PURA_MOUSE
ID PURA_MOUSE Reviewed; 321 AA.
AC P42669;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Transcriptional activator protein Pur-alpha;
DE AltName: Full=Purine-rich single-stranded DNA-binding protein alpha;
GN Name=Pura;
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].
RX PubMed=7959008; DOI=10.1016/0378-1119(94)90167-8;
RA Ma Z.-W., Bergemann A.D., Johnson E.M.;
RT "Conservation in human and mouse Pur alpha of a motif common to several
RT proteins involved in initiation of DNA replication.";
RL Gene 149:311-314(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX PubMed=9334258; DOI=10.1074/jbc.272.42.26727;
RA Kelm R.J. Jr., Elder P.K., Strauch A.R., Getz M.J.;
RT "Sequence of cDNAs encoding components of vascular actin single-stranded
RT DNA-binding factor 2 establish identity to Puralpha and Purbeta.";
RL J. Biol. Chem. 272:26727-26733(1997).
RN [3]
RP PROTEIN SEQUENCE OF 176-198 AND 204-228, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP SUBUNIT.
RX PubMed=10318844; DOI=10.1074/jbc.274.20.14238;
RA Kelm R.J. Jr., Cogan J.G., Elder P.K., Strauch A.R., Getz M.J.;
RT "Molecular interactions between single-stranded DNA-binding proteins
RT associated with an essential MCAT element in the mouse smooth muscle alpha-
RT actin promoter.";
RL J. Biol. Chem. 274:14238-14245(1999).
RN [5]
RP INTERACTION WITH FMR1.
RX PubMed=12147688; DOI=10.1074/jbc.m203608200;
RA Ohashi S., Koike K., Omori A., Ichinose S., Ohara S., Kobayashi S.,
RA Sato T.A., Anzai K.;
RT "Identification of mRNA/protein (mRNP) complexes containing Puralpha,
RT mStaufen, fragile X protein, and myosin Va and their association with rough
RT endoplasmic reticulum equipped with a kinesin motor.";
RL J. Biol. Chem. 277:37804-37810(2002).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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).
CC -!- FUNCTION: This is a probable transcription activator that specifically
CC binds the purine-rich single strand of the PUR element located upstream
CC of the c-Myc gene. May play a role in the initiation of DNA replication
CC and in recombination.
CC -!- SUBUNIT: Homodimer, heterodimer with PURB and heterotrimer with PURB
CC and YBX1/Y-box protein 1 (PubMed:10318844). Interacts with FMR1; this
CC interaction occurs in association with polyribosome (PubMed:12147688).
CC {ECO:0000269|PubMed:10318844, ECO:0000269|PubMed:12147688}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the PUR DNA-binding protein family.
CC {ECO:0000305}.
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DR EMBL; U02098; AAA64630.1; -; mRNA.
DR EMBL; AF017631; AAB71860.1; -; mRNA.
DR CCDS; CCDS29151.1; -.
DR RefSeq; NP_033015.1; NM_008989.3.
DR RefSeq; XP_006525787.1; XM_006525724.3.
DR RefSeq; XP_011245162.1; XM_011246860.2.
DR AlphaFoldDB; P42669; -.
DR SMR; P42669; -.
DR BioGRID; 202515; 33.
DR IntAct; P42669; 12.
DR STRING; 10090.ENSMUSP00000059404; -.
DR iPTMnet; P42669; -.
DR PhosphoSitePlus; P42669; -.
DR SwissPalm; P42669; -.
DR UCD-2DPAGE; P42669; -.
DR EPD; P42669; -.
DR jPOST; P42669; -.
DR MaxQB; P42669; -.
DR PaxDb; P42669; -.
DR PeptideAtlas; P42669; -.
DR PRIDE; P42669; -.
DR ProteomicsDB; 301890; -.
DR Antibodypedia; 26834; 277 antibodies from 28 providers.
DR DNASU; 19290; -.
DR Ensembl; ENSMUST00000051301; ENSMUSP00000059404; ENSMUSG00000043991.
DR GeneID; 19290; -.
DR KEGG; mmu:19290; -.
DR UCSC; uc008enh.2; mouse.
DR CTD; 5813; -.
DR MGI; MGI:103079; Pura.
DR VEuPathDB; HostDB:ENSMUSG00000043991; -.
DR eggNOG; KOG3074; Eukaryota.
DR GeneTree; ENSGT00950000183162; -.
DR HOGENOM; CLU_057873_1_1_1; -.
DR InParanoid; P42669; -.
DR OMA; WAKFGST; -.
DR OrthoDB; 1248813at2759; -.
DR PhylomeDB; P42669; -.
DR TreeFam; TF313701; -.
DR BioGRID-ORCS; 19290; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Pura; mouse.
DR PRO; PR:P42669; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P42669; protein.
DR Bgee; ENSMUSG00000043991; Expressed in ventral tegmental area and 251 other tissues.
DR Genevisible; P42669; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; ISO:MGI.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IDA:HGNC-UCL.
DR GO; GO:0032422; F:purine-rich negative regulatory element binding; IDA:HGNC-UCL.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; IDA:MGI.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0098963; P:dendritic transport of messenger ribonucleoprotein complex; IDA:SynGO.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISO:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0046651; P:lymphocyte proliferation; IMP:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:HGNC-UCL.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR006628; PUR-bd_fam.
DR InterPro; IPR030500; PURalpha.
DR PANTHER; PTHR12611; PTHR12611; 1.
DR PANTHER; PTHR12611:SF2; PTHR12611:SF2; 1.
DR Pfam; PF04845; PurA; 1.
DR SMART; SM00712; PUR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CHAIN 2..321
FT /note="Transcriptional activator protein Pur-alpha"
FT /id="PRO_0000097108"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00577"
SQ SEQUENCE 321 AA; 34884 MW; 0379DBD96D47DCEA CRC64;
MADRDSGSEQ GGAALGSGGS LGHPGSGSGS GGGGGGGGGG GGSGGGGGAP GGLQHETQEL
ASKRVDIQNK RFYLDVKQNA KGRFLKIAEV GAGGNKSRLT LSMSVAVEFR DYLGDFIEHY
AQLGPSQPPD LAQAQDEPRR ALKSEFLVRE NRKYYMDLKE NQRGRFLRIR QTVNRGPGLG
STQGQTIALP AQGLIEFRDA LAKLIDDYGV EEEPAELPEG TSLTVDNKRF FFDVGSNKYG
VFMRVSEVKP TYRNSITVPY KVWAKFGHTF CKYSEEMKKI QEKQREKRAA CEQLHQQQQQ
QQEETTAATL LLQGEEEGEE D
