TEF_RAT
ID TEF_RAT Reviewed; 301 AA.
AC P41224; Q3T1I8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Thyrotroph embryonic factor;
GN Name=Tef;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-301, INTERACTION WITH DBP, AND
RP MUTAGENESIS.
RC TISSUE=Pituitary;
RX PubMed=1916262; DOI=10.1101/gad.5.10.1739;
RA Drolet D.W., Scully K.M., Simmons D.M., Wegner M., Chu K., Swanson L.W.,
RA Rosenfeld M.G.;
RT "TEF, a transcription factor expressed specifically in the anterior
RT pituitary during embryogenesis, defines a new class of leucine zipper
RT proteins.";
RL Genes Dev. 5:1739-1753(1991).
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'.
CC -!- SUBUNIT: Binds DNA as a homodimer or a heterodimer. Can form a
CC heterodimer with DBP.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in the rostral portion of the
CC anterior pituitary during embryogenesis. Found in several tissues in
CC juvenile and adult rats.
CC -!- DEVELOPMENTAL STAGE: Expressed up to embryonic day 14 and specifically
CC in the anterior pituitary during embryogenesis.
CC -!- INDUCTION: Accumulates according to a robust circadian rhythm.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. PAR subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB20032.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC101895; AAI01896.1; -; mRNA.
DR EMBL; S58745; AAB20032.1; ALT_INIT; mRNA.
DR PIR; A40579; A40579.
DR RefSeq; NP_062067.2; NM_019194.2.
DR AlphaFoldDB; P41224; -.
DR SMR; P41224; -.
DR STRING; 10116.ENSRNOP00000026258; -.
DR PaxDb; P41224; -.
DR Ensembl; ENSRNOT00000026258; ENSRNOP00000026258; ENSRNOG00000019383.
DR GeneID; 29362; -.
DR KEGG; rno:29362; -.
DR UCSC; RGD:3841; rat.
DR CTD; 7008; -.
DR RGD; 3841; Tef.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000156578; -.
DR HOGENOM; CLU_051922_2_0_1; -.
DR InParanoid; P41224; -.
DR OrthoDB; 1023460at2759; -.
DR PhylomeDB; P41224; -.
DR TreeFam; TF315869; -.
DR PRO; PR:P41224; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000019383; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; P41224; baseline and differential.
DR Genevisible; P41224; RN.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR040223; PAR_bZIP.
DR InterPro; IPR029832; TEF/VBP.
DR PANTHER; PTHR11988; PTHR11988; 1.
DR PANTHER; PTHR11988:SF24; PTHR11988:SF24; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; Biological rhythms; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..301
FT /note="Thyrotroph embryonic factor"
FT /id="PRO_0000076515"
FT DOMAIN 231..294
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..253
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 254..261
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 42..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10587"
FT MUTAGEN 218
FT /note="K->A: 30-fold decrease in affinity for prolactin
FT recognition element."
FT /evidence="ECO:0000269|PubMed:1916262"
FT MUTAGEN 219
FT /note="K->A: 30-fold decrease in affinity for prolactin
FT recognition element."
FT /evidence="ECO:0000269|PubMed:1916262"
FT MUTAGEN 221
FT /note="K->A: 30-fold decrease in affinity for prolactin
FT recognition element."
FT /evidence="ECO:0000269|PubMed:1916262"
FT MUTAGEN 222
FT /note="K->A: 30-fold decrease in affinity for prolactin
FT recognition element."
FT /evidence="ECO:0000269|PubMed:1916262"
FT MUTAGEN 266
FT /note="L->V: Diminishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:1916262"
FT MUTAGEN 273
FT /note="L->V: Diminishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:1916262"
SQ SEQUENCE 301 AA; 33159 MW; 2EDFB924F6D2D5F3 CRC64;
MSEAGGGKKP PVEPQAGPGP GRAAGERGLS GSFPLVLKKL MENPPRETRL DKEKGKEKLE
EDESAAASTM AVSASLMPPI WDKTIPYDGE SFHLEYMDLD EFLLENGIPA SPTHLAQNLL
LPVAELEGKE SASSSTASPP SSSTAIFQPS ETVSSTESSL EKERETPSPI DPNCVEVDVN
FNPDPADLVL SSVPGGELFN PRKHKFAEED LKPQPMIKKA KKVFVPDEQK DEKYWTRRKK
NNVAAKRSRD ARRLKENQIT IRAAFLEKEN TALRTEVAEL RKEVGKCKTI VSKYETKYGP
L
