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   24-JAN-2024, entry version 178.
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; 10090-ENSMUSP00000047529; -.
DR   ProteomicsDB; 287569; -.
DR   Antibodypedia; 17294; 288 antibodies from 32 providers.
DR   DNASU; 17878; -.
DR   Ensembl; ENSMUST00000044210.5; ENSMUSP00000047529.4; ENSMUSG00000035923.5.
DR   GeneID; 17878; -.
DR   KEGG; mmu:17878; -.
DR   UCSC; uc007gza.1; mouse.
DR   AGR; MGI:97253; -.
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; 5392786at2759; -.
DR   PhylomeDB; P15375; -.
DR   TreeFam; TF316344; -.
DR   Reactome; R-MMU-525793; Myogenesis.
DR   BioGRID-ORCS; 17878; 5 hits in 77 CRISPR screens.
DR   PRO; PR:P15375; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P15375; Protein.
DR   Bgee; ENSMUSG00000035923; Expressed in hindlimb stylopod muscle and 87 other cell types or tissues.
DR   ExpressionAtlas; P15375; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0072686; C:mitotic spindle; ISO:MGI.
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: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 DNA-templated transcription; IMP:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; 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: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   CDD; cd18934; bHLH_TS_MRF4_Myf6; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 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; MYOGENIC FACTOR; 1.
DR   PANTHER; PTHR11534:SF4; MYOGENIC FACTOR 6; 1.
DR   Pfam; PF01586; Basic; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00520; BASIC; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   PROSITE; PS50888; BHLH; 1.
DR   Genevisible; P15375; MM.
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
//