PUM_DROME
ID PUM_DROME Reviewed; 1533 AA.
AC P25822; A4V2K5; Q5BIA7; Q7YU65; Q8IGA8; Q9VHH4; Q9VHH6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Maternal protein pumilio;
GN Name=pum; ORFNames=CG9755;
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, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=1576962; DOI=10.1242/dev.114.1.221;
RA Macdonald P.M.;
RT "The Drosophila pumilio gene: an unusually long transcription unit and an
RT unusual protein.";
RL Development 114:221-232(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=1459455; DOI=10.1101/gad.6.12a.2312;
RA Barker D.D., Wang C., Moore J., Dickinson L.K., Lehmann R.;
RT "Pumilio is essential for function but not for distribution of the
RT Drosophila abdominal determinant Nanos.";
RL Genes Dev. 6:2312-2326(1992).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND E).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP RNA-BINDING, AND FUNCTION.
RX PubMed=9404893;
RA Zamore P.D., Williamson J.R., Lehmann R.;
RT "The Pumilio protein binds RNA through a conserved domain that defines a
RT new class of RNA-binding proteins.";
RL RNA 3:1421-1433(1997).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLY-1330.
RX PubMed=9660969; DOI=10.1016/s1097-2765(00)80085-4;
RA Wharton R.P., Sonoda J., Lee T., Patterson M., Murata Y.;
RT "The Pumilio RNA-binding domain is also a translational regulator.";
RL Mol. Cell 1:863-872(1998).
RN [9]
RP INTERACTION WITH NOS, AND RNA-BINDING.
RX PubMed=10541556; DOI=10.1101/gad.13.20.2704;
RA Sonoda J., Wharton R.P.;
RT "Recruitment of Nanos to hunchback mRNA by Pumilio.";
RL Genes Dev. 13:2704-2712(1999).
RN [10]
RP INTERACTION WITH BRAT AND NOS.
RX PubMed=11274060; DOI=10.1101/gad.870801;
RA Sonoda J., Wharton R.P.;
RT "Drosophila Brain tumor is a translational repressor.";
RL Genes Dev. 15:762-773(2001).
RN [11]
RP 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).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453; SER-468; SER-470;
RP SER-477 AND SER-505, 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 [13]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=22345517; DOI=10.1101/gad.182568.111;
RA Miles W.O., Tschop K., Herr A., Ji J.Y., Dyson N.J.;
RT "Pumilio facilitates miRNA regulation of the E2F3 oncogene.";
RL Genes Dev. 26:356-368(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1092-1411, AND MUTAGENESIS OF
RP ARG-1127; LYS-1167; ARG-1199; HIS-1235; GLY-1330; GLU-1346; CYS-1365;
RP THR-1366; PHE-1367 AND ASN-1368.
RX PubMed=11336677; DOI=10.1016/s0092-8674(01)00318-x;
RA Edwards T.A., Pyle S.E., Wharton R.P., Aggarwal A.K.;
RT "Structure of Pumilio reveals similarity between RNA and peptide binding
RT motifs.";
RL Cell 105:281-289(2001).
CC -!- FUNCTION: Sequence-specific RNA-binding protein that acts as a post-
CC transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds
CC to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-
CC UGUANAUA-3', that is related to the Nanos Response Element (NRE)
CC (PubMed:1459455, PubMed:1576962, PubMed:9404893, PubMed:9660969,
CC PubMed:22345517). Mediates post-transcriptional repression of
CC transcripts via different mechanisms: acts via direct recruitment of
CC deadenylase complexes leading to translational inhibition and mRNA
CC degradation (By similarity). Also mediates deadenylation-independent
CC repression by promoting accessibility of miRNAs (PubMed:22345517).
CC Mediates post-transcriptional silencing of E2f mRNA by binding to its
CC 3'-UTR and promoting miRNA regulation (PubMed:22345517). Required for
CC abdominal development and to support proliferation and self-renewal of
CC germ cells. Pum is the only gene required for nos activity that is not
CC also required for posterior localization of germline determinants. Pum
CC is required during embryogenesis when nos activity apparently moves
CC anteriorly from the posterior pole (PubMed:1459455, PubMed:1576962,
CC PubMed:9404893, PubMed:9660969). {ECO:0000250|UniProtKB:Q14671,
CC ECO:0000269|PubMed:1459455, ECO:0000269|PubMed:1576962,
CC ECO:0000269|PubMed:22345517, ECO:0000269|PubMed:9404893,
CC ECO:0000269|PubMed:9660969}.
CC -!- SUBUNIT: Interacts with nos and brat. Acts via the formation of a
CC quaternary complex composed of pum, nos, brat and the 3'-UTR mRNA of
CC hb. {ECO:0000269|PubMed:10541556, ECO:0000269|PubMed:11274060}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1576962}.
CC Cytoplasm, Cytoplasmic ribonucleoprotein granule
CC {ECO:0000269|PubMed:17178403}. Note=It is concentrated in the cortical
CC region of the embryo beneath the nuclei. {ECO:0000269|PubMed:1576962}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A; Synonyms=C, D;
CC IsoId=P25822-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P25822-2; Sequence=VSP_008216, VSP_008217;
CC Name=E;
CC IsoId=P25822-3; Sequence=VSP_009313, VSP_009314;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in
CC embryos. {ECO:0000269|PubMed:1459455, ECO:0000269|PubMed:1576962}.
CC -!- DOMAIN: The pumilio repeats mediate the association with RNA by packing
CC together to form a right-handed superhelix that approximates a half
CC donut. RNA-binding occurs on the concave side of the surface. Pum is
CC composed of 8 pumilio repeats of 36 residues; each repeat binds a
CC single nucleotide in its RNA target. Residues at positions 12 and 16 of
CC the pumilio repeat bind each RNA base via hydrogen bonding or van der
CC Waals contacts with the Watson-Crick edge, while the amino acid at
CC position 13 makes a stacking interaction. The recognition of RNA by
CC pumilio repeats is base specific: cysteine and glutamine at position 12
CC and 16, respectively, bind adenine; asparagine and glutamine bind
CC uracil; and serine and glutamate bind guanine.
CC {ECO:0000250|UniProtKB:Q14671}.
CC -!- DISRUPTION PHENOTYPE: Flies display defective abdomen pattern formation
CC and are embryonic lethal. {ECO:0000269|PubMed:1459455}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX33465.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X62589; CAA44474.1; -; mRNA.
DR EMBL; L07943; AAB59189.1; -; mRNA.
DR EMBL; AE014297; AAF54340.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF54338.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN13409.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13410.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41523.1; -; Genomic_DNA.
DR EMBL; BT001872; AAN71644.1; -; mRNA.
DR EMBL; BT009970; AAQ22439.1; -; mRNA.
DR EMBL; BT021317; AAX33465.1; ALT_FRAME; mRNA.
DR PIR; A46221; A46221.
DR RefSeq; NP_001262403.1; NM_001275474.1. [P25822-1]
DR RefSeq; NP_524285.2; NM_079561.4. [P25822-1]
DR RefSeq; NP_731314.1; NM_169258.3. [P25822-1]
DR RefSeq; NP_731315.1; NM_169259.3. [P25822-1]
DR RefSeq; NP_731316.2; NM_169260.4. [P25822-2]
DR RefSeq; NP_788604.1; NM_176427.3. [P25822-3]
DR PDB; 3H3D; X-ray; 2.30 A; X/Y=1093-1411.
DR PDB; 5KL1; X-ray; 3.70 A; A=1091-1426.
DR PDB; 5KL8; X-ray; 4.00 A; A=1091-1426.
DR PDB; 5KLA; X-ray; 1.14 A; A=1091-1426.
DR PDBsum; 3H3D; -.
DR PDBsum; 5KL1; -.
DR PDBsum; 5KL8; -.
DR PDBsum; 5KLA; -.
DR AlphaFoldDB; P25822; -.
DR SASBDB; P25822; -.
DR SMR; P25822; -.
DR BioGRID; 66261; 58.
DR IntAct; P25822; 4.
DR MINT; P25822; -.
DR STRING; 7227.FBpp0305823; -.
DR iPTMnet; P25822; -.
DR PaxDb; P25822; -.
DR PRIDE; P25822; -.
DR DNASU; 41094; -.
DR EnsemblMetazoa; FBtr0081990; FBpp0081470; FBgn0003165. [P25822-1]
DR EnsemblMetazoa; FBtr0081991; FBpp0081471; FBgn0003165. [P25822-1]
DR EnsemblMetazoa; FBtr0081992; FBpp0081472; FBgn0003165. [P25822-1]
DR EnsemblMetazoa; FBtr0081993; FBpp0081473; FBgn0003165. [P25822-2]
DR EnsemblMetazoa; FBtr0081994; FBpp0081474; FBgn0003165. [P25822-3]
DR EnsemblMetazoa; FBtr0333667; FBpp0305823; FBgn0003165. [P25822-1]
DR GeneID; 41094; -.
DR KEGG; dme:Dmel_CG9755; -.
DR UCSC; CG9755-RA; d. melanogaster. [P25822-1]
DR CTD; 41094; -.
DR FlyBase; FBgn0003165; pum.
DR VEuPathDB; VectorBase:FBgn0003165; -.
DR eggNOG; KOG1488; Eukaryota.
DR GeneTree; ENSGT00940000169170; -.
DR HOGENOM; CLU_004017_0_1_1; -.
DR InParanoid; P25822; -.
DR OMA; YRNAASS; -.
DR PhylomeDB; P25822; -.
DR SignaLink; P25822; -.
DR BioGRID-ORCS; 41094; 1 hit in 3 CRISPR screens.
DR EvolutionaryTrace; P25822; -.
DR GenomeRNAi; 41094; -.
DR PRO; PR:P25822; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003165; Expressed in embryonic/larval hemocyte (Drosophila) and 29 other tissues.
DR ExpressionAtlas; P25822; baseline and differential.
DR Genevisible; P25822; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0097482; C:muscle cell postsynaptic specialization; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061176; C:type Ib terminal bouton; IDA:FlyBase.
DR GO; GO:0061177; C:type Is terminal bouton; IDA:FlyBase.
DR GO; GO:1905762; F:CCR4-NOT complex binding; IDA:FlyBase.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IPI:FlyBase.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IDA:FlyBase.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; TAS:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0016477; P:cell migration; TAS:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; TAS:FlyBase.
DR GO; GO:0008258; P:head involution; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:FlyBase.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0045786; P:negative regulation of cell cycle; TAS:FlyBase.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:FlyBase.
DR GO; GO:0017148; P:negative regulation of translation; TAS:FlyBase.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; TAS:FlyBase.
DR GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR GO; GO:0007280; P:pole cell migration; IMP:FlyBase.
DR GO; GO:1901835; P:positive regulation of deadenylation-independent decapping of nuclear-transcribed mRNA; IMP:FlyBase.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:FlyBase.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:FlyBase.
DR GO; GO:0045727; P:positive regulation of translation; TAS:FlyBase.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IDA:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IBA:GO_Central.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IDA:FlyBase.
DR CDD; cd07920; Pumilio; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR033712; Pumilio_RNA-bd.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR Pfam; PF00806; PUF; 8.
DR SMART; SM00025; Pumilio; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50302; PUM; 8.
DR PROSITE; PS50303; PUM_HD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW Translation regulation.
FT CHAIN 1..1533
FT /note="Maternal protein pumilio"
FT /id="PRO_0000075916"
FT DOMAIN 1091..1428
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 1111..1146
FT /note="Pumilio 1"
FT REPEAT 1147..1182
FT /note="Pumilio 2"
FT REPEAT 1183..1218
FT /note="Pumilio 3"
FT REPEAT 1219..1254
FT /note="Pumilio 4"
FT REPEAT 1255..1290
FT /note="Pumilio 5"
FT REPEAT 1291..1326
FT /note="Pumilio 6"
FT REPEAT 1327..1362
FT /note="Pumilio 7"
FT REPEAT 1366..1402
FT /note="Pumilio 8"
FT REGION 102..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1130
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1162..1166
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1198..1202
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1234..1238
FT /note="Non-specific-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1270..1274
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1306..1310
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1342..1346
FT /note="Guanine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1382..1386
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1494..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..866
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..598
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_009313"
FT VAR_SEQ 1..348
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_008216"
FT VAR_SEQ 349..372
FT /note="AAMMPPQNQYMNSSAVAAANRNAA -> MMKLLHDFILDARTAEDVALTQEM
FT (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_008217"
FT VAR_SEQ 599..659
FT /note="GAYAAHQQMAAQMSQLQPPMMNGVGGGMPMAAQSPMLNHQAAGPNHMESPGN
FT LLQQQNFDV -> MVVLETASALLGGPYAQGAPALKMVQKRYIGLHHWLGPIRSKELKE
FT HIVSDDVLSLAFNHN (in isoform E)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_009314"
FT MUTAGEN 1127
FT /note="R->A: Disrupts RNA-binding."
FT /evidence="ECO:0000269|PubMed:11336677"
FT MUTAGEN 1167
FT /note="K->A: Disrupts RNA-binding."
FT /evidence="ECO:0000269|PubMed:11336677"
FT MUTAGEN 1199
FT /note="R->A: Disrupts RNA-binding."
FT /evidence="ECO:0000269|PubMed:11336677"
FT MUTAGEN 1235
FT /note="H->A: Disrupts RNA-binding."
FT /evidence="ECO:0000269|PubMed:11336677"
FT MUTAGEN 1330
FT /note="G->D: In Pum680; abolishes interaction with brat and
FT translational repression activity but not RNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:11336677,
FT ECO:0000269|PubMed:9660969"
FT MUTAGEN 1346
FT /note="E->K: Disrupts RNA-binding."
FT /evidence="ECO:0000269|PubMed:11336677"
FT MUTAGEN 1365
FT /note="C->R: Abolishes interaction with brat."
FT /evidence="ECO:0000269|PubMed:11336677"
FT MUTAGEN 1366
FT /note="T->D: Abolishes interaction with brat."
FT /evidence="ECO:0000269|PubMed:11336677"
FT MUTAGEN 1367
FT /note="F->S: Abolishes interaction with nos."
FT /evidence="ECO:0000269|PubMed:11336677"
FT MUTAGEN 1368
FT /note="N->S: Abolishes interaction with brat."
FT /evidence="ECO:0000269|PubMed:11336677"
FT CONFLICT 362
FT /note="S -> A (in Ref. 1; CAA44474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1103
FT /note="R -> P (in Ref. 2; AAB59189)"
FT /evidence="ECO:0000305"
FT CONFLICT 1165
FT /note="I -> S (in Ref. 6; AAX33465)"
FT /evidence="ECO:0000305"
FT CONFLICT 1374
FT /note="V -> M (in Ref. 5; AAQ22439)"
FT /evidence="ECO:0000305"
FT CONFLICT 1406..1407
FT /note="PH -> KN (in Ref. 1; CAA44474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1491
FT /note="N -> S (in Ref. 5; AAQ22439)"
FT /evidence="ECO:0000305"
FT CONFLICT 1496
FT /note="V -> I (in Ref. 2; AAB59189)"
FT /evidence="ECO:0000305"
FT CONFLICT 1519
FT /note="S -> G (in Ref. 2; AAB59189)"
FT /evidence="ECO:0000305"
FT HELIX 1094..1100
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1109..1112
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1116..1120
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1123..1133
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1138..1150
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1152..1156
FT /evidence="ECO:0007829|PDB:5KLA"
FT TURN 1159..1161
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1162..1171
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1174..1184
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1188..1192
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1197..1207
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1210..1218
FT /evidence="ECO:0007829|PDB:5KLA"
FT TURN 1219..1222
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1224..1228
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1233..1243
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1246..1249
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1250..1256
FT /evidence="ECO:0007829|PDB:5KLA"
FT TURN 1257..1259
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1260..1264
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1269..1279
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1282..1292
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1296..1300
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1305..1315
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1318..1326
FT /evidence="ECO:0007829|PDB:5KLA"
FT TURN 1327..1330
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1332..1336
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1341..1351
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1354..1365
FT /evidence="ECO:0007829|PDB:5KLA"
FT STRAND 1366..1370
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1371..1377
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1381..1391
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1394..1404
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1405..1407
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1408..1411
FT /evidence="ECO:0007829|PDB:5KLA"
FT TURN 1415..1417
FT /evidence="ECO:0007829|PDB:5KLA"
FT HELIX 1418..1425
FT /evidence="ECO:0007829|PDB:5KLA"
SQ SEQUENCE 1533 AA; 157528 MW; 0A343220BB1F0B27 CRC64;
MKFLGGNDDR NGRGGVGVGT DAIVGSRGGV SQDAADAAGA AAAAAVGYVF QQRPSPGGVG
VGVGGVGGGV PGVGAVGSTL HEAAAAEYAA HFAQKQQQTR WACGDDGHGI DNPDKWKYNP
PMNPANAAPG GPPGNGSNGG PGAIGTIGMG SGLGGGGGGG AGGGNNGGSG TNGGLHHQSM
AAAAANMAAM QQAAALAKHN HMISQAAAAV AAQQQHQHPH QQHPQQQQQQ QQAQNQGHPH
HLMGGGNGLG NGNGLGIQHP GQQQQQQQQQ QQQQHPGQYN ANLLNHAAAL GHMSSYAQSG
GSMYDHHGGA MHPGMNGGMP KQQPLGPPGA GGPQDYVYMG GQTTVPMGAA MMPPQNQYMN
SSAVAAANRN AAITTSTAKK LWEKSDGKGV SSSTPGGPLH PLQIPGIGDP SSVWKDHTWS
TQGENILVPP PSRAYAHGGA SDTSNSGNAG ILSPRDSTCA KVVEYVFSGS PTNKDSSLSG
LEPHLRNLKF DDNDKSRDDK EKANSPFDTN GLKKDDQVTN SNGVVNGIDD DKGFNRTPGS
RQPSPAEESQ PRPPNLLFPP LPFNHMLMDH GQGMGGGLGG VVGSGNGVGG GSGGGGAGGA
YAAHQQMAAQ MSQLQPPMMN GVGGGMPMAA QSPMLNHQAA GPNHMESPGN LLQQQNFDVQ
QLFRSQNPGL AAVATNAAAA AAAAAAATSA ASAAAAVGAP PVPNGSLQQS QQQQQQQQQQ
QQQQQMHMAA ASQQFLAAQQ QAQNAAYAAQ QATSYVINPG QEAAPYMGMI AAAQMPYYGV
APWGMYPGNL IPQQGTQPRR PLTPSQQGAE NQPYQVIPAF LDHTGSLLMG GPRTGTPMRL
VSPAPVLVPP GATRAGPPPP QGPQLYQPQP QTAQQNLYSQ QNGSSVGGLA LNTSSLTGRR
DSFDRSTSAF SPSTMDYTSS GVAAAANAVN STVAQAAAAA AAAAAARGKW PGAMSGAASG
AYGALGAGNA SASPLGAPIT PPPSAQSCLL GSRAPGAESR QRQQQQQQLA AVGLPATAAA
AQAAVAAAAN NMFGSNSSIF SNPLAIPGTA AVAAAAAAAA AANSRQVAAT AAAAAAVAAA
AGGVGGAPQP GRSRLLEDFR NQRYPNLQLR DLANHIVEFS QDQHGSRFIQ QKLERATAAE
KQMVFSEILA AAYSLMTDVF GNYVIQKFFE FGTPEQKNTL GMQVKGHVLQ LALQMYGCRV
IQKALESISP EQQQEIVHEL DGHVLKCVKD QNGNHVVQKC IECVDPVALQ FIINAFKGQV
YSLSTHPYGC RVIQRILEHC TAEQTTPILD ELHEHTEQLI QDQYGNYVIQ HVLEHGKQED
KSILINSVRG KVLVLSQHKF ASNVVEKCVT HATRGERTGL IDEVCTFNDN ALHVMMKDQY
ANYVVQKMID VSEPTQLKKL MTKIRPHMAA LRKYTYGKHI NAKLEKYYMK ITNPITVGTG
AGGVPAASSA AAVSSGATSA SVTACTSGSS TTTTSTTNSL ASPTICSVQE NGSAMVVEPS
SPDASESSSS VVSGAVNSSL GPIGPPTNGN VVL
