STAU_DROME
ID STAU_DROME Reviewed; 1026 AA.
AC P25159; Q6NQY8; Q86PB7; Q9V8B8; Q9V8B9;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Maternal effect protein staufen;
GN Name=stau; ORFNames=CG5753;
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 [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=1712672; DOI=10.1016/0092-8674(91)90138-o;
RA St Johnston D., Beuchle D., Nuesslein-Volhard C.;
RT "Staufen, a gene required to localize maternal RNAs in the Drosophila
RT egg.";
RL Cell 66:51-63(1991).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley; TISSUE=Embryo, Larva, and Pupae;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8001156; DOI=10.1016/0092-8674(94)90013-2;
RA Ferrandon D., Elphick L., Nusslein-Volhard C., St Johnston D.;
RT "Staufen protein associates with the 3'UTR of bicoid mRNA to form particles
RT that move in a microtubule-dependent manner.";
RL Cell 79:1221-1232(1994).
RN [6]
RP CHARACTERIZATION OF DRBM DOMAINS.
RX PubMed=10716936; DOI=10.1093/emboj/19.6.1366;
RA Micklem D.R., Adams J., Grunert S., St Johnston D.;
RT "Distinct roles of two conserved Staufen domains in oskar mRNA localization
RT and translation.";
RL EMBO J. 19:1366-1377(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563; SER-570; THR-650;
RP THR-655 AND SER-676, AND 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 [8]
RP STRUCTURE BY NMR OF 579-646.
RX PubMed=7628456; DOI=10.1002/j.1460-2075.1995.tb07362.x;
RA Bycroft M., Grunert S., Murzin A.G., Proctor M., St Johnston D.;
RT "NMR solution structure of a dsRNA binding domain from Drosophila staufen
RT protein reveals homology to the N-terminal domain of ribosomal protein
RT S5.";
RL EMBO J. 14:3563-3571(1995).
RN [9]
RP ERRATUM OF PUBMED:7628456.
RA Bycroft M., Grunert S., Murzin A.G., Proctor M., St Johnston D.;
RL EMBO J. 14:4385-4385(1995).
RN [10]
RP STRUCTURE BY NMR OF 571-646, FUNCTION, AND MUTAGENESIS OF 581-SER--GLN-582;
RP 584-HIS--GLU-585; ILE-586; PHE-596; 599-LEU--GLU-602; HIS-606; LYS-608;
RP 628-LYS--LYS-629; LYS-632; 633-LYS--ALA-634 AND 635-ALA--ALA-636.
RX PubMed=10698941; DOI=10.1093/emboj/19.5.997;
RA Ramos A., Grunert S., Adams J., Micklem D.R., Proctor M.R., Freund S.,
RA Bycroft M., St Johnston D., Varani G.;
RT "RNA recognition by a Staufen double-stranded RNA-binding domain.";
RL EMBO J. 19:997-1009(2000).
RN [11]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH ME31B; TRAL; UPF1; AGO2 AND
RP FMR1, AND SUBCELLULAR LOCATION.
RX PubMed=17178403; DOI=10.1016/j.neuron.2006.10.028;
RA Barbee S.A., Estes P.S., Cziko A.M., Hillebrand J., Luedeman R.A.,
RA Coller J.M., Johnson N., Howlett I.C., Geng C., Ueda R., Brand A.H.,
RA Newbury S.F., Wilhelm J.E., Levine R.B., Nakamura A., Parker R.,
RA Ramaswami M.;
RT "Staufen- and FMRP-containing neuronal RNPs are structurally and
RT functionally related to somatic P bodies.";
RL Neuron 52:997-1009(2006).
CC -!- FUNCTION: RNA-binding protein which forms ribonucleoprotein complexes
CC (RNPs) that play critical roles in the localization, translational
CC repression and turnover of RNAs during embryogenesis, neurotransmission
CC and neurogenesis (PubMed:10698941, PubMed:1712672, PubMed:8001156,
CC PubMed:17178403). In the oocyte, essential for the localization of both
CC the osk/oskar mRNA to the posterior pole and bcd/bicoid RNA to the
CC anterior pole, and is therefore required for the correct anterior-
CC posterior patterning of the developing embryo (PubMed:10698941,
CC PubMed:1712672, PubMed:8001156). Association with osk or bcd at their
CC respective poles, appears to promote the formation and stabilization of
CC the ribonucleoprotein complexes (PubMed:1712672, PubMed:8001156).
CC Integral component of diverse neuritic ribonucleoprotein complexes
CC (RNPs) that mediate the transport, translation and turnover of neuronal
CC RNAs during neuorgenesis and the translation repression of synaptic
CC transcripts in preparation for their dendritic targeting
CC (PubMed:17178403). {ECO:0000269|PubMed:10698941,
CC ECO:0000269|PubMed:1712672, ECO:0000269|PubMed:17178403,
CC ECO:0000269|PubMed:8001156}.
CC -!- SUBUNIT: Component of neuronal ribonucleoprotein complexes (RNPs) that
CC contains at least various translational repressor and mRNA turnover
CC proteins such as me31B, tral, Upf1, AGO2 and sometimes Fmr1.
CC {ECO:0000269|PubMed:17178403}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule
CC {ECO:0000269|PubMed:17178403}. Note=Detected within ribonucleoprotein
CC granules in pherpiheral nerves that are exiting the larval central
CC nervous system, and cell bodies within the ventral ganglion.
CC {ECO:0000269|PubMed:17178403}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P25159-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P25159-2; Sequence=VSP_014781;
CC -!- TISSUE SPECIFICITY: Polar granules at the posterior pole of the oocyte,
CC and by the time the egg is laid, at the anterior pole.
CC {ECO:0000269|PubMed:1712672, ECO:0000269|PubMed:8001156}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:1712672, ECO:0000269|PubMed:8001156}.
CC -!- DOMAIN: Contains a proline-rich domain. The insertion of this domain in
CC the DRBM 2 domain is required for stau-oskar mRNA localization.
CC -!- DOMAIN: DRBM 3 domain binds optimally to stem-loops containing 12 bp
CC (in vitro).
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DR EMBL; M69111; AAA73062.1; -; mRNA.
DR EMBL; AE013599; AAF57752.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57753.1; -; Genomic_DNA.
DR EMBL; BT003228; AAO24983.1; -; mRNA.
DR EMBL; BT010297; AAQ23615.1; -; mRNA.
DR PIR; A40315; A40315.
DR RefSeq; NP_001163185.1; NM_001169714.2.
DR RefSeq; NP_476751.1; NM_057403.4. [P25159-1]
DR RefSeq; NP_725748.1; NM_166263.2. [P25159-2]
DR PDB; 1EKZ; NMR; -; A=571-646.
DR PDB; 1STU; NMR; -; A=579-646.
DR PDB; 5CFF; X-ray; 2.50 A; E/F/G/H=953-1019.
DR PDBsum; 1EKZ; -.
DR PDBsum; 1STU; -.
DR PDBsum; 5CFF; -.
DR AlphaFoldDB; P25159; -.
DR SMR; P25159; -.
DR BioGRID; 62749; 88.
DR IntAct; P25159; 6.
DR STRING; 7227.FBpp0085962; -.
DR iPTMnet; P25159; -.
DR PaxDb; P25159; -.
DR ABCD; P25159; 2 sequenced antibodies.
DR EnsemblMetazoa; FBtr0086783; FBpp0085962; FBgn0003520. [P25159-1]
DR EnsemblMetazoa; FBtr0086784; FBpp0085963; FBgn0003520. [P25159-2]
DR GeneID; 37065; -.
DR KEGG; dme:Dmel_CG5753; -.
DR UCSC; CG5753-RA; d. melanogaster. [P25159-1]
DR CTD; 37065; -.
DR FlyBase; FBgn0003520; stau.
DR VEuPathDB; VectorBase:FBgn0003520; -.
DR eggNOG; KOG3732; Eukaryota.
DR InParanoid; P25159; -.
DR OMA; TKQTPMK; -.
DR PhylomeDB; P25159; -.
DR SignaLink; P25159; -.
DR BioGRID-ORCS; 37065; 0 hits in 3 CRISPR screens.
DR ChiTaRS; stau; fly.
DR EvolutionaryTrace; P25159; -.
DR GenomeRNAi; 37065; -.
DR PRO; PR:P25159; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003520; Expressed in brain and 52 other tissues.
DR ExpressionAtlas; P25159; baseline and differential.
DR Genevisible; P25159; DM.
DR GO; GO:0045179; C:apical cortex; IDA:FlyBase.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0045180; C:basal cortex; IDA:FlyBase.
DR GO; GO:0009925; C:basal plasma membrane; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0060293; C:germ plasm; IDA:BHF-UCL.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0061803; C:posterior cell cortex; IDA:FlyBase.
DR GO; GO:0071212; C:subsynaptic reticulum; IDA:FlyBase.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:FlyBase.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; IGI:FlyBase.
DR GO; GO:0098964; P:anterograde dendritic transport of messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; TAS:FlyBase.
DR GO; GO:0045450; P:bicoid mRNA localization; TAS:FlyBase.
DR GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; TAS:FlyBase.
DR GO; GO:0007400; P:neuroblast fate determination; TAS:FlyBase.
DR GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR GO; GO:0007315; P:pole plasm assembly; IMP:FlyBase.
DR GO; GO:0007318; P:pole plasm protein localization; IMP:FlyBase.
DR GO; GO:0007316; P:pole plasm RNA localization; IMP:FlyBase.
DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IMP:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0035418; P:protein localization to synapse; IMP:FlyBase.
DR GO; GO:0046011; P:regulation of oskar mRNA translation; TAS:FlyBase.
DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IGI:FlyBase.
DR GO; GO:0006403; P:RNA localization; IMP:FlyBase.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR032478; Staufen_C.
DR Pfam; PF00035; dsrm; 4.
DR Pfam; PF16482; Staufen_C; 1.
DR SMART; SM00358; DSRM; 4.
DR PROSITE; PS50137; DS_RBD; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1026
FT /note="Maternal effect protein staufen"
FT /id="PRO_0000072250"
FT DOMAIN 311..378
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 490..557
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 578..645
FT /note="DRBM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 711..781
FT /note="DRBM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 951..1018
FT /note="DRBM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 16..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 606
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT BINDING 608
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT BINDING 628
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT BINDING 629
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT BINDING 632
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 650
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 655
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_014781"
FT MUTAGEN 581..582
FT /note="SQ->AA: Affects RNA binding without altering the
FT conformation of the domain."
FT /evidence="ECO:0000269|PubMed:10698941"
FT MUTAGEN 584..585
FT /note="HE->AA: Affects RNA binding without altering the
FT conformation of the domain."
FT /evidence="ECO:0000269|PubMed:10698941"
FT MUTAGEN 586
FT /note="I->A: Crucial for the structure of DRBM 3."
FT /evidence="ECO:0000269|PubMed:10698941"
FT MUTAGEN 596
FT /note="F->A: Crucial for the structure of DRBM 3."
FT /evidence="ECO:0000269|PubMed:10698941"
FT MUTAGEN 599..602
FT /note="LREE->AAAA: Strongly reduces RNA binding."
FT /evidence="ECO:0000269|PubMed:10698941"
FT MUTAGEN 606
FT /note="H->A: Abolishes RNA binding without altering the
FT conformation of the domain."
FT /evidence="ECO:0000269|PubMed:10698941"
FT MUTAGEN 608
FT /note="K->A: Abolishes RNA binding without altering the
FT conformation of the domain."
FT /evidence="ECO:0000269|PubMed:10698941"
FT MUTAGEN 628..629
FT /note="KK->AA: Abolishes RNA binding without altering the
FT conformation of the domain."
FT /evidence="ECO:0000269|PubMed:10698941"
FT MUTAGEN 632
FT /note="K->A: Abolishes RNA binding without altering the
FT conformation of the domain."
FT /evidence="ECO:0000269|PubMed:10698941"
FT MUTAGEN 633..634
FT /note="KR->AA: No effect on RNA binding."
FT /evidence="ECO:0000269|PubMed:10698941"
FT MUTAGEN 635..636
FT /note="AA->SS: Crucial for the structure of DRBM 3."
FT /evidence="ECO:0000269|PubMed:10698941"
FT CONFLICT 84
FT /note="G -> A (in Ref. 1; AAA73062)"
FT /evidence="ECO:0000305"
FT CONFLICT 684..685
FT /note="PT -> TM (in Ref. 1; AAA73062)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="S -> C (in Ref. 1; AAA73062)"
FT /evidence="ECO:0000305"
FT CONFLICT 841
FT /note="Missing (in Ref. 4; AAQ23615)"
FT /evidence="ECO:0000305"
FT HELIX 579..589
FT /evidence="ECO:0007829|PDB:1EKZ"
FT STRAND 595..601
FT /evidence="ECO:0007829|PDB:1EKZ"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:1EKZ"
FT STRAND 610..616
FT /evidence="ECO:0007829|PDB:1EKZ"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:1EKZ"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:1EKZ"
FT HELIX 633..643
FT /evidence="ECO:0007829|PDB:1EKZ"
FT HELIX 953..962
FT /evidence="ECO:0007829|PDB:5CFF"
FT STRAND 967..972
FT /evidence="ECO:0007829|PDB:5CFF"
FT STRAND 977..986
FT /evidence="ECO:0007829|PDB:5CFF"
FT STRAND 992..1000
FT /evidence="ECO:0007829|PDB:5CFF"
FT HELIX 1001..1018
FT /evidence="ECO:0007829|PDB:5CFF"
SQ SEQUENCE 1026 AA; 110283 MW; 3D390391F988B0A2 CRC64;
MQHNVHAARP APHIRAAHHH SHSHAHMHLH PGMEQHLGPS LQQQQQPPPP PQQPPHRDLH
ARLNHHHLHA QQQQQQQTSS NQAGAVAAAG AAYHHGNINS NSGSNISSNS NQMQKIRQQH
QHLSSSNGLL GNQPPGPPPQ AFNPLAGNPA ALAYNQLPPH PPHHMAAHLG SYAAPPPHYY
MSQAKPAKYN HYGSNANSNS GSNNSNSNYA PKAILQNTYR NQKVVVPPVV QEVTPVPEPP
VTTNNATTNS TSNSTVIASE PVTQEDTSQK PETRQEPASA DDHVSTGNID ATGALSNEDT
SSSGRGGKDK TPMCLVNELA RYNKITHQYR LTEERGPAHC KTFTVTLMLG DEEYSADGFK
IKKAQHLAAS KAIEETMYKH PPPKIRRSEE GGPMRTHITP TVELNALAMK LGQRTFYLLD
PTQIPPTDSI VPPEFAGGHL LTAPGPGMPQ PPPPPAYALR QRLGNGFVPI PSQPMHPHFF
HGPGQRPFPP KFPSRFALPP PLGAHVHHGP NGPFPSVPTP PSKITLFVGK QKFVGIGRTL
QQAKHDAAAR ALQVLKTQAI SASEEALEDS MDEGDKKSPI SQVHEIGIKR NMTVHFKVLR
EEGPAHMKNF ITACIVGSIV TEGEGNGKKV SKKRAAEKML VELQKLPPLT PTKQTPLKRI
KVKTPGKSGA AAREGSVVSG TDGPTQTGKP ERRKRLNPPK DKLIDMDDAD NPITKLIQLQ
QTRKEKEPIF ELIAKNGNET ARRREFVMEV SASGSTARGT GNSKKLAKRN AAQALFELLE
AVQVTPTNET QSSEECSTSA TMSAVTAPAV EATAEGKVPM VATPVGPMPG ILILRQNKKP
AKKRDQIVIV KSNVESKEEE ANKEVAVAAE ENSNNSANSG DSSNSSSGDS QATEAASESA
LNTSTGSNTS GVSSNSSNVG ANTDGNNHAE SKNNTESSSN STSNTQSAGV HMKEQLLYLS
KLLDFEVNFS DYPKGNHNEF LTIVTLSTHP PQICHGVGKS SEESQNDAAS NALKILSKLG
LNNAMK
