ID   TEF_PHOSU               Reviewed;         221 AA.
AC   P97516;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   22-FEB-2023, entry version 84.
DE   RecName: Full=Thyrotroph embryonic factor;
DE   Flags: Fragment;
GN   Name=TEF;
OS   Phodopus sungorus (Striped hairy-footed hamster) (Djungarian hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Phodopus.
OX   NCBI_TaxID=10044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bockmann J.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor that binds to and transactivates the
CC       TSHB promoter. Binds to a minimal DNA-binding sequence 5'-
CC       [TC][AG][AG]TTA[TC][AG]-3' (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as a homodimer or a heterodimer. Can form a
CC       heterodimer with DBP (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- INDUCTION: Accumulates according to a robust circadian rhythm.
CC   -!- SIMILARITY: Belongs to the bZIP family. PAR subfamily. {ECO:0000305}.
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DR   EMBL; Y11149; CAA72036.1; -; mRNA.
DR   AlphaFoldDB; P97516; -.
DR   SMR; P97516; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   CDD; cd14695; bZIP_HLF; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR040223; PAR_bZIP.
DR   PANTHER; PTHR11988:SF24; THYROTROPH EMBRYONIC FACTOR; 1.
DR   PANTHER; PTHR11988; THYROTROPH EMBRYONIC FACTOR RELATED; 1.
DR   Pfam; PF07716; bZIP_2; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
PE   2: Evidence at transcript level;
KW   Activator; Biological rhythms; DNA-binding; Nucleus; Transcription;
KW   Transcription regulation.
FT   CHAIN           <1..>221
FT                   /note="Thyrotroph embryonic factor"
FT                   /id="PRO_0000076514"
FT   DOMAIN          173..221
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          72..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..195
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          196..203
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        72..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         221
SQ   SEQUENCE   221 AA;  24528 MW;  69645BCA042CFA8B CRC64;
     LEEDESAAAS TMAVSASLMP PIWDKTIPYD GESFHLEYMD LDEFLLENGI PASPTHLAQN
     LLLPVAELEG KESASSSTAS PPSSSTAVFQ PSETVSSTES SLEKERETPS PIDPNCVEVD
     VNFNPDPADL VLSSVPGGEL FNPRKHKFAE EDLKPQPMIK KAKKVFVPDE QKDEKYWTRR
     KKNNVAAKRS RDARRLKENQ ITIRAAFLEK ENTALRTEVA D
//