MYF5_MOUSE
ID MYF5_MOUSE Reviewed; 255 AA.
AC P24699; Q543W7;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Myogenic factor 5;
DE Short=Myf-5;
GN Name=Myf5; Synonyms=Myf-5;
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].
RC STRAIN=C3H/HeJ; TISSUE=Skeletal muscle, and Smooth muscle;
RX PubMed=1741288; DOI=10.1093/nar/20.3.539;
RA Buonanno A., Apone L., Morasso M.I., Beers R., Brenner H.R., Eftimie R.;
RT "The MyoD family of myogenic factors is regulated by electrical activity:
RT isolation and characterization of a mouse Myf-5 cDNA.";
RL Nucleic Acids Res. 20:539-544(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP FUNCTION, AND PROMOTER BINDING.
RX PubMed=21798092; DOI=10.1186/2044-5040-1-14;
RA Londhe P., Davie J.K.;
RT "Sequential association of myogenic regulatory factors and E proteins at
RT muscle-specific genes.";
RL Skelet. Muscle 1:14-14(2011).
CC -!- FUNCTION: Acts as a transcriptional activator that promotes
CC transcription of muscle-specific target genes and plays a role in
CC muscle differentiation. Together with MYOG and MYOD1, co-occupies
CC muscle-specific gene promoter core region during myogenesis. Induces
CC fibroblasts to differentiate into myoblasts. Probable sequence specific
CC DNA-binding protein. {ECO:0000269|PubMed:21798092}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X56182; CAA39643.1; -; mRNA.
DR EMBL; AK044894; BAC32132.1; -; mRNA.
DR EMBL; AK083402; BAC38902.1; -; mRNA.
DR CCDS; CCDS24161.1; -.
DR PIR; S22825; S22825.
DR RefSeq; NP_032682.1; NM_008656.5.
DR RefSeq; XP_006513382.1; XM_006513319.2.
DR AlphaFoldDB; P24699; -.
DR SMR; P24699; -.
DR BioGRID; 201641; 2.
DR STRING; 10090.ENSMUSP00000000445; -.
DR iPTMnet; P24699; -.
DR PhosphoSitePlus; P24699; -.
DR PaxDb; P24699; -.
DR PRIDE; P24699; -.
DR Antibodypedia; 17297; 472 antibodies from 37 providers.
DR DNASU; 17877; -.
DR Ensembl; ENSMUST00000000445; ENSMUSP00000000445; ENSMUSG00000000435.
DR GeneID; 17877; -.
DR KEGG; mmu:17877; -.
DR UCSC; uc007gyz.1; mouse.
DR CTD; 4617; -.
DR MGI; MGI:97252; Myf5.
DR VEuPathDB; HostDB:ENSMUSG00000000435; -.
DR eggNOG; KOG3960; Eukaryota.
DR GeneTree; ENSGT00950000182959; -.
DR HOGENOM; CLU_066887_0_0_1; -.
DR InParanoid; P24699; -.
DR OMA; MAECNSP; -.
DR OrthoDB; 1471470at2759; -.
DR PhylomeDB; P24699; -.
DR TreeFam; TF316344; -.
DR Reactome; R-MMU-525793; Myogenesis.
DR BioGRID-ORCS; 17877; 1 hit in 71 CRISPR screens.
DR PRO; PR:P24699; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P24699; protein.
DR Bgee; ENSMUSG00000000435; Expressed in myotome and 85 other tissues.
DR ExpressionAtlas; P24699; baseline and differential.
DR Genevisible; P24699; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; TAS:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0001502; P:cartilage condensation; IMP:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0007517; P:muscle organ development; IMP:MGI.
DR GO; GO:0048644; P:muscle organ morphogenesis; IGI:MGI.
DR GO; GO:0060415; P:muscle tissue morphogenesis; IMP:MGI.
DR GO; GO:0001503; P:ossification; IMP:MGI.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IBA:GO_Central.
DR GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR022032; Myf5.
DR InterPro; IPR002546; MyoD_N.
DR InterPro; IPR039704; Myogenic_factor.
DR PANTHER; PTHR11534; PTHR11534; 1.
DR Pfam; PF01586; Basic; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF12232; Myf5; 1.
DR SMART; SM00520; BASIC; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Developmental protein; Differentiation; DNA-binding; Myogenesis;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..255
FT /note="Myogenic factor 5"
FT /id="PRO_0000127345"
FT DOMAIN 83..134
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 226..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 255 AA; 28229 MW; 0BDCBEDF2ABCAEC9 CRC64;
MDMTDGCQFS PSEYFYEGSC IPSPEDEFGD QFEPRVAAFG AHKAELQGSD DEEHVRAPTG
HHQAGHCLMW ACKACKRKST TMDRRKAATM RERRRLKKVN QAFETLKRCT TTNPNQRLPK
VEILRNAIRY IESLQELLRE QVENYYSLPG QSCSEPTSPT SNCSDGMPEC NSPVWSRKNS
SFDSIYCPDV SNACAADKSS VSSLDCLSSI VDRITSTEPS ELALQDTASL SPATSANSQP
ATPGPSSSRL IYHVL
