JUND_BOVIN
ID JUND_BOVIN Reviewed; 347 AA.
AC A7YY54;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Transcription factor JunD {ECO:0000305};
DE AltName: Full=Transcription factor AP-1 subunit JunD {ECO:0000305};
GN Name=JUND;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor binding AP-1 sites (By similarity).
CC Heterodimerizes with proteins of the FOS family to form an AP-1
CC transcription factor complex, thereby enhancing their DNA binding
CC activity to an AP-1 consensus sequence 3'-TGA[GC]TCA-5' and enhancing
CC their transcriptional activity (By similarity).
CC {ECO:0000250|UniProtKB:P17535}.
CC -!- SUBUNIT: Heterodimer; binds DNA as a heterodimer (By similarity).
CC Component of an AP-1 transcription factor complex composed of JUN-FOS
CC heterodimers (By similarity). As part of the AP-1 transcription factor
CC complex, forms heterodimers with FOS proteins, thereby binding to the
CC AP-1 consensus sequence and stimulating transcription (By similarity).
CC Forms heterodimers with FOSB; thereby binding to the AP-1 consensus
CC sequence (By similarity). Interacts (via MBM motif) with MEN1; this
CC interaction represses transcriptional activation (By similarity).
CC Interacts with MAPK10; this interaction is inhibited in the presence of
CC MEN1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P13346,
CC ECO:0000250|UniProtKB:P17535}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- DOMAIN: Binds DNA via bZIP domain; DNA-binding is under control of
CC cellular redox homeostasis (in vitro) (By similarity). To enable DNA
CC binding, the bZIP domain must undergo a conformational rearrangement
CC which requires the reduction of the interchain disulfide bond between
CC FosB and JunD (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P17535}.
CC -!- PTM: Phosphorylated by MAP kinases MAPK8 and MAPK10; phosphorylation is
CC inhibited in the presence of MEN1. {ECO:0000250|UniProtKB:P17535}.
CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
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DR EMBL; BC151336; AAI51337.1; -; mRNA.
DR RefSeq; NP_001096723.1; NM_001103253.1.
DR AlphaFoldDB; A7YY54; -.
DR SMR; A7YY54; -.
DR iPTMnet; A7YY54; -.
DR PRIDE; A7YY54; -.
DR GeneID; 517192; -.
DR KEGG; bta:517192; -.
DR CTD; 3727; -.
DR InParanoid; A7YY54; -.
DR OrthoDB; 1090460at2759; -.
DR Proteomes; UP000009136; Unplaced.
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 InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR005643; JNK.
DR InterPro; IPR029823; JunD.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR11462:SF7; PTHR11462:SF7; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF03957; Jun; 1.
DR PRINTS; PR00043; LEUZIPPRJUN.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..347
FT /note="Transcription factor JunD"
FT /id="PRO_0000311123"
FT DOMAIN 268..331
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..295
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 296..324
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOTIF 29..41
FT /note="Menin-binding motif (MBM)"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT MOTIF 48..57
FT /note="MAP kinase docking motif; essential for its
FT phosphorylation"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT COMPBIAS 218..233
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT MOD_RES 102
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT DISULFID 285
FT /note="Interchain (with C-172 in FOSB)"
FT /evidence="ECO:0000250|UniProtKB:P17535"
SQ SEQUENCE 347 AA; 35352 MW; AEF47BCE2ABC4B91 CRC64;
METPFYGDEA LSGLGGGGSS SGGGGSFASP GRLFPGAPPT AAPGSMMKKD ALTLSLSEQV
AAALKPAAAP PPGPLRTDGA PGTAPPDGLL ASPELGLLKL ASPELERLII QSNGLVTTTP
TSTQFLYPKV AASEEQEFAE GFVKALEDLH KQNQLSAGAA SAAAAAGGPS GTAAGAAPPS
ELAPAAATPE APVYANLSSY AGGTGSAGGA ATVAFAAEPV PFPPPPPPGT LGPPRLAALK
DEPQTVPDVP SFGESPPLSP IDMDTQERIK AERKRLRNRI AASKCRKRKL ERISRLEEKV
KTLKSQNTEL ASTASLLREQ VAQLKQKVLS HVNSGCQLLP QHQVPAY
