VASAL_PENVA
ID VASAL_PENVA Reviewed; 703 AA.
AC Q4JG17;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Probable ATP-dependent RNA helicase vasa-like {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P09052};
DE AltName: Full=Vasa homolog {ECO:0000303|PubMed:16955407};
DE Short=Lv-Vasa {ECO:0000303|PubMed:16955407};
DE AltName: Full=Vasa-like protein {ECO:0000303|PubMed:16955407, ECO:0000312|EMBL:AAY89069.2};
GN Name=vasa {ECO:0000303|PubMed:16955407};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000312|EMBL:AAY89069.2};
RN [1] {ECO:0000312|EMBL:AAY89069.2}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND PHYLOGENETIC ANALYSIS.
RC TISSUE=Ovary {ECO:0000303|PubMed:16955407, ECO:0000312|EMBL:AAY89069.2};
RX PubMed=16955407; DOI=10.1002/mrd.20622;
RA Aflalo E.D., Bakhrat A., Raviv S., Harari D., Sagi A., Abdu U.;
RT "Characterization of a vasa-like gene from the pacific white shrimp
RT Litopenaeus vannamei and its expression during oogenesis.";
RL Mol. Reprod. Dev. 74:172-177(2007).
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.
CC {ECO:0000250|UniProtKB:P09052}.
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:0000250|UniProtKB:P09052};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16955407}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:16955407}. Note=Component of the meiotic
CC nuage, also named P granule, a germ-cell-specific organelle required to
CC repress transposon activity during meiosis. Later seen in the pole
CC plasm at the posterior end of the oocyte as a component of polar
CC granules (By similarity). Localized to the cytoplasm of the oocyte
CC throughout oogenesis (PubMed:16955407). {ECO:0000250|UniProtKB:P09052,
CC ECO:0000269|PubMed:16955407}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries and testis. Not expressed in
CC somatic tissue of the ovaries including follicle cells, muscle and
CC connective tissue. {ECO:0000269|PubMed:16955407}.
CC -!- DEVELOPMENTAL STAGE: First detected in oogonia cells and highly
CC expressed in late vitellogenic oocytes during oogenesis.
CC {ECO:0000269|PubMed:16955407}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC subfamily. {ECO:0000305}.
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DR EMBL; DQ095772; AAY89069.2; -; mRNA.
DR AlphaFoldDB; Q4JG17; -.
DR SMR; Q4JG17; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
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 InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00098; zf-CCHC; 3.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00343; ZnF_C2HC; 3.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF57756; SSF57756; 2.
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.
DR PROSITE; PS50158; ZF_CCHC; 3.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Developmental protein; Differentiation; Helicase;
KW Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Oogenesis; Repeat;
KW RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..703
FT /note="Probable ATP-dependent RNA helicase vasa-like"
FT /id="PRO_0000439761"
FT DOMAIN 292..475
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 506..651
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 77..92
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 166..181
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 189..204
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 261..289
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 419..422
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 94..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 305..312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 703 AA; 75746 MW; 60266B023C9ED8F3 CRC64;
MSDDWDETDA APASDWNIES FGLPTSFGST KKTCNTGNAF NDGEGGFDEG SQSNFDDPFR
SGGGGFGGRG RGGPRACFKC GDEGHMARDC PSASDSRGNR TNNRRQDNWG GGSSSKPANG
EPFGFGSAFG DNQESDPFGA TESSGFGFGS GSGSRGGRRN DGGRGCFKCG EEGHMSRDCP
SGGGRNKGCF KCGQEGHNAR DCPNPGEGSE EKKPRAPLYI PADVNEDELF VMGIEAGSNF
DAYANVPANV SGAEPIQPAA ESFQSMNLRP LLLENIVKAG YGCPTPVQKY TIPNVMNGRD
IMACAQTGSG KTAAFLLPML HYILDNNCPS NAFEEPAQPT GLVICPTREL AIQIMREARK
FSHSSVAKCC VAYGGAAGFH QLKTIHSGCH ILVATPGRLL DFLEKGKIVF SSLKYLVLDE
ADRMLDMGFL SSIKTVINHK TMTPTAERIT LMFSATFPHE IQELASAFLN NYLFVVVGTV
GAANTDVKQE VLCVPKFEKK AKLVEMCEEI LISADDEKIL VFVEQKRVAD FVGTYLCEKK
FRATTMHGDR YQAQREQALS EFRTGVHNIL VATAVTARGL DIKGIGVVVN YDLPKDIDEY
VHRIGRTGRL GNRGLSISFY DDETDACLTK DLVKVLSEAN QTIPDWLTQK ANASGHAQTY
HGSGLFASSD IRSKNGGGRG WEKNQASSFL GGPSESNVDE EWD
