MYPOP_MOUSE
ID MYPOP_MOUSE Reviewed; 393 AA.
AC Q8R4U1; Q7TNR1; Q8CFP0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Myb-related transcription factor, partner of profilin;
DE AltName: Full=Myb-related protein p42POP;
DE AltName: Full=Partner of profilin;
GN Name=Mypop; Synonyms=P42pop;
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), FUNCTION, INTERACTION WITH PFN1,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-274 AND
RP LEU-281.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=15615774; DOI=10.1242/jcs.01618;
RA Lederer M., Jockusch B.M., Rothkegel M.;
RT "Profilin regulates the activity of p42POP, a novel Myb-related
RT transcription factor.";
RL J. Cell Sci. 118:331-341(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 126-393 (ISOFORM 1).
RC TISSUE=Eye;
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).
CC -!- FUNCTION: Transcriptional repressor; DNA-binding protein that
CC specifically recognizes the core sequence 5'-YAAC[GT]G-3'. Dimerization
CC with PFN1 reduces its DNA-binding capacity.
CC {ECO:0000269|PubMed:15615774}.
CC -!- SUBUNIT: Interacts with PFN1. Homodimer and heterodimer with PFN1.
CC {ECO:0000269|PubMed:15615774}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15615774}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R4U1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R4U1-2; Sequence=VSP_034858, VSP_034859;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, liver and
CC testis. Moderate expression in heart, lung and skeletal muscle. Low
CC expression in spleen and kidney. {ECO:0000269|PubMed:15615774}.
CC -!- DOMAIN: The proline-rich region is required for PFN1 interaction.
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DR EMBL; AF364868; AAL83995.1; -; mRNA.
DR EMBL; BC042748; AAH42748.1; -; mRNA.
DR EMBL; BC055832; AAH55832.1; -; mRNA.
DR CCDS; CCDS39792.1; -. [Q8R4U1-1]
DR RefSeq; NP_663554.1; NM_145579.3. [Q8R4U1-1]
DR RefSeq; XP_006539882.1; XM_006539819.3. [Q8R4U1-1]
DR AlphaFoldDB; Q8R4U1; -.
DR BioGRID; 231324; 2.
DR STRING; 10090.ENSMUSP00000058718; -.
DR iPTMnet; Q8R4U1; -.
DR PhosphoSitePlus; Q8R4U1; -.
DR MaxQB; Q8R4U1; -.
DR PaxDb; Q8R4U1; -.
DR PeptideAtlas; Q8R4U1; -.
DR PRIDE; Q8R4U1; -.
DR ProteomicsDB; 293607; -. [Q8R4U1-1]
DR ProteomicsDB; 293608; -. [Q8R4U1-2]
DR Antibodypedia; 45635; 22 antibodies from 10 providers.
DR DNASU; 232934; -.
DR Ensembl; ENSMUST00000059331; ENSMUSP00000058718; ENSMUSG00000048481. [Q8R4U1-1]
DR Ensembl; ENSMUST00000131087; ENSMUSP00000117357; ENSMUSG00000048481. [Q8R4U1-1]
DR GeneID; 232934; -.
DR KEGG; mmu:232934; -.
DR UCSC; uc009fka.2; mouse. [Q8R4U1-1]
DR CTD; 339344; -.
DR MGI; MGI:2446472; Mypop.
DR VEuPathDB; HostDB:ENSMUSG00000048481; -.
DR eggNOG; ENOG502RV5V; Eukaryota.
DR GeneTree; ENSGT00450000040421; -.
DR HOGENOM; CLU_046143_2_0_1; -.
DR InParanoid; Q8R4U1; -.
DR OMA; QEGGCPR; -.
DR OrthoDB; 1378970at2759; -.
DR PhylomeDB; Q8R4U1; -.
DR TreeFam; TF338618; -.
DR BioGRID-ORCS; 232934; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Mypop; mouse.
DR PRO; PR:Q8R4U1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R4U1; protein.
DR Bgee; ENSMUSG00000048481; Expressed in perirhinal cortex and 185 other tissues.
DR Genevisible; Q8R4U1; MM.
DR GO; GO:0005634; C:nucleus; IDA: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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:MGI.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR028002; Myb_DNA-bind_5.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF13873; Myb_DNA-bind_5; 1.
DR SMART; SM00717; SANT; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..393
FT /note="Myb-related transcription factor, partner of
FT profilin"
FT /id="PRO_0000344800"
FT DOMAIN 16..88
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 87..90
FT /note="Nuclear localization signal"
FT MOTIF 376..379
FT /note="Nuclear localization signal"
FT MOTIF 384..387
FT /note="Nuclear localization signal"
FT COMPBIAS 140..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..323
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..393
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 171..178
FT /note="DTPAQSKG -> GESQSQFL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034858"
FT VAR_SEQ 179..393
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034859"
FT MUTAGEN 274
FT /note="L->A: Reduction in homodimerization. Abolishes
FT homodimerization; when associated with P-281."
FT /evidence="ECO:0000269|PubMed:15615774"
FT MUTAGEN 274
FT /note="L->P: Reduction in homodimerization. Abolishes
FT homodimerization; when associated with A-281."
FT /evidence="ECO:0000269|PubMed:15615774"
FT MUTAGEN 281
FT /note="L->A: Reduction in homodimerization."
FT /evidence="ECO:0000269|PubMed:15615774"
FT MUTAGEN 281
FT /note="L->P: Reduction in homodimerization."
FT /evidence="ECO:0000269|PubMed:15615774"
SQ SEQUENCE 393 AA; 41890 MW; 70356EBA89BB49C8 CRC64;
MASATAAAAP GEAEETTRLR KPRFSFEENQ ILIREVRAHY PQLYGAQSRR VSVAERRRVW
DSIATKINGI TSWKRTGQEV QKRWNDFKRR TKEKLARVPH STQGAGPAAE DAFSAEEETI
FAILGPGVAG PGAGSGAEES RAAASSQPQA STASTQRYVL SEDRRQDRRA DTPAQSKGGS
SSPESWARPS CNPQEAKERE STSPAAMQPV QLPRLALSPP LPAPPPPPTA LAQVAPSSPS
PTPPRPTSAP EQSLDFLRAQ QETANAIREL AGTLRQGLAK LSEALSALLP LLPGTPADPL
PPPPPPPPPP PPKPVLPPSA PKVELAPEPV SVVAAVVDGA VVAARGVIIS PRSEEGVPKP
LPPAPPLPLH DSPPHKRRKG FPTRKRRGRW KSP
