HBP1C_WHEAT
ID HBP1C_WHEAT Reviewed; 476 AA.
AC Q41558;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Transcription factor HBP-1b(c1);
DE Flags: Fragment;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DNA-BINDING.
RC STRAIN=cv. Horoshirikomugi;
RX PubMed=8144592; DOI=10.1016/s0021-9258(17)36978-8;
RA Mikami K., Sakamoto A., Iwabuchi M.;
RT "The HBP-1 family of wheat basic/leucine zipper proteins interacts with
RT overlapping cis-acting hexamer motifs of plant histone genes.";
RL J. Biol. Chem. 269:9974-9985(1994).
CC -!- FUNCTION: Transcriptional activator that binds specifically to the DNA
CC sequence 5'-TGACG-3'. Recognizes ocs elements like the as-1 motif of
CC the cauliflower mosaic virus 35S promoter. Binding to the as-1-like cis
CC elements mediate auxin- and salicylic acid-inducible transcription.
CC Binds to the hexamer motif 5'-ACGTCA-3' of histone gene promoters.
CC -!- SUBUNIT: Binds DNA as a dimer.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; D12921; BAA02305.2; -; mRNA.
DR PIR; C54415; C54415.
DR AlphaFoldDB; Q41558; -.
DR STRING; 4565.Traes_3AL_5490CF370.1; -.
DR eggNOG; ENOG502QU32; Eukaryota.
DR OMA; NLNNMQP; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q41558; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR025422; TGA_domain.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF14144; DOG1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
DR PROSITE; PS51806; DOG1; 1.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN <1..476
FT /note="Transcription factor HBP-1b(c1)"
FT /id="PRO_0000076552"
FT DOMAIN 189..252
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT DOMAIN 256..473
FT /note="DOG1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01147"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..211
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 217..231
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COILED 201..242
FT /evidence="ECO:0000255"
FT COMPBIAS 133..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 476 AA; 51787 MW; DD4668F6A2932D88 CRC64;
ESRRGGGGPA AAAAAAGDPR GPMPGFGAPQ HTIPTNVNVM QPSRVADLGA LAHSAGFRIE
DLANFSTNNL FNLKPNTHAY TSDPLQFGNY GKSISPTDLA TTAAAAAAVT AVDPQALLQQ
KGVQPNLVAL RTHNNDNWGE SSMADTSPRT DTSTDPDIDI DERNQMFEQG QLAAPTASDS
SDKSRDKLDH KSLRRLAQNR EAARKSRLRK KAYIQNLESS RLKLTQLEQE LQRARQQGIF
ISSSGDQSQS ASGNGAVAFD MEYARWLEEH NKHINELRAA ANAHAGDDDL RKIVDSIMSQ
YDEFFRLKGV AAKADVFHVL SGMWKTPAER CFMWLGGFRS SELLKLLAGQ LEPLTEQQLT
GICNLQQSSQ QAEDALSQGM EALQQSLAET LASGSLGPAG SSGNVASYMG QMAMAMGKLG
TLENFLRQAD NLRLQTLQQM QRILTTRQSA RALLAISDYF SRLRALSSLW LARPRE