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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi289 – 296ATPPROSITE-ProRule annotation8

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)DescriptionActionsGraphical viewLength
Mutagenesisi184 – 188DINNN → AAAAA: Enhances protein stability. Does not affect protein distribution in the oocyte. 1 Publication5
Mutagenesisi184D → A: Decreases interaction with gus. 2 Publications1
Mutagenesisi185I → A: Decreases interaction with gus. 1 Publication1
Mutagenesisi186 – 189NNNN → ANNA: Strongly decreases interaction with gus. 1 Publication4
Mutagenesisi186 – 188NNN → AAA: Abolishes interaction with gus. 1 Publication3
Mutagenesisi187N → A: Strongly decreases interaction with gus. 2 Publications1
Mutagenesisi188N → A: Strongly decreases interaction with gus. 2 Publications1
Mutagenesisi189N → A: Does not affect interaction with gus. 2 Publications1
Mutagenesisi256I → N: Fails to bind and unwind RNA. 1 Publication1
Mutagenesisi271I → M: Fails to bind and unwind RNA. 1 Publication1
Mutagenesisi328R → A: Reduction in RNA-binding, reduced RNA-dependent ATPase and unwinding activities. 1 Publication1
Mutagenesisi329E → A: Increase in RNA-binding and no significant change to RNA-dependent ATPase or unwinding activities. 1 Publication1
Mutagenesisi333Q → A: Reduction in RNA-binding, drastic reduction in unwinding activities, no significant change to RNA-dependent ATPase activity. 1 Publication1
Mutagenesisi378R → A: Reduction in RNA-binding, significantly reduced RNA-dependent ATPase and unwinding activities. 1 Publication1
Mutagenesisi381D → A: Increase in RNA-binding. 1 Publication1
Mutagenesisi525Q → A: Reduction in RNA-binding, abolished unwinding activities and no significant change to RNA-dependent ATPase activity. 1 Publication1
Mutagenesisi528R → A: Reduction in RNA-binding, barely detectable RNA-dependent ATPase activity and completely defective unwinding activity. 1 Publication1
Mutagenesisi546T → A: Moderately decreased the RNA binding, abolished both the RNA-dependent ATPase and unwinding activities. 1 Publication1
Mutagenesisi551R → A: Reduction in RNA-binding, drastic reduction in unwinding activities and no significant change to RNA-dependent ATPase activity. 1 Publication1
Mutagenesisi552G → E: Fails to unwind RNA. 1 Publication1
Mutagenesisi554D → A: No change to RNA-binding, abolished unwinding activities and no significant change to RNA-dependent ATPase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000549761 – 661ATP-dependent RNA helicase vasa, isoform AAdd BLAST661

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei22Phosphoserine1 Publication1
Modified residuei27Phosphothreonine1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP09052.

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. baseline.

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 interactors.
DIPiDIP-20604N.
IntActiP09052. 9 interactors.
MINTiMINT-970294.

Structurei

Secondary structure

1661
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi189 – 192Combined sources4
Helixi195 – 199Combined sources5
Helixi211 – 214Combined sources4
Helixi225 – 230Combined sources6
Beta strandi233 – 239Combined sources7
Helixi247 – 249Combined sources3
Helixi254 – 262Combined sources9
Helixi270 – 280Combined sources11
Beta strandi285 – 288Combined sources4
Helixi295 – 309Combined sources15
Beta strandi320 – 324Combined sources5
Helixi328 – 341Combined sources14
Turni342 – 344Combined sources3
Helixi358 – 365Combined sources8
Beta strandi370 – 374Combined sources5
Helixi376 – 384Combined sources9
Beta strandi395 – 399Combined sources5
Helixi401 – 404Combined sources4
Turni407 – 409Combined sources3
Helixi410 – 418Combined sources9
Beta strandi427 – 433Combined sources7
Helixi437 – 444Combined sources8
Beta strandi451 – 457Combined sources7
Beta strandi465 – 471Combined sources7
Helixi474 – 476Combined sources3
Helixi477 – 487Combined sources11
Beta strandi492 – 495Combined sources4
Helixi499 – 511Combined sources13
Beta strandi516 – 520Combined sources5
Helixi525 – 536Combined sources12
Beta strandi541 – 545Combined sources5
Helixi547 – 549Combined sources3
Beta strandi560 – 565Combined sources6
Helixi570 – 577Combined sources8
Beta strandi587 – 593Combined sources7
Turni595 – 597Combined sources3
Helixi599 – 601Combined sources3
Helixi602 – 611Combined sources10
Helixi618 – 620Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09052.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati93 – 9917
Repeati100 – 10627
Repeati107 – 11337
Repeati114 – 12047
Repeati121 – 12757
Domaini276 – 453Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST178
Domaini477 – 624Helicase C-terminalPROSITE-ProRule annotationAdd BLAST148

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni93 – 1275 X 7 AA tandem repeats of [FS]-R-G-G-[EQ]-G-GAdd BLAST35
Regioni184 – 203Required for posterior localization in oocyteAdd BLAST20
Regioni184 – 188Gus binding5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi245 – 273Q motifAdd BLAST29
Motifi399 – 402DEAD box4

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)DescriptionActionsGraphical viewLength
Sequence conflicti35A → R in AAA29013 (PubMed:3052853).Curated1
Sequence conflicti153 – 165Missing in AAA29013 (PubMed:3052853).CuratedAdd BLAST13
Sequence conflicti192V → A in CAA31405 (PubMed:3140040).Curated1
Sequence conflicti192V → A in AAA29013 (PubMed:3052853).Curated1
Sequence conflicti265Y → F in CAA31405 (PubMed:3140040).Curated1
Sequence conflicti322V → C in AAA29013 (PubMed:3052853).Curated1
Sequence conflicti452F → S in CAA31405 (PubMed:3140040).Curated1
Sequence conflicti582R → C in CAA31405 (PubMed:3140040).Curated1
Sequence conflicti594D → H in AAA29013 (PubMed:3052853).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP09052.

Proteomic databases

PRIDEiP09052.

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. baseline.

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: November 30, 2016
This is version 173 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.