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Database: UniProt
Entry: L5LKD5_MYODS
LinkDB: L5LKD5_MYODS
Original site: L5LKD5_MYODS 
ID   L5LKD5_MYODS            Unreviewed;       672 AA.
AC   L5LKD5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   25-OCT-2017, entry version 32.
DE   RecName: Full=Myogenic factor {ECO:0000256|RuleBase:RU003428};
GN   ORFNames=MDA_GLEAN10004042 {ECO:0000313|EMBL:ELK26702.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Vespertilionidae; Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26702.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y.,
RA   Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y.,
RA   Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G.,
RA   Wang L.F., Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the
RT   evolution of flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- FUNCTION: Induces fibroblasts to differentiate into myoblasts.
CC       Acts as a transcriptional activator that promotes transcription of
CC       muscle-specific target genes and plays a role in muscle
CC       differentiation. {ECO:0000256|RuleBase:RU003428}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another
CC       bHLH protein. {ECO:0000256|RuleBase:RU003428}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU003428}.
CC   -!- SIMILARITY: Belongs to the potassium channel family.
CC       {ECO:0000256|SAAS:SAAS00692852}.
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DR   EMBL; KB110898; ELK26702.1; -; Genomic_DNA.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0007517; P:muscle organ development; IEA:InterPro.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00083; HLH; 1.
DR   InterPro; IPR002546; Basic.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR   InterPro; IPR005403; K_chnl_volt-dep_Kv3.1.
DR   InterPro; IPR022032; Myf5.
DR   InterPro; IPR011333; SKP1/BTB/POZ.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR028325; VG_K_chnl.
DR   PANTHER; PTHR11537; PTHR11537; 1.
DR   Pfam; PF01586; Basic; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00010; HLH; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF12232; Myf5; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01581; KV31CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01498; SHAWCHANNEL.
DR   SMART; SM00520; BASIC; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000010556};
KW   DNA-binding {ECO:0000256|RuleBase:RU003428};
KW   Ion channel {ECO:0000256|SAAS:SAAS00417203};
KW   Ion transport {ECO:0000256|SAAS:SAAS00417186};
KW   Membrane {ECO:0000256|SAAS:SAAS00788393, ECO:0000256|SAM:Phobius};
KW   Nucleus {ECO:0000256|RuleBase:RU003428};
KW   Potassium {ECO:0000256|SAAS:SAAS00417282};
KW   Potassium channel {ECO:0000256|SAAS:SAAS00417246};
KW   Potassium transport {ECO:0000256|SAAS:SAAS00417240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00793138,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00789957,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00417268};
KW   Voltage-gated channel {ECO:0000256|SAAS:SAAS00091688}.
FT   TRANSMEM    349    370       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    405    427       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    506    527       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    548    565       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    577    606       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      108    159       BHLH. {ECO:0000259|PROSITE:PS50888}.
SQ   SEQUENCE   672 AA;  75398 MW;  34923E7519440972 CRC64;
     MELLSPPLRD VDLTGPDGSL CNFATADDFY DDPCFDSPDL RFFEDLDPRL VHVGAFLKPE
     DSHFPAAVHP APGAREDEHV RAPSGHHQAG RCLLWACKAC KRKTTNADRR KAATMRERRR
     LSKVNEAFET LKRCTSSNPN QRLPKVEILR NAIRYIEGLQ ALLRDQDAAP PGAAAAFYAP
     GPLPSGRGGE HYSGDSDASS PRSNCSDGMM DYSGPTSGAR RRNCYDGSYF SQASSGVFAH
     ILNYYRTGKL HCPADVCGPL YEEELAFWGI DETDVEPCCW MTYRQHRDAE EALDSFGDGP
     GDSGDGEDEL EMTKRLALSD SPDGRPGGFW RRWQPRIWAL FEDPYSSRYA RYVALASLFF
     ILVSITTFCL ETHERFNPIV NKTEIENVRN GTQVRYYREA ETEAFLTYIE GVCVVWFTFE
     FLMRVVFCPN KVEFIKNSLN IIDFVAILPF YLEVGLSGLS SKAAKDVLGF LRVVRFVRIL
     RIFKLTRHFV GLRVLGHTLR ASTNEFLLLI IFLALGVLIF ATMIYYAERI GAQPNDPSAS
     EHTHFKNIPI GFWWAVVTMT TLGYGDMYPQ TWSGMLVGAL CALAGVLTIA MPVPVIVNNF
     GMYYSLAMAK QKLPKKKKKH IPRPPQLGSP NYCKSVVNSP HHSTQSDTCP LAQEEILEIN
     RAGRKPLRGM SI
//
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