ATPase and unwinding activities. 1 Publication
Mutagenesisi329 – 3291E → A: Increase in RNA-binding and no significant change to RNA-dependent ATPase or unwinding activities. 1 Publication
Mutagenesisi333 – 3331Q → A: Reduction in RNA-binding, drastic reduction in unwinding activities, no significant change to RNA-dependent ATPase activity. 1 Publication
Mutagenesisi378 – 3781R → A: Reduction in RNA-binding, significantly reduced RNA-dependent ATPase and unwinding activities. 1 Publication
Mutagenesisi381 – 3811D → A: Increase in RNA-binding. 1 Publication
Mutagenesisi525 – 5251Q → A: Reduction in RNA-binding, abolished unwinding activities and no significant change to RNA-dependent ATPase activity. 1 Publication
Mutagenesisi528 – 5281R → A: Reduction in RNA-binding, barely detectable RNA-dependent ATPase activity and completely defective unwinding activity. 1 Publication
Mutagenesisi546 – 5461T → A: Moderately decreased the RNA binding, abolished both the RNA-dependent ATPase and unwinding activities. 1 Publication
Mutagenesisi551 – 5511R → A: Reduction in RNA-binding, drastic reduction in unwinding activities and no significant change to RNA-dependent ATPase activity. 1 Publication
Mutagenesisi552 – 5521G → E: Fails to unwind RNA. 1 Publication
Mutagenesisi554 – 5541D → A: No change to RNA-binding, abolished unwinding activities and no significant change to RNA-dependent ATPase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 661661ATP-dependent RNA helicase vasa, isoform APRO_0000054976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Phosphoserine1 Publication
Modified residuei27 – 271Phosphothreonine1 Publication

Post-translational modificationi

Ubiquitinated during oogenesis. Deubiquitinated by faf, which protects this protein from proteasome-mediated degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

PTM databases

iPTMnetiP09052.

Expressioni

Tissue specificityi

Abundantly expressed in the female germline. Gus and faf are required for vas expression in the posterior pole of the oocyte.5 Publications

Developmental stagei

Expressed both maternally and zygotically.3 Publications

Gene expression databases

BgeeiFBgn0262526.
ExpressionAtlasiP09052. differential.

Interactioni

Subunit structurei

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FsnQ9V6L92EBI-134067,EBI-126933
gusA1Z6E05EBI-134067,EBI-75338
SPSB1Q96BD62EBI-134067,EBI-2659201From a different organism.
SPSB2Q996192EBI-134067,EBI-2323209From a different organism.

Protein-protein interaction databases

BioGridi60902. 12 interactions.
DIPiDIP-20604N.
IntActiP09052. 9 interactions.
MINTiMINT-970294.

Structurei

Secondary structure

1
661
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi189 – 1924Combined sources
Helixi195 – 1995Combined sources
Helixi211 – 2144Combined sources
Helixi225 – 2306Combined sources
Beta strandi233 – 2397Combined sources
Helixi247 – 2493Combined sources
Helixi254 – 2629Combined sources
Helixi270 – 28011Combined sources
Beta strandi285 – 2884Combined sources
Helixi295 – 30915Combined sources
Beta strandi320 – 3245Combined sources
Helixi328 – 34114Combined sources
Turni342 – 3443Combined sources
Helixi358 – 3658Combined sources
Beta strandi370 – 3745Combined sources
Helixi376 – 3849Combined sources
Beta strandi395 – 3995Combined sources
Helixi401 – 4044Combined sources
Turni407 – 4093Combined sources
Helixi410 – 4189Combined sources
Beta strandi427 – 4337Combined sources
Helixi437 – 4448Combined sources
Beta strandi451 – 4577Combined sources
Beta strandi465 – 4717Combined sources
Helixi474 – 4763Combined sources
Helixi477 – 48711Combined sources
Beta strandi492 – 4954Combined sources
Helixi499 – 51113Combined sources
Beta strandi516 – 5205Combined sources
Helixi525 – 53612Combined sources
Beta strandi541 – 5455Combined sources
Helixi547 – 5493Combined sources
Beta strandi560 – 5656Combined sources
Helixi570 – 5778Combined sources
Beta strandi587 – 5937Combined sources
Turni595 – 5973Combined sources
Helixi599 – 6013Combined sources
Helixi602 – 61110Combined sources
Helixi618 – 6203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DB3X-ray2.20A/B/C/D200-623[»]
2IHSX-ray2.20C/D184-203[»]
3EMWX-ray1.80B184-203[»]
3F2OX-ray2.05C/D184-203[»]
ProteinModelPortaliP09052.
SMRiP09052. Positions 202-621.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09052.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati93 – 9971
Repeati100 – 10672
Repeati107 – 11373
Repeati114 – 12074
Repeati121 – 12775
Domaini276 – 453178Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini477 – 624148Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 127355 X 7 AA tandem repeats of [FS]-R-G-G-[EQ]-G-GAdd
BLAST
Regioni184 – 20320Required for posterior localization in oocyteAdd
BLAST
Regioni184 – 1885Gus binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi245 – 27329Q motifAdd
BLAST
Motifi399 – 4024DEAD box

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

OMAiKQTIYEV.
OrthoDBiEOG091G03JV.
PhylomeDBiP09052.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P09052-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSDDWDDEPI VDTRGARGGD WSDDEDTAKS FSGEAEGDGV GGSGGEGGGY
60 70 80 90 100
QGGNRDVFGR IGGGRGGGAG GYRGGNRDGG GFHGGRREGE RDFRGGEGGF
110 120 130 140 150
RGGQGGSRGG QGGSRGGQGG FRGGEGGFRG RLYENEDGDE RRGRLDREER
160 170 180 190 200
GGERRGRLDR EERGGERGER GDGGFARRRR NEDDINNNNN IVEDVERKRE
210 220 230 240 250
FYIPPEPSND AIEIFSSGIA SGIHFSKYNN IPVKVTGSDV PQPIQHFTSA
260 270 280 290 300
DLRDIIIDNV NKSGYKIPTP IQKCSIPVIS SGRDLMACAQ TGSGKTAAFL
310 320 330 340 350
LPILSKLLED PHELELGRPQ VVIVSPTREL AIQIFNEARK FAFESYLKIG
360 370 380 390 400
IVYGGTSFRH QNECITRGCH VVIATPGRLL DFVDRTFITF EDTRFVVLDE
410 420 430 440 450
ADRMLDMGFS EDMRRIMTHV TMRPEHQTLM FSATFPEEIQ RMAGEFLKNY
460 470 480 490 500
VFVAIGIVGG ACSDVKQTIY EVNKYAKRSK LIEILSEQAD GTIVFVETKR
510 520 530 540 550
GADFLASFLS EKEFPTTSIH GDRLQSQREQ ALRDFKNGSM KVLIATSVAS
560 570 580 590 600
RGLDIKNIKH VINYDMPSKI DDYVHRIGRT GRVGNNGRAT SFFDPEKDRA
610 620 630 640 650
IAADLVKILE GSGQTVPDFL RTCGAGGDGG YSNQNFGGVD VRGRGNYVGD
660
ATNVEEEEQW D
Length:661
Mass (Da):72,331
Last modified:December 1, 2000 - v3
Checksum:i8617C25CCB3130B9
GO
Isoform solo (identifier: B6JUP5-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry B6JUP5.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:1,031
Mass (Da):112,515
GO

Sequence cautioni

The sequence AAL89864 differs from that shown. Reason: Frameshift at position 50. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351A → R in AAA29013 (PubMed:3052853).Curated
Sequence conflicti153 – 16513Missing in AAA29013 (PubMed:3052853).CuratedAdd
BLAST
Sequence conflicti192 – 1921V → A in CAA31405 (PubMed:3140040).Curated
Sequence conflicti192 – 1921V → A in AAA29013 (PubMed:3052853).Curated
Sequence conflicti265 – 2651Y → F in CAA31405 (PubMed:3140040).Curated
Sequence conflicti322 – 3221V → C in AAA29013 (PubMed:3052853).Curated
Sequence conflicti452 – 4521F → S in CAA31405 (PubMed:3140040).Curated
Sequence conflicti582 – 5821R → C in CAA31405 (PubMed:3140040).Curated
Sequence conflicti594 – 5941D → H in AAA29013 (PubMed:3052853).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12945, X12946 Genomic DNA. Translation: CAA31405.1.
M23560 mRNA. Translation: AAA29013.1.
AE014134 Genomic DNA. Translation: AAF53438.1.
AY084126 mRNA. Translation: AAL89864.1. Frameshift.
PIRiA58768.
RefSeqiNP_001260458.1. NM_001273529.2. [P09052-1]
NP_001303322.1. NM_001316393.1. [P09052-1]
NP_723899.1. NM_165103.3. [P09052-1]
UniGeneiDm.4715.

Genome annotation databases

EnsemblMetazoaiFBtr0304854; FBpp0293394; FBgn0262526. [P09052-1]
FBtr0332472; FBpp0304748; FBgn0262526. [P09052-1]
GeneIDi26067080.
KEGGidme:Dmel_CG46283.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12945, X12946 Genomic DNA. Translation: CAA31405.1.
M23560 mRNA. Translation: AAA29013.1.
AE014134 Genomic DNA. Translation: AAF53438.1.
AY084126 mRNA. Translation: AAL89864.1. Frameshift.
PIRiA58768.
RefSeqiNP_001260458.1. NM_001273529.2. [P09052-1]
NP_001303322.1. NM_001316393.1. [P09052-1]
NP_723899.1. NM_165103.3. [P09052-1]
UniGeneiDm.4715.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DB3X-ray2.20A/B/C/D200-623[»]
2IHSX-ray2.20C/D184-203[»]
3EMWX-ray1.80B184-203[»]
3F2OX-ray2.05C/D184-203[»]
ProteinModelPortaliP09052.
SMRiP09052. Positions 202-621.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60902. 12 interactions.
DIPiDIP-20604N.
IntActiP09052. 9 interactions.
MINTiMINT-970294.

PTM databases

iPTMnetiP09052.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0304854; FBpp0293394; FBgn0262526. [P09052-1]
FBtr0332472; FBpp0304748; FBgn0262526. [P09052-1]
GeneIDi26067080.
KEGGidme:Dmel_CG46283.

Organism-specific databases

CTDi26067080.
FlyBaseiFBgn0262526. vas.

Phylogenomic databases

OMAiKQTIYEV.
OrthoDBiEOG091G03JV.
PhylomeDBiP09052.

Miscellaneous databases

ChiTaRSivas. fly.
EvolutionaryTraceiP09052.

Gene expression databases

BgeeiFBgn0262526.
ExpressionAtlasiP09052. differential.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVASA1_DROME
AccessioniPrimary (citable) accession number: P09052
Secondary accession number(s): Q24582, Q8SXU8, Q9V3Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: December 1, 2000
Last modified: September 7, 2016
This is version 170 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.