VASA1_DROME
ID VASA1_DROME Reviewed; 661 AA.
AC P09052; Q24582; Q8SXU8; Q9V3Q8;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=ATP-dependent RNA helicase vasa {ECO:0000303|PubMed:3052853};
DE EC=3.6.4.13 {ECO:0000269|PubMed:8026330};
DE AltName: Full=Antigen Mab46F11;
GN Name=vas {ECO:0000312|FlyBase:FBgn0283442};
GN Synonyms=vasa {ECO:0000303|PubMed:3140040};
GN ORFNames=CG46283 {ECO:0000312|FlyBase:FBgn0283442};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=3140040; DOI=10.1038/335611a0;
RA Lasko P.F., Ashburner M.;
RT "The product of the Drosophila gene vasa is very similar to eukaryotic
RT initiation factor-4A.";
RL Nature 335:611-617(1988).
RN [2]
RP SEQUENCE REVISION.
RA Lasko P.F.;
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=3052853; DOI=10.1016/0092-8674(88)90216-4;
RA Hay B., Jan L.Y., Jan Y.N.;
RT "A protein component of Drosophila polar granules is encoded by vasa and
RT has extensive sequence similarity to ATP-dependent helicases.";
RL Cell 55:577-587(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA Celniker S.E., Rubin G.M.;
RT "An exploration of the sequence of a 2.9-Mb region of the genome of
RT Drosophila melanogaster: the Adh region.";
RL Genetics 153:179-219(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ILE-256; ILE-271 AND GLY-552.
RX PubMed=8026330; DOI=10.1242/dev.120.5.1201;
RA Liang L., Diehl-Jones W., Lasko P.;
RT "Localization of vasa protein to the Drosophila pole plasm is independent
RT of its RNA-binding and helicase activities.";
RL Development 120:1201-1211(1994).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=9521895; DOI=10.1242/dev.125.9.1569;
RA Styhler S., Nakamura A., Swan A., Suter B., Lasko P.;
RT "vasa is required for GURKEN accumulation in the oocyte, and is involved in
RT oocyte differentiation and germline cyst development.";
RL Development 125:1569-1578(1998).
RN [10]
RP FUNCTION, INTERACTION WITH EIF5B, AND DISRUPTION PHENOTYPE.
RX PubMed=10678180; DOI=10.1016/s1097-2765(00)80414-1;
RA Carrera P., Johnstone O., Nakamura A., Casanova J., Jackle H., Lasko P.;
RT "VASA mediates translation through interaction with a Drosophila yIF2
RT homolog.";
RL Mol. Cell 5:181-187(2000).
RN [11]
RP FUNCTION.
RX PubMed=11526087; DOI=10.1242/dev.128.14.2823;
RA Harris A.N., Macdonald P.M.;
RT "Aubergine encodes a Drosophila polar granule component required for pole
RT cell formation and related to eIF2C.";
RL Development 128:2823-2832(2001).
RN [12]
RP FUNCTION, INTERACTION WITH GUS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=12479811; DOI=10.1016/s1534-5807(02)00361-1;
RA Styhler S., Nakamura A., Lasko P.;
RT "VASA localization requires the SPRY-domain and SOCS-box containing
RT protein, GUSTAVUS.";
RL Dev. Cell 3:865-876(2002).
RN [13]
RP FUNCTION, INTERACTION WITH FAF, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND UBIQUITINATION.
RX PubMed=14588248; DOI=10.1016/j.cub.2003.10.026;
RA Liu N., Dansereau D.A., Lasko P.;
RT "Fat facets interacts with vasa in the Drosophila pole plasm and protects
RT it from degradation.";
RL Curr. Biol. 13:1905-1909(2003).
RN [14]
RP INTERACTION WITH PIWI; DCR-1 AND FMR1, AND SUBCELLULAR LOCATION.
RX PubMed=16949822; DOI=10.1016/j.cub.2006.08.051;
RA Megosh H.B., Cox D.N., Campbell C., Lin H.;
RT "The role of PIWI and the miRNA machinery in Drosophila germline
RT determination.";
RL Curr. Biol. 16:1884-1894(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND THR-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [16]
RP FUNCTION, AND INTERACTION WITH AUB; ME31B; EIF-4A AND TER94.
RX PubMed=18590813; DOI=10.1016/j.mod.2008.06.005;
RA Thomson T., Liu N., Arkov A., Lehmann R., Lasko P.;
RT "Isolation of new polar granule components in Drosophila reveals P body and
RT ER associated proteins.";
RL Mech. Dev. 125:865-873(2008).
RN [17]
RP FUNCTION, INTERACTION WITH GUS AND FSN, SUBCELLULAR LOCATION, MUTAGENESIS
RP OF 184-ASP--ASN-188; ASP-184; ASN-187; ASN-188 AND ASN-189, AND MOTIF.
RX PubMed=20123973; DOI=10.1128/mcb.01100-09;
RA Kugler J.M., Woo J.S., Oh B.H., Lasko P.;
RT "Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3
RT ligase specificity receptors.";
RL Mol. Cell. Biol. 30:1769-1782(2010).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 200-623 IN COMPLEX WITH SSRNA AND
RP ATP, FUNCTION, AND MUTAGENESIS OF ARG-328; GLU-329; GLN-333; ARG-378;
RP ASP-381; GLN-525; ARG-528; THR-546; ARG-551 AND ASP-554.
RX PubMed=16630817; DOI=10.1016/j.cell.2006.01.054;
RA Sengoku T., Nureki O., Nakamura A., Kobayashi S., Yokoyama S.;
RT "Structural basis for RNA unwinding by the DEAD-box protein Drosophila
RT Vasa.";
RL Cell 125:287-300(2006).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 184-203 IN COMPLEX WITH GUS, AND
RP MUTAGENESIS OF ASP-184; ILE-185; 186-ASN--ASN-189; 186-ASN--ASN-188;
RP ASN-187; ASN-188 AND ASN-189.
RX PubMed=17189197; DOI=10.1016/j.molcel.2006.11.009;
RA Woo J.S., Suh H.Y., Park S.Y., Oh B.H.;
RT "Structural basis for protein recognition by B30.2/SPRY domains.";
RL Mol. Cell 24:967-976(2006).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 184-203.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human spla/ryanodine receptor domain and socs box
RT containing 1 (spsb1) in complex with a 20-residue vasa peptide.";
RL Submitted (DEC-2008) to the PDB data bank.
RN [21] {ECO:0007744|PDB:3EMW, ECO:0007744|PDB:3F2O}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 184-203 IN COMPLEX WITH HUMAN
RP SPSB1 AND SPSB2, AND MOTIF.
RX PubMed=20561531; DOI=10.1016/j.jmb.2010.06.017;
RA Filippakopoulos P., Low A., Sharpe T.D., Uppenberg J., Yao S., Kuang Z.,
RA Savitsky P., Lewis R.S., Nicholson S.E., Norton R.S., Bullock A.N.;
RT "Structural basis for Par-4 recognition by the SPRY domain- and SOCS box-
RT containing proteins SPSB1, SPSB2, and SPSB4.";
RL J. Mol. Biol. 401:389-402(2010).
CC -!- FUNCTION: Involved in translational control mechanisms operating in
CC early stages of oogenesis. Required maternally in many stages of
CC oogenesis, including cystocyte differentiation, oocyte differentiation,
CC and specification of anterior-posterior polarity in the developing
CC cysts. Essential for the formation and/or structural integrity of
CC perinuclear nuage particles during germ cell formation. Required for
CC gus, Fsn and aub accumulation at the posterior pole of the embryo.
CC Required for the localization of vas to the perinuclear region of nurse
CC cells. {ECO:0000269|PubMed:10678180, ECO:0000269|PubMed:11526087,
CC ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:14588248,
CC ECO:0000269|PubMed:16630817, ECO:0000269|PubMed:18590813,
CC ECO:0000269|PubMed:20123973, ECO:0000269|PubMed:3052853,
CC ECO:0000269|PubMed:3140040, ECO:0000269|PubMed:8026330,
CC ECO:0000269|PubMed:9521895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:8026330};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8026330};
CC -!- SUBUNIT: Interacts with eIF5B and faf. Interacts with gus (via
CC B30.2/SPRY domain) and Fsn (via B30.2/SPRY domain). Interacts with aub,
CC me31B, eIF-4a and TER94. Interacts with piwi; this interaction is RNA
CC independent. Interacts with Dcr-1 and Fmr1; these interactions occur in
CC the polar granules. {ECO:0000269|PubMed:10678180,
CC ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:14588248,
CC ECO:0000269|PubMed:16630817, ECO:0000269|PubMed:16949822,
CC ECO:0000269|PubMed:17189197, ECO:0000269|PubMed:18590813,
CC ECO:0000269|PubMed:20123973}.
CC -!- INTERACTION:
CC P09052; Q9V6L9: Fsn; NbExp=2; IntAct=EBI-134067, EBI-126933;
CC P09052; A1Z6E0: gus; NbExp=5; IntAct=EBI-134067, EBI-75338;
CC P09052; Q96BD6: SPSB1; Xeno; NbExp=2; IntAct=EBI-134067, EBI-2659201;
CC P09052; Q99619: SPSB2; Xeno; NbExp=2; IntAct=EBI-134067, EBI-2323209;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12479811,
CC ECO:0000269|PubMed:14588248, ECO:0000269|PubMed:16949822,
CC ECO:0000269|PubMed:20123973, ECO:0000269|PubMed:8026330}.
CC Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC specific organelle required to repress transposon activity during
CC meiosis. Later seen in the pole plasm at the posterior end of the
CC oocyte as a component of polar granules. {ECO:0000269|PubMed:14588248,
CC ECO:0000269|PubMed:8026330}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=vas {ECO:0000312|FlyBase:FBgn0283442}; Synonyms=A;
CC IsoId=P09052-1; Sequence=Displayed;
CC Name=solo;
CC IsoId=B6JUP5-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the female germline. Gus
CC and faf are required for vas expression in the posterior pole of the
CC oocyte. {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:14588248,
CC ECO:0000269|PubMed:3052853, ECO:0000269|PubMed:3140040,
CC ECO:0000269|PubMed:9521895}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:3052853,
CC ECO:0000269|PubMed:3140040}.
CC -!- DOMAIN: The B30.2/SPRY domain-binding motif mediates recognition by
CC proteins containing a B30.2/SPRY domain. {ECO:0000269|PubMed:20123973,
CC ECO:0000269|PubMed:20561531}.
CC -!- PTM: Ubiquitinated during oogenesis. Deubiquitinated by faf, which
CC protects this protein from proteasome-mediated degradation.
CC {ECO:0000269|PubMed:14588248}.
CC -!- DISRUPTION PHENOTYPE: Defective growth of germline cysts. Fails to
CC efficiently accumulate many localized RNAs, such as Bic-D, orb, osk and
CC nos, but still accumulates grk RNA. {ECO:0000269|PubMed:10678180,
CC ECO:0000269|PubMed:3140040, ECO:0000269|PubMed:9521895}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL89864.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X12945; CAA31405.1; -; Genomic_DNA.
DR EMBL; X12946; CAA31405.1; JOINED; Genomic_DNA.
DR EMBL; M23560; AAA29013.1; -; mRNA.
DR EMBL; AE014134; AAF53438.1; -; Genomic_DNA.
DR EMBL; AY084126; AAL89864.1; ALT_FRAME; mRNA.
DR PIR; A58768; A58768.
DR RefSeq; NP_001260458.1; NM_001273529.2. [P09052-1]
DR RefSeq; NP_001303322.1; NM_001316393.1. [P09052-1]
DR RefSeq; NP_723899.1; NM_165103.3. [P09052-1]
DR PDB; 2DB3; X-ray; 2.20 A; A/B/C/D=200-623.
DR PDB; 2IHS; X-ray; 2.20 A; C/D=184-203.
DR PDB; 3EMW; X-ray; 1.80 A; B=184-203.
DR PDB; 3F2O; X-ray; 2.05 A; C/D=184-203.
DR PDB; 5NT7; X-ray; 1.40 A; B/D=463-623.
DR PDBsum; 2DB3; -.
DR PDBsum; 2IHS; -.
DR PDBsum; 3EMW; -.
DR PDBsum; 3F2O; -.
DR PDBsum; 5NT7; -.
DR AlphaFoldDB; P09052; -.
DR SMR; P09052; -.
DR BioGRID; 60902; 23.
DR DIP; DIP-20604N; -.
DR ELM; P09052; -.
DR IntAct; P09052; 9.
DR MINT; P09052; -.
DR iPTMnet; P09052; -.
DR PRIDE; P09052; -.
DR EnsemblMetazoa; FBtr0445185; FBpp0401445; FBgn0283442. [P09052-1]
DR EnsemblMetazoa; FBtr0445186; FBpp0401446; FBgn0283442. [P09052-1]
DR EnsemblMetazoa; FBtr0445187; FBpp0401447; FBgn0283442. [P09052-1]
DR GeneID; 26067080; -.
DR KEGG; dme:Dmel_CG46283; -.
DR CTD; 26067080; -.
DR FlyBase; FBgn0283442; vas.
DR VEuPathDB; VectorBase:FBgn0283442; -.
DR GeneTree; ENSGT00940000157507; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR OMA; DVKQTIY; -.
DR PhylomeDB; P09052; -.
DR SignaLink; P09052; -.
DR BioGRID-ORCS; 26067080; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; P09052; -.
DR GenomeRNAi; 26067080; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0283442; Expressed in egg chamber and 9 other tissues.
DR ExpressionAtlas; P09052; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043073; C:germ cell nucleus; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:0061803; C:posterior cell cortex; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007276; P:gamete generation; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR CDD; cd17967; DEADc_DDX3_DDX4; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044763; Ded1/Dbp1_DEADc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm;
KW Developmental protein; Differentiation; Helicase; Hydrolase; Magnesium;
KW Nucleotide-binding; Oogenesis; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..661
FT /note="ATP-dependent RNA helicase vasa"
FT /id="PRO_0000054976"
FT REPEAT 93..99
FT /note="1"
FT REPEAT 100..106
FT /note="2"
FT REPEAT 107..113
FT /note="3"
FT REPEAT 114..120
FT /note="4"
FT REPEAT 121..127
FT /note="5"
FT DOMAIN 276..453
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 477..624
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..127
FT /note="5 X 7 AA tandem repeats of [FS]-R-G-G-[EQ]-G-G"
FT REGION 184..203
FT /note="Required for posterior localization in oocyte"
FT MOTIF 184..188
FT /note="B30.2/SPRY domain-binding motif"
FT /evidence="ECO:0000269|PubMed:20123973,
FT ECO:0000269|PubMed:20561531"
FT MOTIF 245..273
FT /note="Q motif"
FT MOTIF 399..402
FT /note="DEAD box"
FT COMPBIAS 7..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289..296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 27
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 184..188
FT /note="DINNN->AAAAA: Enhances protein stability. Does not
FT affect protein distribution in the oocyte."
FT /evidence="ECO:0000269|PubMed:20123973"
FT MUTAGEN 184
FT /note="D->A: Decreases interaction with gus."
FT /evidence="ECO:0000269|PubMed:17189197,
FT ECO:0000269|PubMed:20123973"
FT MUTAGEN 185
FT /note="I->A: Decreases interaction with gus."
FT /evidence="ECO:0000269|PubMed:17189197"
FT MUTAGEN 186..189
FT /note="NNNN->ANNA: Strongly decreases interaction with
FT gus."
FT /evidence="ECO:0000269|PubMed:17189197"
FT MUTAGEN 186..188
FT /note="NNN->AAA: Abolishes interaction with gus."
FT /evidence="ECO:0000269|PubMed:17189197"
FT MUTAGEN 187
FT /note="N->A: Strongly decreases interaction with gus."
FT /evidence="ECO:0000269|PubMed:17189197,
FT ECO:0000269|PubMed:20123973"
FT MUTAGEN 188
FT /note="N->A: Strongly decreases interaction with gus."
FT /evidence="ECO:0000269|PubMed:17189197,
FT ECO:0000269|PubMed:20123973"
FT MUTAGEN 189
FT /note="N->A: Does not affect interaction with gus."
FT /evidence="ECO:0000269|PubMed:17189197,
FT ECO:0000269|PubMed:20123973"
FT MUTAGEN 256
FT /note="I->N: Fails to bind and unwind RNA."
FT /evidence="ECO:0000269|PubMed:8026330"
FT MUTAGEN 271
FT /note="I->M: Fails to bind and unwind RNA."
FT /evidence="ECO:0000269|PubMed:8026330"
FT MUTAGEN 328
FT /note="R->A: Reduction in RNA-binding, reduced RNA-
FT dependent ATPase and unwinding activities."
FT /evidence="ECO:0000269|PubMed:16630817"
FT MUTAGEN 329
FT /note="E->A: Increase in RNA-binding and no significant
FT change to RNA-dependent ATPase or unwinding activities."
FT /evidence="ECO:0000269|PubMed:16630817"
FT MUTAGEN 333
FT /note="Q->A: Reduction in RNA-binding, drastic reduction in
FT unwinding activities, no significant change to RNA-
FT dependent ATPase activity."
FT /evidence="ECO:0000269|PubMed:16630817"
FT MUTAGEN 378
FT /note="R->A: Reduction in RNA-binding, significantly
FT reduced RNA-dependent ATPase and unwinding activities."
FT /evidence="ECO:0000269|PubMed:16630817"
FT MUTAGEN 381
FT /note="D->A: Increase in RNA-binding."
FT /evidence="ECO:0000269|PubMed:16630817"
FT MUTAGEN 525
FT /note="Q->A: Reduction in RNA-binding, abolished unwinding
FT activities and no significant change to RNA-dependent
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:16630817"
FT MUTAGEN 528
FT /note="R->A: Reduction in RNA-binding, barely detectable
FT RNA-dependent ATPase activity and completely defective
FT unwinding activity."
FT /evidence="ECO:0000269|PubMed:16630817"
FT MUTAGEN 546
FT /note="T->A: Moderately decreased the RNA binding,
FT abolished both the RNA-dependent ATPase and unwinding
FT activities."
FT /evidence="ECO:0000269|PubMed:16630817"
FT MUTAGEN 551
FT /note="R->A: Reduction in RNA-binding, drastic reduction in
FT unwinding activities and no significant change to RNA-
FT dependent ATPase activity."
FT /evidence="ECO:0000269|PubMed:16630817"
FT MUTAGEN 552
FT /note="G->E: Fails to unwind RNA."
FT /evidence="ECO:0000269|PubMed:8026330"
FT MUTAGEN 554
FT /note="D->A: No change to RNA-binding, abolished unwinding
FT activities and no significant change to RNA-dependent
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:16630817"
FT CONFLICT 35
FT /note="A -> R (in Ref. 3; AAA29013)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..165
FT /note="Missing (in Ref. 3; AAA29013)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="V -> A (in Ref. 1; CAA31405 and 3; AAA29013)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="Y -> F (in Ref. 1; CAA31405)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="V -> C (in Ref. 3; AAA29013)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="F -> S (in Ref. 1; CAA31405)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="R -> C (in Ref. 1; CAA31405)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="D -> H (in Ref. 3; AAA29013)"
FT /evidence="ECO:0000305"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:3F2O"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:3F2O"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:2DB3"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:2DB3"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:2DB3"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:2DB3"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:2DB3"
FT HELIX 270..280
FT /evidence="ECO:0007829|PDB:2DB3"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:2DB3"
FT HELIX 295..309
FT /evidence="ECO:0007829|PDB:2DB3"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:2DB3"
FT HELIX 328..341
FT /evidence="ECO:0007829|PDB:2DB3"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:2DB3"
FT HELIX 358..365
FT /evidence="ECO:0007829|PDB:2DB3"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:2DB3"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:2DB3"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:2DB3"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:2DB3"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:2DB3"
FT HELIX 410..418
FT /evidence="ECO:0007829|PDB:2DB3"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:2DB3"
FT HELIX 437..444
FT /evidence="ECO:0007829|PDB:2DB3"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:2DB3"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 477..487
FT /evidence="ECO:0007829|PDB:5NT7"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 499..511
FT /evidence="ECO:0007829|PDB:5NT7"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 525..536
FT /evidence="ECO:0007829|PDB:5NT7"
FT STRAND 541..546
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 547..550
FT /evidence="ECO:0007829|PDB:5NT7"
FT STRAND 559..565
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 570..577
FT /evidence="ECO:0007829|PDB:5NT7"
FT STRAND 588..593
FT /evidence="ECO:0007829|PDB:5NT7"
FT TURN 595..597
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 599..601
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 602..611
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:5NT7"
SQ SEQUENCE 661 AA; 72331 MW; 8617C25CCB3130B9 CRC64;
MSDDWDDEPI VDTRGARGGD WSDDEDTAKS FSGEAEGDGV GGSGGEGGGY QGGNRDVFGR
IGGGRGGGAG GYRGGNRDGG GFHGGRREGE RDFRGGEGGF RGGQGGSRGG QGGSRGGQGG
FRGGEGGFRG RLYENEDGDE RRGRLDREER GGERRGRLDR EERGGERGER GDGGFARRRR
NEDDINNNNN IVEDVERKRE FYIPPEPSND AIEIFSSGIA SGIHFSKYNN IPVKVTGSDV
PQPIQHFTSA DLRDIIIDNV NKSGYKIPTP IQKCSIPVIS SGRDLMACAQ TGSGKTAAFL
LPILSKLLED PHELELGRPQ VVIVSPTREL AIQIFNEARK FAFESYLKIG IVYGGTSFRH
QNECITRGCH VVIATPGRLL DFVDRTFITF EDTRFVVLDE ADRMLDMGFS EDMRRIMTHV
TMRPEHQTLM FSATFPEEIQ RMAGEFLKNY VFVAIGIVGG ACSDVKQTIY EVNKYAKRSK
LIEILSEQAD GTIVFVETKR GADFLASFLS EKEFPTTSIH GDRLQSQREQ ALRDFKNGSM
KVLIATSVAS RGLDIKNIKH VINYDMPSKI DDYVHRIGRT GRVGNNGRAT SFFDPEKDRA
IAADLVKILE GSGQTVPDFL RTCGAGGDGG YSNQNFGGVD VRGRGNYVGD ATNVEEEEQW
D
