TCF15_CHICK
ID TCF15_CHICK Reviewed; 183 AA.
AC P79782; O13112;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Transcription factor 15;
DE Short=TCF-15;
DE AltName: Full=Paraxis {ECO:0000303|PubMed:9187085, ECO:0000303|PubMed:9281340};
DE AltName: Full=Protein bHLH-EC2 {ECO:0000250|UniProtKB:Q60756};
GN Name=TCF15; Synonyms=BHLHEC2 {ECO:0000250|UniProtKB:Q60756};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Embryo;
RX PubMed=9187085; DOI=10.1006/dbio.1997.8561;
RA Sosic D., Brand-Saberi B., Schmidt C., Christ B., Olson E.N.;
RT "Regulation of paraxis expression and somite formation by ectoderm- and
RT neural tube-derived signals.";
RL Dev. Biol. 185:229-243(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=9281340; DOI=10.1006/dbio.1997.8663;
RA Barnes G.L., Alexander P.G., Hsu C.W., Mariani B.D., Tuan R.S.;
RT "Cloning and characterization of chicken Paraxis: a regulator of paraxial
RT mesoderm development and somite formation.";
RL Dev. Biol. 189:95-111(1997).
CC -!- FUNCTION: Early transcription factor that plays a key role in
CC somitogenesis, paraxial mesoderm development and regulation of stem
CC cell pluripotency. Essential for the mesenchymal to epithelial
CC transition associated with somite formation. Required for somite
CC morphogenesis, thereby regulating patterning of the axial skeleton and
CC skeletal muscles. Also plays a key role in regulation of stem cell
CC pluripotency. Promotes pluripotency exit of embryonic stem cells (ESCs)
CC by priming ESCs for differentiation. Acts as a key regulator of self-
CC renewal of hematopoietic stem cells (HSCs) by mediating HSCs quiescence
CC and long-term self-renewal. Acts by forming a heterodimer with another
CC helix-loop-helix (bHLH) protein, that binds DNA on E-box motifs (5'-
CC CANNTG-3') and activates transcription of target genes.
CC {ECO:0000250|UniProtKB:Q60756}.
CC -!- SUBUNIT: Heterodimer; efficient DNA binding requires dimerization with
CC another bHLH protein. {ECO:0000250|UniProtKB:Q60756}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q60756,
CC ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- DEVELOPMENTAL STAGE: First detected in a subpopulation of cells lateral
CC to the primitive streak corresponding with the area of prospective
CC segmental plate mesoderm and somites (PubMed:9187085, PubMed:9281340).
CC Later in development, it is expressed throughout the segmental plate
CC and newly formed somites and is restricted to the paraxial mesoderm
CC (PubMed:9187085, PubMed:9281340). After somite formation, its
CC expression decline in the lateral region of the somite (PubMed:9187085,
CC PubMed:9281340). Later it is expressed at highest levels at the cranial
CC and caudal edges of the more mature somites (PubMed:9187085,
CC PubMed:9281340). As the dermomyotome and sclerotome formed, expression
CC disappeared from the ventral regions of the somite, but persisted in
CC the dermomyotome (PubMed:9187085, PubMed:9281340). When the
CC dermomyotome developed further into the dermatome and myotome,
CC expression is detected in both compartments, although more prominently
CC in the dermatome (PubMed:9187085, PubMed:9281340). Expression was also
CC detected in migrating precursors of tongue muscle and in the limb buds
CC (PubMed:9187085, PubMed:9281340). {ECO:0000269|PubMed:9187085,
CC ECO:0000269|PubMed:9281340}.
CC -!- INDUCTION: Surface ectoderm and neural tube are the sources of
CC inductive signals required for gene expression and for somite
CC formation. {ECO:0000269|PubMed:9187085}.
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DR EMBL; U76665; AAC60208.1; -; mRNA.
DR EMBL; U72641; AAB41698.1; -; mRNA.
DR RefSeq; NP_990277.1; NM_204946.2.
DR AlphaFoldDB; P79782; -.
DR SMR; P79782; -.
DR STRING; 9031.ENSGALP00000040766; -.
DR GeneID; 395788; -.
DR KEGG; gga:395788; -.
DR CTD; 6939; -.
DR VEuPathDB; HostDB:geneid_395788; -.
DR eggNOG; KOG4029; Eukaryota.
DR InParanoid; P79782; -.
DR OrthoDB; 1511100at2759; -.
DR PhylomeDB; P79782; -.
DR PRO; PR:P79782; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0032502; P:developmental process; IBA:GO_Central.
DR GO; GO:1902037; P:negative regulation of hematopoietic stem cell differentiation; ISS:UniProtKB.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 2: Evidence at transcript level;
KW Activator; Developmental protein; Differentiation; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..183
FT /note="Transcription factor 15"
FT /id="PRO_0000127463"
FT DOMAIN 61..113
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 24..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 48
FT /note="R -> G (in Ref. 1; AAC60208)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="K -> R (in Ref. 2; AAB41698)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="A -> S (in Ref. 1; AAC60208)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="A -> S (in Ref. 1; AAC60208)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..143
FT /note="GR -> SK (in Ref. 1; AAC60208)"
FT /evidence="ECO:0000305"
FT CONFLICT 149..157
FT /note="CTFCLSNQR -> WTFYFNNHG (in Ref. 2; AAB41698)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="G -> V (in Ref. 2; AAB41698)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..167
FT /note="LGG -> HGD (in Ref. 2; AAB41698)"
FT /evidence="ECO:0000305"
FT CONFLICT 180..181
FT /note="VA -> GN (in Ref. 2; AAB41698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 183 AA; 20195 MW; A2AF94011522401C CRC64;
MAFTMLRPMA ARVLYPDIGM LSEDEENRSE SDTSDQSYGC CEGAEARRKV PRKTGPMVMV
KQRQAANARE RDRTQSVNTA FTALRTLIPT EPVDRKLSKI ETLRLASSYI AHLANVLLLG
EGCEDGQPCF SAIYGAKGDL DGRQPRSICT FCLSNQRKGG GRRDLGGNCL KVRGVTPLRV
ARR
