GAWKY_DROME
ID GAWKY_DROME Reviewed; 1384 AA.
AC Q8SY33; Q8MSF0; Q9V4F1;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Protein Gawky {ECO:0000312|FlyBase:FBgn0051992};
GN Name=gw; Synonyms=GW182 {ECO:0000303|PubMed:16177138}; ORFNames=CG31992;
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 [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 [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537572};
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 [3] {ECO:0000312|EMBL:AAL68245.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL68245.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569}, and
RC Ovary {ECO:0000269|PubMed:12537569};
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 [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=16177138; DOI=10.1261/rna.2191905;
RA Rehwinkel J., Behm-Ansmant I., Gatfield D., Izaurralde E.;
RT "A crucial role for GW182 and the DCP1:DCP2 decapping complex in miRNA-
RT mediated gene silencing.";
RL RNA 11:1640-1647(2005).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH AGO1, AND SUBCELLULAR LOCATION.
RX PubMed=16815998; DOI=10.1101/gad.1424106;
RA Behm-Ansmant I., Rehwinkel J., Doerks T., Stark A., Bork P., Izaurralde E.;
RT "mRNA degradation by miRNAs and GW182 requires both CCR4:NOT deadenylase
RT and DCP1:DCP2 decapping complexes.";
RL Genes Dev. 20:1885-1898(2006).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16880270; DOI=10.1083/jcb.200512103;
RA Schneider M.D., Najand N., Chaker S., Pare J.M., Haskins J., Hughes S.C.,
RA Hobman T.C., Locke J., Simmonds A.J.;
RT "Gawky is a component of cytoplasmic mRNA processing bodies required for
RT early Drosophila development.";
RL J. Cell Biol. 174:349-358(2006).
RN [7] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH AGO1.
RX PubMed=18345015; DOI=10.1038/nsmb.1405;
RA Eulalio A., Huntzinger E., Izaurralde E.;
RT "GW182 interaction with Argonaute is essential for miRNA-mediated
RT translational repression and mRNA decay.";
RL Nat. Struct. Mol. Biol. 15:346-353(2008).
RN [8] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH PABP.
RX PubMed=19797087; DOI=10.1128/mcb.01081-09;
RA Zekri L., Huntzinger E., Heimstadt S., Izaurralde E.;
RT "The silencing domain of GW182 interacts with PABPC1 to promote
RT translational repression and degradation of microRNA targets and is
RT required for target release.";
RL Mol. Cell. Biol. 29:6220-6231(2009).
RN [9] {ECO:0000305}
RP REGIONS SUFFICIENT FOR MIRNA-MEDIATED SILENCING.
RX PubMed=19304924; DOI=10.1261/rna.1364909;
RA Chekulaeva M., Filipowicz W., Parker R.;
RT "Multiple independent domains of dGW182 function in miRNA-mediated
RT repression in Drosophila.";
RL RNA 15:794-803(2009).
RN [10] {ECO:0000305}
RP REGIONS REQUIRED FOR INTERACTION WITH AGO1 AND MIRNA-MEDIATED SILENCING,
RP AND ROLE OF UBA DOMAIN.
RX PubMed=19383769; DOI=10.1261/rna.1605509;
RA Eulalio A., Helms S., Fritzsch C., Fauser M., Izaurralde E.;
RT "A C-terminal silencing domain in GW182 is essential for miRNA function.";
RL RNA 15:1067-1077(2009).
RN [11] {ECO:0000305}
RP REGIONS REQUIRED FOR INTERACTION WITH AGO1 AND MIRNA-MEDIATED SILENCING.
RX PubMed=20530530; DOI=10.1093/nar/gkq501;
RA Chekulaeva M., Parker R., Filipowicz W.;
RT "The GW/WG repeats of Drosophila GW182 function as effector motifs for
RT miRNA-mediated repression.";
RL Nucleic Acids Res. 38:6673-6683(2010).
RN [12] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH CCR4-NOT AND PAN COMPLEXES.
RX PubMed=21981923; DOI=10.1016/j.molcel.2011.09.007;
RA Braun J.E., Huntzinger E., Fauser M., Izaurralde E.;
RT "GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA
RT targets.";
RL Mol. Cell 44:120-133(2011).
RN [13] {ECO:0000305, ECO:0000312|PDB:2WBR}
RP STRUCTURE BY NMR OF 1114-1198, AND ROLE OF RRM DOMAIN.
RX PubMed=19295135; DOI=10.1093/nar/gkp173;
RA Eulalio A., Tritschler F., Buttner R., Weichenrieder O., Izaurralde E.,
RA Truffault V.;
RT "The RRM domain in GW182 proteins contributes to miRNA-mediated gene
RT silencing.";
RL Nucleic Acids Res. 37:2974-2983(2009).
CC -!- FUNCTION: Required for gene silencing mediated by micro-RNAs (miRNAs).
CC Silences both polyadenylated and deadenylated mRNAs. Required for
CC miRNA-mediated translational repression and mRNA decay. Not required
CC for miRNA target recognition. Necessary to initiate but not to maintain
CC silencing. Promotes mRNA deadenylation through the recruitment of the
CC CCR4-NOT and PAN complexes and promotes decapping by the DCP1-DCP2
CC complex. Dissociates from silenced mRNAs after deadenylation. Required
CC for completion of nuclear divisions during early embryonic development.
CC {ECO:0000269|PubMed:16177138, ECO:0000269|PubMed:16815998,
CC ECO:0000269|PubMed:16880270, ECO:0000269|PubMed:18345015,
CC ECO:0000269|PubMed:19797087, ECO:0000269|PubMed:21981923}.
CC -!- SUBUNIT: Interacts (via N-terminal region) with AGO1 (via Piwi domain);
CC the interaction is essential for localization of AGO1 in P-bodies and
CC for miRNA-mediated silencing. Interacts with pAbp/PABPC1; this
CC interaction interferes with the binding of pAbp to eIF4G and is
CC required for miRNA-mediated silencing. Interacts with CCR4-NOT complex
CC members Not1, Rga/NOT2, twin/CCR4, Pop2 and NOT3/5 and with PAN complex
CC members CG8232/PAN2 and CG11486/PAN3. {ECO:0000269|PubMed:16815998,
CC ECO:0000269|PubMed:18345015, ECO:0000269|PubMed:19797087,
CC ECO:0000269|PubMed:21981923}.
CC -!- INTERACTION:
CC Q8SY33; Q32KD4: AGO1; NbExp=4; IntAct=EBI-160693, EBI-105513;
CC Q8SY33; D3DMN9: CG11486-RC; NbExp=2; IntAct=EBI-160693, EBI-6512959;
CC Q8SY33; A8DY81: Not1; NbExp=2; IntAct=EBI-160693, EBI-3428401;
CC Q8SY33; P21187: pAbp; NbExp=11; IntAct=EBI-160693, EBI-103658;
CC Q8SY33; A1Z7K9: PAN2; NbExp=2; IntAct=EBI-160693, EBI-193297;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16815998,
CC ECO:0000269|PubMed:16880270}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A; Synonyms=B, E, F;
CC IsoId=Q8SY33-1; Sequence=Displayed;
CC Name=I;
CC IsoId=Q8SY33-2; Sequence=VSP_047895;
CC Name=J;
CC IsoId=Q8SY33-3; Sequence=VSP_047896;
CC -!- DEVELOPMENTAL STAGE: Highest levels are found during early embryonic
CC development until approximately 18 hours and during pupariation.
CC {ECO:0000269|PubMed:16880270}.
CC -!- DOMAIN: The UBA domain is not required for correct subcellular
CC location, gene silencing or interaction with pAbp.
CC {ECO:0000269|PubMed:19383769}.
CC -!- DOMAIN: The RRM domain lacks RNA-binding properties and does not bind
CC RNA in vitro. It is not required for P-body localization or for
CC interaction with AGO1 or miRNAs but is required for silencing. May play
CC a role in protein-protein interactions. {ECO:0000269|PubMed:19295135,
CC ECO:0000303|PubMed:19295135}.
CC -!- SIMILARITY: Belongs to the GW182 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50720.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014135; AAF59322.2; -; Genomic_DNA.
DR EMBL; AE014135; AAF59323.2; -; Genomic_DNA.
DR EMBL; AE014135; AAN06507.2; -; Genomic_DNA.
DR EMBL; AE014135; AAN06508.1; -; Genomic_DNA.
DR EMBL; AE014135; AAN06509.1; -; Genomic_DNA.
DR EMBL; AE014135; AAX52511.2; -; Genomic_DNA.
DR EMBL; AY075429; AAL68245.1; -; mRNA.
DR EMBL; AY118860; AAM50720.1; ALT_INIT; mRNA.
DR RefSeq; NP_001014691.2; NM_001014691.2. [Q8SY33-3]
DR RefSeq; NP_726596.1; NM_166780.2. [Q8SY33-1]
DR RefSeq; NP_726597.1; NM_166781.2. [Q8SY33-1]
DR RefSeq; NP_726599.2; NM_166783.2.
DR RefSeq; NP_726600.1; NM_166784.2. [Q8SY33-1]
DR RefSeq; NP_726601.1; NM_166785.2. [Q8SY33-1]
DR PDB; 2WBR; NMR; -; A=1114-1198.
DR PDBsum; 2WBR; -.
DR AlphaFoldDB; Q8SY33; -.
DR SMR; Q8SY33; -.
DR BioGRID; 68639; 22.
DR DIP; DIP-35525N; -.
DR ELM; Q8SY33; -.
DR IntAct; Q8SY33; 12.
DR MINT; Q8SY33; -.
DR STRING; 7227.FBpp0088165; -.
DR PaxDb; Q8SY33; -.
DR PRIDE; Q8SY33; -.
DR ABCD; Q8SY33; 14 sequenced antibodies.
DR DNASU; 43808; -.
DR EnsemblMetazoa; FBtr0089096; FBpp0088165; FBgn0051992. [Q8SY33-1]
DR EnsemblMetazoa; FBtr0089097; FBpp0088166; FBgn0051992. [Q8SY33-1]
DR EnsemblMetazoa; FBtr0089100; FBpp0088169; FBgn0051992. [Q8SY33-1]
DR EnsemblMetazoa; FBtr0089101; FBpp0088170; FBgn0051992. [Q8SY33-1]
DR EnsemblMetazoa; FBtr0310543; FBpp0302680; FBgn0051992. [Q8SY33-3]
DR GeneID; 43808; -.
DR KEGG; dme:Dmel_CG31992; -.
DR UCSC; CG31992-RA; d. melanogaster. [Q8SY33-1]
DR CTD; 43808; -.
DR FlyBase; FBgn0051992; gw.
DR VEuPathDB; VectorBase:FBgn0051992; -.
DR eggNOG; ENOG502QWFQ; Eukaryota.
DR InParanoid; Q8SY33; -.
DR OMA; ANSWDKV; -.
DR PhylomeDB; Q8SY33; -.
DR Reactome; R-DME-426496; Post-transcriptional silencing by small RNAs.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR SignaLink; Q8SY33; -.
DR BioGRID-ORCS; 43808; 1 hit in 3 CRISPR screens.
DR ChiTaRS; gw; fly.
DR EvolutionaryTrace; Q8SY33; -.
DR GenomeRNAi; 43808; -.
DR PRO; PR:Q8SY33; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0051992; Expressed in cleaving embryo and 24 other tissues.
DR Genevisible; Q8SY33; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:FlyBase.
DR GO; GO:0016442; C:RISC complex; IPI:FlyBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:FlyBase.
DR GO; GO:0001700; P:embryonic development via the syncytial blastoderm; IDA:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IMP:UniProtKB.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IEA:InterPro.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:FlyBase.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR CDD; cd14284; UBA_GAWKY; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR019486; Argonaute_hook_dom.
DR InterPro; IPR041971; Gawky_UBA.
DR InterPro; IPR033503; GW182.
DR InterPro; IPR026805; GW182_M_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR13020:SF25; PTHR13020:SF25; 1.
DR Pfam; PF10427; Ago_hook; 1.
DR Pfam; PF12938; M_domain; 1.
DR Pfam; PF00627; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Translation regulation.
FT CHAIN 1..1384
FT /note="Protein Gawky"
FT /id="PRO_0000415948"
FT DOMAIN 547..588
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 1117..1189
FT /note="RRM"
FT /evidence="ECO:0000255"
FT REGION 1..605
FT /note="Sufficient for miRNA-mediated silencing"
FT /evidence="ECO:0000269|PubMed:19304924"
FT REGION 1..205
FT /note="Required for interaction with AGO1"
FT /evidence="ECO:0000269|PubMed:20530530"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..490
FT /note="Minimal N-terminal region required for miRNA-
FT mediated silencing"
FT /evidence="ECO:0000269|PubMed:20530530"
FT REGION 263..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..830
FT /note="Sufficient for miRNA-mediated silencing"
FT /evidence="ECO:0000269|PubMed:19304924"
FT REGION 607..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..1115
FT /note="Not required for interaction with AGO1 or miRNAs or
FT for localization to P-bodies but necessary for miRNA-
FT mediated silencing and for interaction with pAbp"
FT /evidence="ECO:0000269|PubMed:19383769,
FT ECO:0000269|PubMed:19797087, ECO:0000269|PubMed:20530530"
FT REGION 889..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1215
FT /note="Sufficient for miRNA-mediated silencing"
FT /evidence="ECO:0000269|PubMed:19304924"
FT REGION 962..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1384
FT /note="Not required for interaction with AGO1 or miRNAs or
FT for localization to P-bodies but necessary for miRNA-
FT mediated silencing, dissociation from AGO1 and miRNAs and
FT interaction with pAbp"
FT /evidence="ECO:0000269|PubMed:19383769,
FT ECO:0000269|PubMed:19797087, ECO:0000269|PubMed:20530530"
FT REGION 1318..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 969..971
FT /note="Missing (in isoform I)"
FT /evidence="ECO:0000305"
FT /id="VSP_047895"
FT VAR_SEQ 1035..1036
FT /note="Missing (in isoform J)"
FT /evidence="ECO:0000305"
FT /id="VSP_047896"
FT STRAND 1118..1122
FT /evidence="ECO:0007829|PDB:2WBR"
FT HELIX 1131..1140
FT /evidence="ECO:0007829|PDB:2WBR"
FT STRAND 1143..1149
FT /evidence="ECO:0007829|PDB:2WBR"
FT TURN 1150..1153
FT /evidence="ECO:0007829|PDB:2WBR"
FT STRAND 1154..1161
FT /evidence="ECO:0007829|PDB:2WBR"
FT HELIX 1162..1172
FT /evidence="ECO:0007829|PDB:2WBR"
FT STRAND 1175..1177
FT /evidence="ECO:0007829|PDB:2WBR"
FT STRAND 1180..1185
FT /evidence="ECO:0007829|PDB:2WBR"
FT HELIX 1189..1196
FT /evidence="ECO:0007829|PDB:2WBR"
SQ SEQUENCE 1384 AA; 142973 MW; 4E87DFE49050883E CRC64;
MREALFSQDG WGCQHVNQDT NWEVPSSPEP ANKDAPGPPM WKPSINNGTD LWESNLRNGG
QPAAQQVPKP SWGHTPSSNL GGTWGEDDDG ADSSSVWTGG AVSNAGSGAA VGVNQAGVNV
GPGGVVSSGG PQWGQGVVGV GLGSTGGNGS SNITGSSGVA TGSSGNSSNA GNGWGDPREI
RPLGVGGSMD IRNVEHRGGN GSGATSSDPR DIRMIDPRDP IRGDPRGISG RLNGTSEMWG
HHPQMSHNQL QGINKMVGQS VATASTSVGT SGSGIGPGGP GPSTVSGNIP TQWGPAQPVS
VGVSGPKDMS KQISGWEEPS PPPQRRSIPN YDDGTSLWGQ QTRVPAASGH WKDMTDSIGR
SSHLMRGQSQ TGGIGIAGVG NSNVPVGANP SNPISSVVGP QARIPSVGGV QHKPDGGAMW
VHSGNVGGRN NVAAVTTWGD DTHSVNVGAP SSGSVSSNNW VDDKSNSTLA QNSWSDPAPV
GVSWGNKQSK PPSNSASSGW STAAGVVDGV DLGSEWNTHG GIIGKSQQQQ KLAGLNVGMV
NVINAEIIKQ SKQYRILVEN GFKKEDVERA LVIANMNIEE AADMLRANSS LSMDGWRRHD
ESLGSYADHN SSTSSGGFAG RYPVNSGQPS MSFPHNNLMN NMGGTAVTGG NNNTNMTALQ
VQKYLNQGQH GVAVGPQAVG NSSAVSVGFG QNTSNAAVAG AASVNIAANT NNQPSGQQIR
MLGQQIQLAI HSGFISSQIL TQPLTQTTLN LLNQLLSNIK HLQAAQQSLT RGGNVNPMAV
NVAISKYKQQ IQNLQNQINA QQAVYVKQQN MQPTSQQQQP QQQQLPSVHL SNSGNDYLRG
HDAINNLQSN FSELNINKPS GYQGASNQQS RLNQWKLPVL DKEINSDSTE FSRAPGATKQ
NLTANTSNIN SLGLQNDSTW STGRSIGDGW PDPSSDNENK DWSVAQPTSA ATAYTDLVQE
FEPGKPWKGS QIKSIEDDPS ITPGSVARSP LSINSTPKDA DIFANTGKNS PTDLPPLSLS
SSTWSFNPNQ NYPSHSWSDN SQQCTATSEL WTSPLNKSSS RGPPPGLTAN SNKSANSNAS
TPTTITGGAN GWLQPRSGGV QTTNTNWTGG NTTWGSSWLL LKNLTAQIDG PTLRTLCMQH
GPLVSFHPYL NQGIALCKYT TREEANKAQM ALNNCVLANT TIFAESPSEN EVQSIMQHLP
QTPSSTSSSG TSGGNVGGVG TSANNANSGS AACLSGNNSG NGNGSASGAG SGNNGNSSCN
NSAAGGGSSS NNTITTVANS NLVGSSGSVS NSSGVTANSS TVSVVSCTAS GNSINGAGTA
NSSGSKSSAN NLASGQSSAS NLTNSTNSTW RQTSQNQALQ SQSRPSGREA DFDYISLVYS
IVDD
