MYF6_MOUSE
ID MYF6_MOUSE Reviewed; 242 AA.
AC P15375;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Myogenic factor 6;
DE Short=Myf-6;
DE AltName: Full=Herculin;
DE AltName: Full=Muscle-specific regulatory factor 4;
GN Name=Myf6; Synonyms=Mrf4, Myf-6;
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 [GENOMIC DNA].
RC STRAIN=BALB/c Charon 4A; TISSUE=Spleen;
RX PubMed=2300571; DOI=10.1073/pnas.87.3.1089;
RA Miner J.H., Wold B.;
RT "Herculin, a fourth member of the MyoD family of myogenic regulatory
RT genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1089-1093(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Skeletal muscle;
RX PubMed=2045411; DOI=10.1083/jcb.113.6.1255;
RA Bober E., Lyons G.L., Braun T., Cossu G., Buckingham M., Arnold H.-H.;
RT "The muscle regulatory gene, Myf-6, has a biphasic pattern of expression
RT during early mouse development.";
RL J. Cell Biol. 113:1255-1265(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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).
CC -!- FUNCTION: Involved in muscle differentiation (myogenic factor). Induces
CC fibroblasts to differentiate into myoblasts. Probable sequence specific
CC DNA-binding protein.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Interacts with CSRP3. {ECO:0000250|UniProtKB:P19335}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Skeletal muscle.
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DR EMBL; M30499; AAA37802.1; -; Genomic_DNA.
DR EMBL; X59060; CAA41785.1; -; mRNA.
DR EMBL; AK029370; BAC26423.1; -; mRNA.
DR CCDS; CCDS24162.1; -.
DR PIR; A34872; A34872.
DR RefSeq; NP_032683.1; NM_008657.2.
DR AlphaFoldDB; P15375; -.
DR SMR; P15375; -.
DR IntAct; P15375; 1.
DR MINT; P15375; -.
DR STRING; 10090.ENSMUSP00000047529; -.
DR iPTMnet; P15375; -.
DR PhosphoSitePlus; P15375; -.
DR PaxDb; P15375; -.
DR PRIDE; P15375; -.
DR ProteomicsDB; 287569; -.
DR Antibodypedia; 17294; 258 antibodies from 32 providers.
DR DNASU; 17878; -.
DR Ensembl; ENSMUST00000044210; ENSMUSP00000047529; ENSMUSG00000035923.
DR GeneID; 17878; -.
DR KEGG; mmu:17878; -.
DR UCSC; uc007gza.1; mouse.
DR CTD; 4618; -.
DR MGI; MGI:97253; Myf6.
DR VEuPathDB; HostDB:ENSMUSG00000035923; -.
DR eggNOG; KOG3960; Eukaryota.
DR GeneTree; ENSGT00950000182959; -.
DR HOGENOM; CLU_100258_0_0_1; -.
DR InParanoid; P15375; -.
DR OMA; SPCQDQI; -.
DR OrthoDB; 1471470at2759; -.
DR PhylomeDB; P15375; -.
DR TreeFam; TF316344; -.
DR Reactome; R-MMU-525793; Myogenesis.
DR BioGRID-ORCS; 17878; 5 hits in 72 CRISPR screens.
DR PRO; PR:P15375; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P15375; protein.
DR Bgee; ENSMUSG00000035923; Expressed in hindlimb stylopod muscle and 85 other tissues.
DR ExpressionAtlas; P15375; baseline and differential.
DR Genevisible; P15375; MM.
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:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0060415; P:muscle tissue morphogenesis; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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:0045893; P:positive regulation of transcription, DNA-templated; 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:0043403; P:skeletal muscle tissue regeneration; ISO: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; IPR002546; MyoD_N.
DR InterPro; IPR039704; Myogenic_factor.
DR PANTHER; PTHR11534; PTHR11534; 1.
DR Pfam; PF01586; Basic; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00520; BASIC; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; DNA-binding; Myogenesis; Nucleus;
KW Reference proteome.
FT CHAIN 1..242
FT /note="Myogenic factor 6"
FT /id="PRO_0000127352"
FT DOMAIN 93..144
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 31..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 242 AA; 26987 MW; DF5FF9A3FA5BBFD5 CRC64;
MMMDLFETGS YFFYLDGENV TLQPLEVAEG SPLYPGSDGT LSPCQDQMPQ EAGSDSSGEE
HVLAPPGLQP PHCPGQCLIW ACKTCKRKSA PTDRRKAATL RERRRLKKIN EAFEALKRRT
VANPNQRLPK VEILRSAISY IERLQDLLHR LDQQEKMQEL GVDPYSYKPK QEILEGADFL
RTCSPQWPSV SDHSRGLVIT AKEGGANVDA SASSSLQRLS SIVDSISSEE RKLPSVEEVV
EK
