PUM1_MOUSE
ID PUM1_MOUSE Reviewed; 1189 AA.
AC Q80U78; Q80X96; Q80YU8; Q8BPV7; Q9EPU6;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Pumilio homolog 1 {ECO:0000305};
GN Name=Pum1 {ECO:0000312|MGI:MGI:1931749};
GN Synonyms=Kiaa0099 {ECO:0000303|PubMed:12693553};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12667987; DOI=10.1016/s1079-9796(03)00003-2;
RA Spassov D.S., Jurecic R.;
RT "Mouse Pum1 and Pum2 genes, members of the Pumilio family of RNA-binding
RT proteins, show differential expression in fetal and adult hematopoietic
RT stem cells and progenitors.";
RL Blood Cells Mol. Dis. 30:55-69(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-710, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-124; SER-229 AND
RP SER-710, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=22342750; DOI=10.1016/j.cub.2012.01.039;
RA Chen D., Zheng W., Lin A., Uyhazi K., Zhao H., Lin H.;
RT "Pumilio 1 suppresses multiple activators of p53 to safeguard
RT spermatogenesis.";
RL Curr. Biol. 22:420-425(2012).
RN [9]
RP FUNCTION.
RX PubMed=24412312; DOI=10.1016/j.stem.2013.12.008;
RA Leeb M., Dietmann S., Paramor M., Niwa H., Smith A.;
RT "Genetic exploration of the exit from self-renewal using haploid embryonic
RT stem cells.";
RL Cell Stem Cell 14:385-393(2014).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25768905; DOI=10.1016/j.cell.2015.02.012;
RA Gennarino V.A., Singh R.K., White J.J., De Maio A., Han K., Kim J.Y.,
RA Jafar-Nejad P., di Ronza A., Kang H., Sayegh L.S., Cooper T.A., Orr H.T.,
RA Sillitoe R.V., Zoghbi H.Y.;
RT "Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
RT increasing wild-type Ataxin1 levels.";
RL Cell 160:1087-1098(2015).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=29474920; DOI=10.1016/j.cell.2018.02.006;
RA Gennarino V.A., Palmer E.E., McDonell L.M., Wang L., Adamski C.J.,
RA Koire A., See L., Chen C.A., Schaaf C.P., Rosenfeld J.A., Panzer J.A.,
RA Moog U., Hao S., Bye A., Kirk E.P., Stankiewicz P., Breman A.M.,
RA McBride A., Kandula T., Dubbs H.A., Macintosh R., Cardamone M., Zhu Y.,
RA Ying K., Dias K.R., Cho M.T., Henderson L.B., Baskin B., Morris P., Tao J.,
RA Cowley M.J., Dinger M.E., Roscioli T., Caluseriu O., Suchowersky O.,
RA Sachdev R.K., Lichtarge O., Tang J., Boycott K.M., Holder J.L. Jr.,
RA Zoghbi H.Y.;
RT "A mild PUM1 mutation is associated with adult-onset ataxia, whereas
RT haploinsufficiency causes developmental delay and seizures.";
RL Cell 172:924-936(2018).
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 Mediates post-transcriptional repression of transcripts via different
CC mechanisms: acts via direct recruitment of the CCR4-POP2-NOT
CC deadenylase leading to translational inhibition and mRNA degradation.
CC Also mediates deadenylation-independent repression by promoting
CC accessibility of miRNAs. Following growth factor stimulation,
CC phosphorylated and binds to the 3'-UTR of CDKN1B/p27 mRNA, inducing a
CC local conformational change that exposes miRNA-binding sites, promoting
CC association of miR-221 and miR-222, efficient suppression of CDKN1B/p27
CC expression, and rapid entry to the cell cycle (By similarity). Acts as
CC a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR
CC and facilitating miRNA regulation (By similarity). Represses a program
CC of genes necessary to maintain genomic stability such as key mitotic,
CC DNA repair and DNA replication factors. Its ability to repress those
CC target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated
CC by DNA damage) which, due to its high abundance and multitude of
CC PUMILIO binding sites, is able to sequester a significant fraction of
CC PUM1 and PUM2 in the cytoplasm (By similarity). Involved in neuronal
CC functions by regulating ATXN1 mRNA levels: acts by binding to the 3'-
CC UTR of ATXN1 transcripts, leading to their down-regulation
CC independently of the miRNA machinery (PubMed:25768905). In testis, acts
CC as a post-transcriptional regulator of spermatogenesis by binding to
CC the 3'-UTR of mRNAs coding for regulators of p53/TP53
CC (PubMed:22342750). Involved in embryonic stem cell renewal by
CC facilitating the exit from the ground state: acts by targeting mRNAs
CC coding for naive pluripotency transcription factors and accelerates
CC their down-regulation at the onset of differentiation
CC (PubMed:24412312). Binds specifically to miRNA MIR199A precursor, with
CC PUM2, regulates miRNA MIR199A expression at a postranscriptional level
CC (By similarity). {ECO:0000250|UniProtKB:Q14671,
CC ECO:0000269|PubMed:22342750, ECO:0000269|PubMed:24412312,
CC ECO:0000269|PubMed:25768905}.
CC -!- SUBUNIT: Recruits the CCR4-POP2-NOT deadenylase leading to
CC translational inhibition and mRNA degradation (By similarity).
CC Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q14671}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22342750}.
CC Cytoplasm, P-body {ECO:0000250|UniProtKB:Q14671}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q14671}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80U78-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80U78-2; Sequence=VSP_009317, VSP_009318;
CC Name=3;
CC IsoId=Q80U78-3; Sequence=VSP_009317;
CC Name=4;
CC IsoId=Q80U78-4; Sequence=VSP_009315, VSP_009316;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart,
CC kidney, liver, lung, skin, intestine, spleen, testis and thymus. Weakly
CC or not expressed in muscles and stomach. Expressed at various stages of
CC myeloid and lymphoid cell development (PubMed:12667987). Highly
CC expressed in testis (PubMed:22342750). Expressed in all major brain
CC regions (at protein level) (PubMed:25768905).
CC {ECO:0000269|PubMed:12667987, ECO:0000269|PubMed:22342750,
CC ECO:0000269|PubMed:25768905}.
CC -!- DEVELOPMENTAL STAGE: During the development of the testis, expressed 2
CC days postpartum (dpp) and then starts to increase at 14 dpp when
CC pachytene spermatocytes first appear. {ECO:0000269|PubMed:22342750}.
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. PUM1 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 -!- PTM: Phosphorylation at Ser-715 promotes RNA-binding activity.
CC Following growth factor stimulation phosphorylated at Ser-715,
CC promoting binding to the 3'-UTR of CDKN1B/p27 mRNA.
CC {ECO:0000250|UniProtKB:Q14671}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and grow to adulthood without
CC apparent defects except that they are smaller than wild-type mice at 8
CC weeks of age (PubMed:22342750, PubMed:25768905). Males mice however
CC show significantly reduced sperm counts and fertility: testicular
CC hypoplasia is observed (PubMed:22342750). Heterozygous knockout mice
CC manifest neurological dysfunction, hyperactivity, and progressive
CC cerebellar signs including gross and fine motor incoordination
CC (PubMed:25768905, PubMed:29474920). They show spontaneous seizures,
CC abnormal EEG activity with generalized epileptiform spikes by the age
CC of 16 weeks, and have smaller than normal cerebella (PubMed:29474920).
CC {ECO:0000269|PubMed:22342750, ECO:0000269|PubMed:25768905,
CC ECO:0000269|PubMed:29474920}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65487.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF321909; AAG42319.1; -; mRNA.
DR EMBL; AK122205; BAC65487.1; ALT_INIT; mRNA.
DR EMBL; AK052145; BAC34857.1; -; mRNA.
DR EMBL; BC048174; AAH48174.1; -; mRNA.
DR EMBL; BC050747; AAH50747.1; -; mRNA.
DR CCDS; CCDS18710.1; -. [Q80U78-1]
DR CCDS; CCDS51311.1; -. [Q80U78-2]
DR CCDS; CCDS51312.1; -. [Q80U78-3]
DR RefSeq; NP_001153075.1; NM_001159603.1. [Q80U78-2]
DR RefSeq; NP_001153076.1; NM_001159604.1. [Q80U78-3]
DR RefSeq; NP_109647.2; NM_030722.2. [Q80U78-1]
DR AlphaFoldDB; Q80U78; -.
DR SMR; Q80U78; -.
DR BioGRID; 219849; 2.
DR IntAct; Q80U78; 4.
DR MINT; Q80U78; -.
DR STRING; 10090.ENSMUSP00000030315; -.
DR iPTMnet; Q80U78; -.
DR PhosphoSitePlus; Q80U78; -.
DR EPD; Q80U78; -.
DR jPOST; Q80U78; -.
DR MaxQB; Q80U78; -.
DR PaxDb; Q80U78; -.
DR PeptideAtlas; Q80U78; -.
DR PRIDE; Q80U78; -.
DR ProteomicsDB; 301922; -. [Q80U78-1]
DR ProteomicsDB; 301923; -. [Q80U78-2]
DR ProteomicsDB; 301924; -. [Q80U78-3]
DR ProteomicsDB; 301925; -. [Q80U78-4]
DR Antibodypedia; 16718; 280 antibodies from 33 providers.
DR DNASU; 80912; -.
DR Ensembl; ENSMUST00000030315; ENSMUSP00000030315; ENSMUSG00000028580. [Q80U78-1]
DR Ensembl; ENSMUST00000097862; ENSMUSP00000095474; ENSMUSG00000028580. [Q80U78-3]
DR Ensembl; ENSMUST00000097864; ENSMUSP00000095476; ENSMUSG00000028580. [Q80U78-2]
DR GeneID; 80912; -.
DR KEGG; mmu:80912; -.
DR UCSC; uc008uzl.2; mouse. [Q80U78-4]
DR UCSC; uc008uzm.3; mouse. [Q80U78-1]
DR UCSC; uc008uzn.3; mouse. [Q80U78-2]
DR CTD; 9698; -.
DR MGI; MGI:1931749; Pum1.
DR VEuPathDB; HostDB:ENSMUSG00000028580; -.
DR eggNOG; KOG1488; Eukaryota.
DR GeneTree; ENSGT00940000158079; -.
DR InParanoid; Q80U78; -.
DR OMA; YRNAASS; -.
DR OrthoDB; 207351at2759; -.
DR PhylomeDB; Q80U78; -.
DR TreeFam; TF318160; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 80912; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Pum1; mouse.
DR PRO; PR:Q80U78; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80U78; protein.
DR Bgee; ENSMUSG00000028580; Expressed in embryonic brain and 82 other tissues.
DR ExpressionAtlas; Q80U78; baseline and differential.
DR Genevisible; Q80U78; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:UniProtKB.
DR GO; GO:0035196; P:miRNA processing; ISS:UniProtKB.
DR GO; GO:0061157; P:mRNA destabilization; IDA:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; ISO:MGI.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IMP:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0051983; P:regulation of chromosome segregation; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
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 Acetylation; Alternative splicing; Cytoplasm; Differentiation; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spermatogenesis;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT CHAIN 2..1189
FT /note="Pumilio homolog 1"
FT /id="PRO_0000075918"
FT DOMAIN 829..1171
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 849..884
FT /note="Pumilio 1"
FT REPEAT 885..920
FT /note="Pumilio 2"
FT REPEAT 921..958
FT /note="Pumilio 3"
FT REPEAT 959..994
FT /note="Pumilio 4"
FT REPEAT 995..1030
FT /note="Pumilio 5"
FT REPEAT 1031..1066
FT /note="Pumilio 6"
FT REPEAT 1067..1102
FT /note="Pumilio 7"
FT REPEAT 1106..1145
FT /note="Pumilio 8"
FT REGION 22..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..868
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 900..904
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 936..940
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 974..978
FT /note="Non-specific-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1010..1014
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1046..1050
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1082..1086
FT /note="Guanine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1083..1086
FT /note="Guanine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1125..1129
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT COMPBIAS 33..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB72"
FT MOD_RES 515
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB72"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 797
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT VAR_SEQ 181..189
FT /note="DHSVSQPIM -> GNLALASLL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009315"
FT VAR_SEQ 190..1189
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009316"
FT VAR_SEQ 418
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009317"
FT VAR_SEQ 952..953
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009318"
FT CONFLICT 186
FT /note="Q -> H (in Ref. 1; AAG42319)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="A -> D (in Ref. 1; AAG42319)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="P -> T (in Ref. 1; AAG42319)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="A -> G (in Ref. 1; AAG42319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1189 AA; 126619 MW; CCB18634FBE3468A CRC64;
MSVACVLKRK AVLWQDSFSP HLKHHPQEPA NPNMPVVLTS GTGSQAQPQP AANQALAAGT
HSSPVPGSIG VAGRSQDDAM VDYFFQRQHG EQLGGGGSGG GGYNTSKHRW PTGDNIHAEH
QVRSMDELNH DFQALALEGR AMGEQLLPGK KFWETDESSK DGPKGIFLGD QWRDSAWGTS
DHSVSQPIMV QRRPGQSFHV NSEVNSVLSP RSESGGLGVS MVEYVLSSSP GDSCLRKGGF
GPRDADSDEN DKGEKKNKGT FDGDKLGDLK EEGDVMDKTN GLPVQNGIDA DVKDFSRTPG
NCQNSANEVD LLGPNQNGSE GLAQLTSTNG AKPVEDFSNM ESQSVPLDPM EHVGMEPLQF
DYSGTQVPVD SAAATVGLFD YNSQQQLFQR PNALAVQQLT AAQQQQYALA AAHQPHIAGL
APAAFVPNPY IISAAPPGTD PYTAGLAAAA TLGPAVVPHQ YYGVTPWGVY PASLFQQQAA
AAAAATNSAT QQSAPQAQQG QQQVLRGGAS QRPLTPNQNQ QGQQTDPLVA AAAVNSALAF
GQGLAAGMPG YPVLAPAAYY DQTGALVVNA GARNGLGAPV RLVAPAPVII SSSAAQAAVA
AAAASANGAA GGLAGTTNGP FRPLGTQQPQ PQPQQQPSNN LASSSFYGNN SLSSNSQSSS
LFSQGSAQPA NTSLGFGSSS SLGATLGSAL GGFGTAVANS NTGSGSRRDS LTGSSDLYKR
TSSSLAPIGH SFYSSLSYSS SPGPVGMPLP SQGPGHSQTP PPSLSSHGSS SSLNLGGLTN
GSGRYISAAP GAEAKYRSAS SASSLFSPSS TLFSSSRLRY GMSDVMPSGR SRLLEDFRNN
RYPNLQLREI AGHIMEFSQD QHGSRFIQLK LERATAAERQ LVFNEILQAA YQLMVDVFGN
YVIQKFFEFG SHEQKLALAE RIRGHVLSLA LQMYGCRVIQ KALEFIPSDQ QVINEMVREL
DGHVLKCVKD QNGNHVVQKC IECVQPQSLQ FIIDAFKGQV FALSTHPYGC RVIQRILEHC
LPDQTLPILE ELHQHTEQLV QDQYGNYVIQ HVLEHGRPED KSKIVAEIRG NVLVLSQHKF
ASNVVEKCVT HASRTERAVL IDEVCTMNDG PHSALYTMMK DQYANYVVQK MIDVAEPGQR
KIVMHKIRPH IATLRKYTYG KHILAKLEKY YMKNGVDLGP ICGPPNGII
