PUM3_ARATH
ID PUM3_ARATH Reviewed; 964 AA.
AC Q9ZW02;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Pumilio homolog 3;
DE Short=APUM-3;
DE Short=AtPUM3;
GN Name=APUM3; OrderedLocusNames=At2g29140; ORFNames=F16P2.48;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, FUNCTION, AND RNA-BINDING.
RX PubMed=19682068; DOI=10.1111/j.1742-4658.2009.07230.x;
RA Francischini C.W., Quaggio R.B.;
RT "Molecular characterization of Arabidopsis thaliana PUF proteins -- binding
RT specificity and target candidates.";
RL FEBS J. 276:5456-5470(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [5]
RP GENE FAMILY.
RX PubMed=20214804; DOI=10.1186/1471-2229-10-44;
RA Tam P.P., Barrette-Ng I.H., Simon D.M., Tam M.W., Ang A.L., Muench D.G.;
RT "The Puf family of RNA-binding proteins in plants: phylogeny, structural
RT modeling, activity and subcellular localization.";
RL BMC Plant Biol. 10:44-44(2010).
CC -!- FUNCTION: Sequence-specific RNA-binding protein that regulates
CC translation and mRNA stability by binding the 3'-UTR of target mRNAs.
CC Binds the APUM-binding elements (APBEs) in the 3'-UTR mRNA sequence of
CC CLV1, PNH, WUS and FAS2. {ECO:0000269|PubMed:19682068}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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. The number as well as the specific sequence of the repeats
CC determine the specificity for target mRNAs (By similarity).
CC {ECO:0000250}.
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DR EMBL; AC004561; AAC95220.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08216.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61937.1; -; Genomic_DNA.
DR PIR; A84693; A84693.
DR RefSeq; NP_001324126.1; NM_001336202.1.
DR RefSeq; NP_180478.1; NM_128471.4.
DR AlphaFoldDB; Q9ZW02; -.
DR SMR; Q9ZW02; -.
DR STRING; 3702.AT2G29140.1; -.
DR iPTMnet; Q9ZW02; -.
DR PaxDb; Q9ZW02; -.
DR PRIDE; Q9ZW02; -.
DR ProteomicsDB; 226356; -.
DR EnsemblPlants; AT2G29140.1; AT2G29140.1; AT2G29140.
DR EnsemblPlants; AT2G29140.2; AT2G29140.2; AT2G29140.
DR GeneID; 817463; -.
DR Gramene; AT2G29140.1; AT2G29140.1; AT2G29140.
DR Gramene; AT2G29140.2; AT2G29140.2; AT2G29140.
DR KEGG; ath:AT2G29140; -.
DR Araport; AT2G29140; -.
DR TAIR; locus:2043047; AT2G29140.
DR eggNOG; KOG1488; Eukaryota.
DR HOGENOM; CLU_004017_1_1_1; -.
DR InParanoid; Q9ZW02; -.
DR OMA; MLGASHL; -.
DR OrthoDB; 206600at2759; -.
DR PhylomeDB; Q9ZW02; -.
DR PRO; PR:Q9ZW02; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW02; baseline and differential.
DR Genevisible; Q9ZW02; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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; IPR012940; NABP.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR033712; Pumilio_RNA-bd.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR Pfam; PF07990; NABP; 2.
DR Pfam; PF00806; PUF; 8.
DR SMART; SM00025; Pumilio; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50302; PUM; 9.
DR PROSITE; PS50303; PUM_HD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Translation regulation.
FT CHAIN 1..964
FT /note="Pumilio homolog 3"
FT /id="PRO_0000401385"
FT DOMAIN 606..946
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 626..661
FT /note="Pumilio 1"
FT REPEAT 662..697
FT /note="Pumilio 2"
FT REPEAT 698..733
FT /note="Pumilio 3"
FT REPEAT 734..769
FT /note="Pumilio 4"
FT REPEAT 770..806
FT /note="Pumilio 5"
FT REPEAT 807..842
FT /note="Pumilio 6"
FT REPEAT 843..878
FT /note="Pumilio 7"
FT REPEAT 879..920
FT /note="Pumilio 8"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SS47"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 964 AA; 105987 MW; 40E3FFB1B5A6E43A CRC64;
MMIPELGRRP MHRGNEDSSF GDDYEKEIGV LLGEQQRRQV EADELERELN LYRSGSAPPT
VDGSLSAAGG LFSGGGGASF LEFGGVNKGN GFGGDDEEFR KDPAYLSYYY ANMKLNPRLP
PPLMSREDLR VAQRLKGSNN VLGGVGDRRK VNDSRSLFSM PPGFEAGKPG ASASEWDANG
LIGLGLGGKQ KSFADIFQAD MGHPVVQQPS RPASRNTFDE NVDSNNNLSP SASQGIGAPS
PYCYAAVLGS SLSRNGTPDP QGIARVPSPC LTPIGSGRVS SNDKRNTSNQ SPFNGVTSGL
NESSDLVNAL SGLNLSGTGG LDERGQAEQD VEKVRNYMFG LQDGHNEVNP HGFPNRSDQA
RGTASCRNSQ MRGSQGSAYN SGSGVANPYQ HHDSPNYYAL NPAVASMMAN QLGTNNYSPM
YENASATLGY SAMDSRLHGG SFVSSGQNLS ESRNIGRVGN RMMEGGTGHP SHLADPMYHQ
YARFSENADS FDLLNDPSMD RNYGNSYMNM LEIQRAYLGS QKSQYGLPYK SGSPNSHSYY
GSPTFGSNMS YPGSPLAHHG MPNSLMSPYS PMRRGEVNMR YPAATRNYTG GVMGSWHMDA
SLDEGFGSSM LEEFKSNKTR GFELSEIAGH VVEFSSDQYG SRFIQQKLET ATTDEKNMVY
EEIMPKALAL MTDVFGNYVI QKFFEHGLPP QRRELGEKLI DNVLPLSLQM YGCRVIQKAI
EVVDLDQKIQ MVKELDGHVM RCVRDQNGNH VVQKCIECVP EENIEFIIST FFGHVVTLST
HPYGCRVIQR VLEHCHNPDT QSKVMEEILS TVSMLTQDQY GNYVVQHVLE HGKPDERTVI
IKELAGKIVQ MSQQKFASNV VEKCLTFGGP EERELLVNEM LGTTDENEPL QAMMKDQFAN
YVVQKVLETC DDQQRELILT RIKVHLNALK KYTYGKHIVA RVEKLVAAGE RRMALQSLPQ
PLVA
