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   27-MAR-2024, entry version 161.
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,
RC   Spleen, 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; 4.
DR   IntAct; Q80U78; 4.
DR   MINT; Q80U78; -.
DR   STRING; 10090.ENSMUSP00000030315; -.
DR   GlyGen; Q80U78; 7 sites, 1 O-linked glycan (7 sites).
DR   iPTMnet; Q80U78; -.
DR   PhosphoSitePlus; Q80U78; -.
DR   EPD; Q80U78; -.
DR   jPOST; Q80U78; -.
DR   MaxQB; Q80U78; -.
DR   PaxDb; 10090-ENSMUSP00000030315; -.
DR   PeptideAtlas; Q80U78; -.
DR   ProteomicsDB; 301922; -. [Q80U78-1]
DR   ProteomicsDB; 301923; -. [Q80U78-2]
DR   ProteomicsDB; 301924; -. [Q80U78-3]
DR   ProteomicsDB; 301925; -. [Q80U78-4]
DR   Pumba; Q80U78; -.
DR   Antibodypedia; 16718; 315 antibodies from 33 providers.
DR   DNASU; 80912; -.
DR   Ensembl; ENSMUST00000030315.13; ENSMUSP00000030315.7; ENSMUSG00000028580.16. [Q80U78-1]
DR   Ensembl; ENSMUST00000097862.3; ENSMUSP00000095474.3; ENSMUSG00000028580.16. [Q80U78-3]
DR   Ensembl; ENSMUST00000097864.9; ENSMUSP00000095476.3; ENSMUSG00000028580.16. [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   AGR; MGI:1931749; -.
DR   CTD; 9698; -.
DR   MGI; MGI:1931749; Pum1.
DR   VEuPathDB; HostDB:ENSMUSG00000028580; -.
DR   eggNOG; KOG1488; Eukaryota.
DR   GeneTree; ENSGT00940000158079; -.
DR   InParanoid; Q80U78; -.
DR   OMA; ADVKDFX; -.
DR   OrthoDB; 5472666at2759; -.
DR   PhylomeDB; Q80U78; -.
DR   TreeFam; TF318160; -.
DR   Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR   BioGRID-ORCS; 80912; 7 hits in 76 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 85 other cell types or tissues.
DR   ExpressionAtlas; Q80U78; baseline and differential.
DR   GO; GO:0030424; C:axon; ISO:MGI.
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: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:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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; Leucine-rich Repeat Variant; 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   PANTHER; PTHR12537:SF1; PUMILIO HOMOLOG 1; 1.
DR   PANTHER; PTHR12537; RNA BINDING PROTEIN PUMILIO-RELATED; 1.
DR   Pfam; PF00806; PUF; 8.
DR   SMART; SM00025; Pumilio; 8.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50302; PUM; 8.
DR   PROSITE; PS50303; PUM_HD; 1.
DR   Genevisible; Q80U78; MM.
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
//