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Protein maelstrom

 MAEL_DROME              Reviewed;         459 AA.
Q9VNS0; O17317; Q86BG5;
24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
30-AUG-2017, entry version 134.
RecName: Full=Protein maelstrom;
Name=mael; ORFNames=CG11254;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=9409682;
Clegg N.J., Frost D.M., Larkin M.K., Subrahmanyan L., Bryant Z.,
Ruohola-Baker H.;
"maelstrom is required for an early step in the establishment of
Drosophila oocyte polarity: posterior localization of grk mRNA.";
Development 124:4661-4671(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
FUNCTION.
PubMed=11277405; DOI=10.1007/s004270000114;
Clegg N.J., Findley S.D., Mahowald A.P., Ruohola-Baker H.;
"Maelstrom is required to position the MTOC in stage 2-6 Drosophila
oocytes.";
Dev. Genes Evol. 211:44-48(2001).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=12538514; DOI=10.1242/dev.00310;
Findley S.D., Tamanaha M., Clegg N.J., Ruohola-Baker H.;
"Maelstrom, a Drosophila spindle-class gene, encodes a protein that
colocalizes with Vasa and RDE1/AGO1 homolog, Aubergine, in nuage.";
Development 130:859-871(2003).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=17428915; DOI=10.1073/pnas.0701920104;
Lim A.K., Kai T.;
"Unique germ-line organelle, nuage, functions to repress selfish
genetic elements in Drosophila melanogaster.";
Proc. Natl. Acad. Sci. U.S.A. 104:6714-6719(2007).
[8]
ERRATUM.
Lim A.K., Kai T.;
Proc. Natl. Acad. Sci. U.S.A. 104:20143-20143(2007).
[9]
FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, AND DISRUPTION PHENOTYPE.
PubMed=19758565; DOI=10.1016/j.devcel.2009.07.017;
Pek J.W., Lim A.K., Kai T.;
"Drosophila maelstrom ensures proper germline stem cell lineage
differentiation by repressing microRNA-7.";
Dev. Cell 17:417-424(2009).
[10]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF GLU-131 AND HIS-291.
PubMed=23159368; DOI=10.1016/j.cell.2012.10.040;
Sienski G., Donertas D., Brennecke J.;
"Transcriptional silencing of transposons by Piwi and maelstrom and
its impact on chromatin state and gene expression.";
Cell 151:964-980(2012).
[11]
SUBCELLULAR LOCATION.
PubMed=23913921; DOI=10.1101/gad.221515.113;
Ohtani H., Iwasaki Y.W., Shibuya A., Siomi H., Siomi M.C., Saito K.;
"DmGTSF1 is necessary for Piwi-piRISC-mediated transcriptional
transposon silencing in the Drosophila ovary.";
Genes Dev. 27:1656-1661(2013).
-!- FUNCTION: Involved both in the piRNA and miRNA metabolic
processes. As a component of the meiotic nuage, plays a central
role during oogenesis by repressing transposable elements and
preventing their mobilization, which is essential for the germline
integrity. Repression of transposable elements is mediated via the
piRNA metabolic process, which mediates the repression of
transposable elements during meiosis by forming complexes composed
of piRNAs and Piwi proteins and governs the repression of
transposons. As a nuclear component, it is required for proper
differentiation in the germline stem cell (GSC) lineage by
repressing microRNA-7 (miR-7), thereby acting as an indirect
regulator of bag-of-marbles (Bam). Acts by binding to the promoter
of miR-7 gene and repressing its expression; miR-7 repression
alleviates the Bam repression by miR-7, thereby allowing
differentiation in the germline stem cell (GSC) lineage.
Indirectly required to position the microtubule organizing center
in stage 2-6 oocytes. {ECO:0000269|PubMed:11277405,
ECO:0000269|PubMed:12538514, ECO:0000269|PubMed:17428915,
ECO:0000269|PubMed:19758565, ECO:0000269|PubMed:23159368}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus
{ECO:0000269|PubMed:23913921}. Note=Component of the meiotic
nuage, also named P granule, a germ-cell-specific organelle
required to repress transposon activity during meiosis. Vas, aub
and spn-E are required for nuage localization. Shuttles between
the cytoplasm and the nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=Q9VNS0-1; Sequence=Displayed;
Name=C;
IsoId=Q9VNS0-2; Sequence=VSP_036675;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: In germaria and egg chambers, it is detected
in the germline. In the germarium, it is in all regions, including
region I where the germ cells are dividing. In early egg chambers,
it is uniformly distributed throughout the nurse cells and oocyte
but, by stage 5, it is most concentrated around the outer margins
of the cells, closest to the periphery of the egg chamber. Level
decreases in stages 5 and 6, but most noticeably in the oocyte,
where protein level remains. No detectable protein from stage 8
onward (at protein level). {ECO:0000269|PubMed:23159368,
ECO:0000269|PubMed:9409682}.
-!- DISRUPTION PHENOTYPE: Female sterility and defects in karyosome
formation and oocyte polarity due to transposable element
derepression. Ovary shows mislocalization of 2 proteins involved
in the microRNA and/or RNAi pathways, Dicer and AGO2. In testis,
transit-amplifying cysts fail to differentiate into primary
spermatocytes, instead breaking down into ectopic germline stem
cells (GSC) and smaller cysts, due to a depletion of Bag-of-
marbles (Bam) protein. {ECO:0000269|PubMed:12538514,
ECO:0000269|PubMed:17428915, ECO:0000269|PubMed:19758565,
ECO:0000269|PubMed:23159368}.
-!- SIMILARITY: Belongs to the maelstrom family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF025953; AAB97831.1; -; mRNA.
EMBL; AE014296; AAF51851.1; -; Genomic_DNA.
EMBL; AE014296; AAF51852.1; -; Genomic_DNA.
EMBL; AE014296; AAO41286.1; -; Genomic_DNA.
EMBL; AY119598; AAM50252.1; -; mRNA.
RefSeq; NP_001303390.1; NM_001316461.1. [Q9VNS0-1]
RefSeq; NP_524217.1; NM_079493.4. [Q9VNS0-1]
RefSeq; NP_730739.1; NM_168958.3. [Q9VNS0-1]
RefSeq; NP_788566.1; NM_176388.3. [Q9VNS0-2]
UniGene; Dm.5827; -.
PDB; 4YBG; X-ray; 1.60 A; A=84-333.
PDBsum; 4YBG; -.
ProteinModelPortal; Q9VNS0; -.
SMR; Q9VNS0; -.
BioGrid; 65723; 4.
IntAct; Q9VNS0; 3.
MINT; MINT-336073; -.
STRING; 7227.FBpp0088574; -.
PaxDb; Q9VNS0; -.
PRIDE; Q9VNS0; -.
EnsemblMetazoa; FBtr0089631; FBpp0088574; FBgn0016034. [Q9VNS0-2]
EnsemblMetazoa; FBtr0089632; FBpp0088575; FBgn0016034. [Q9VNS0-1]
EnsemblMetazoa; FBtr0089633; FBpp0088576; FBgn0016034. [Q9VNS0-1]
EnsemblMetazoa; FBtr0347062; FBpp0312456; FBgn0016034. [Q9VNS0-1]
GeneID; 40489; -.
KEGG; dme:Dmel_CG11254; -.
UCSC; CG11254-RA; d. melanogaster. [Q9VNS0-1]
UCSC; CG11254-RC; d. melanogaster.
CTD; 84944; -.
FlyBase; FBgn0016034; mael.
eggNOG; ENOG410INZ4; Eukaryota.
eggNOG; ENOG4111Z8I; LUCA.
InParanoid; Q9VNS0; -.
KO; K18411; -.
OMA; TAGIACQ; -.
OrthoDB; EOG091G0BYM; -.
PhylomeDB; Q9VNS0; -.
GenomeRNAi; 40489; -.
PRO; PR:Q9VNS0; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0016034; -.
ExpressionAtlas; Q9VNS0; differential.
Genevisible; Q9VNS0; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043186; C:P granule; IDA:FlyBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; TAS:FlyBase.
GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
GO; GO:0009950; P:dorsal/ventral axis specification; IMP:FlyBase.
GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:UniProtKB.
GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
GO; GO:0007140; P:male meiotic nuclear division; IBA:GO_Central.
GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010529; P:negative regulation of transposition; IMP:FlyBase.
GO; GO:0007314; P:oocyte anterior/posterior axis specification; IMP:FlyBase.
GO; GO:0048600; P:oocyte fate commitment; IMP:FlyBase.
GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; IMP:FlyBase.
GO; GO:0007312; P:oocyte nucleus migration involved in oocyte dorsal/ventral axis specification; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
GO; GO:0019094; P:pole plasm mRNA localization; NAS:FlyBase.
GO; GO:0008104; P:protein localization; IMP:FlyBase.
GO; GO:0060964; P:regulation of gene silencing by miRNA; IDA:UniProtKB.
GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.30.10; -; 1.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR024970; Maelstrom.
Pfam; PF13017; Maelstrom; 1.
SUPFAM; SSF47095; SSF47095; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; DNA-binding; Meiosis; Nucleus;
Oogenesis; Reference proteome; Repressor; RNA-mediated gene silencing;
Transcription; Transcription regulation.
CHAIN 1 459 Protein maelstrom.
/FTId=PRO_0000367299.
DNA_BIND 2 69 HMG box.
VAR_SEQ 40 40 E -> EPFQ (in isoform C). {ECO:0000305}.
/FTId=VSP_036675.
MUTAGEN 131 131 E->A: Reduces nuclear aCCumulation in
ovary and ovarian somatic cells. Affects
transposable element silencing. Causes
female sterility.
{ECO:0000269|PubMed:23159368}.
MUTAGEN 291 291 H->A: Reduces nuclear aCCumulation in
ovary and ovarian somatic cells. Affects
transposable element silencing. Causes
female sterility.
{ECO:0000269|PubMed:23159368}.
CONFLICT 247 247 L -> F (in Ref. 1; AAB97831).
{ECO:0000305}.
HELIX 85 101 {ECO:0000244|PDB:4YBG}.
HELIX 105 107 {ECO:0000244|PDB:4YBG}.
STRAND 110 120 {ECO:0000244|PDB:4YBG}.
STRAND 122 125 {ECO:0000244|PDB:4YBG}.
STRAND 127 138 {ECO:0000244|PDB:4YBG}.
TURN 139 141 {ECO:0000244|PDB:4YBG}.
STRAND 142 151 {ECO:0000244|PDB:4YBG}.
HELIX 164 170 {ECO:0000244|PDB:4YBG}.
HELIX 186 201 {ECO:0000244|PDB:4YBG}.
STRAND 203 205 {ECO:0000244|PDB:4YBG}.
STRAND 207 211 {ECO:0000244|PDB:4YBG}.
HELIX 213 215 {ECO:0000244|PDB:4YBG}.
HELIX 216 226 {ECO:0000244|PDB:4YBG}.
HELIX 231 234 {ECO:0000244|PDB:4YBG}.
STRAND 239 243 {ECO:0000244|PDB:4YBG}.
HELIX 244 258 {ECO:0000244|PDB:4YBG}.
HELIX 268 277 {ECO:0000244|PDB:4YBG}.
TURN 279 282 {ECO:0000244|PDB:4YBG}.
HELIX 289 294 {ECO:0000244|PDB:4YBG}.
HELIX 297 299 {ECO:0000244|PDB:4YBG}.
HELIX 301 316 {ECO:0000244|PDB:4YBG}.
HELIX 317 319 {ECO:0000244|PDB:4YBG}.
TURN 327 329 {ECO:0000244|PDB:4YBG}.
SEQUENCE 459 AA; 51601 MW; 002F7F1298CFEF4E CRC64;
MAPKKHSGFM MFVNEWRNRN AEGRRMTLAQ AVSHCGTIWE KMNTQQRGPY NSGGKDANVA
QRAKRESSNG HGQVDKAQRE ATESLMDMKR TIERLVLNAK MSHDLENAKF VFVAFNYFTK
ALTTDVYVPA EFAACEYSLK EGIRSIYSTM IDPGQIIFGQ GSDALLHSST THDLPLPPNA
LGEKNMTKLY RNIVDYLSKC QGKGKTLVVF TPAENITMVK SCFRYLECDD DFRDGGEKIQ
VFDIQYLLFI LKKEVMNVAD LNDEKINKFA TDAFFKKDFF EFTAGIACQY HEDNDRTKYC
TQSMVTRWAY TFTDFMCGDL AITVQPGKHI PAQTKPNYLI ISSYASSLDH ESSFDSFYSL
PGSGVKKESQ PEACSLSSSR LSVASSSYKP IDHTSFAANL NEVSEFPSLG MRNSSKHHGI
AASAQREWNA RNLPTHSRLI RKVSDNDFSV NGADGKLKK


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