ID   JUN_CHICK               Reviewed;         314 AA.
AC   P18870;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Transcription factor Jun {ECO:0000305};
DE   AltName: Full=Proto-oncogene c-Jun;
DE   AltName: Full=Transcription factor AP-1 subunit Jun {ECO:0000305};
GN   Name=JUN;
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 [GENOMIC DNA].
RC   TISSUE=Fibroblast;
RX   PubMed=2577867;
RA   Nishimura T., Vogt P.K.;
RT   "The avian cellular homolog of the oncogene jun.";
RL   Oncogene 3:659-663(1988).
RN   [2]
RP   INTERACTION WITH GAHV-2 MEQ.
RX   PubMed=7769661; DOI=10.1128/jvi.69.7.4037-4044.1995;
RA   Qian Z., Brunovskis P., Rauscher F. III, Lee L., Kung H.J.;
RT   "Transactivation activity of Meq, a Marek's disease herpesvirus bZIP
RT   protein persistently expressed in latently infected transformed T cells.";
RL   J. Virol. 69:4037-4044(1995).
CC   -!- FUNCTION: Transcription factor that recognizes and binds to the
CC       enhancer heptamer motif 5'-TGA[CG]TCA-3'. May be involved in activated
CC       KRAS-mediated transcriptional activation of USP28. May bind to the
CC       USP28 promoter. {ECO:0000250|UniProtKB:P05412}.
CC   -!- SUBUNIT: Interacts with FOS to form a dimer. Interacts with Gallid
CC       herpesvirus 2 MEQ protein. {ECO:0000269|PubMed:7769661}.
CC   -!- INTERACTION:
CC       P18870; Q9DGW5: MDV005; Xeno; NbExp=5; IntAct=EBI-445826, EBI-10889526;
CC       P18870; Q77Q71: R-LORF7; Xeno; NbExp=2; IntAct=EBI-445826, EBI-10766689;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA48927.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M57467; AAA48927.1; ALT_INIT; Genomic_DNA.
DR   PIR; I50373; I50373.
DR   RefSeq; NP_001026460.1; NM_001031289.1.
DR   AlphaFoldDB; P18870; -.
DR   SMR; P18870; -.
DR   ELM; P18870; -.
DR   IntAct; P18870; 3.
DR   MINT; P18870; -.
DR   STRING; 9031.ENSGALP00000037247; -.
DR   ChEMBL; CHEMBL1075084; -.
DR   PaxDb; P18870; -.
DR   GeneID; 424673; -.
DR   KEGG; gga:424673; -.
DR   CTD; 3725; -.
DR   VEuPathDB; HostDB:geneid_424673; -.
DR   eggNOG; KOG0837; Eukaryota.
DR   InParanoid; P18870; -.
DR   OrthoDB; 1090460at2759; -.
DR   PhylomeDB; P18870; -.
DR   Reactome; R-GGA-437986; Activated TAK1 mediates Jun kinases (JNK) phosphorylation and activation.
DR   PRO; PR:P18870; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005634; C:nucleus; IDA:AgBase.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0043923; P:positive regulation by host of viral transcription; IMP:AgBase.
DR   GO; GO:0030307; P:positive regulation of cell growth; IMP:AgBase.
DR   GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR015558; C_Jun/v-Jun.
DR   InterPro; IPR005643; JNK.
DR   InterPro; IPR002112; Leuzip_Jun.
DR   InterPro; IPR008917; TF_DNA-bd_sf.
DR   PANTHER; PTHR11462:SF8; PTHR11462:SF8; 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   1: Evidence at protein level;
KW   Activator; DNA-binding; Nucleus; Proto-oncogene; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..314
FT                   /note="Transcription factor Jun"
FT                   /id="PRO_0000076433"
FT   DOMAIN          235..298
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          235..262
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          263..291
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
SQ   SEQUENCE   314 AA;  34358 MW;  B882DBFACEDDE1B1 CRC64;
     MSAKMEPTFY EDALNASFAP PESGGYGYNN AKVLKQSMTL NLSDAASSLK PHLRNKNADI
     LTSPDVGLLK LASPELERLI IQSSNGLITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE
     LHNQNTLPSV TSAAQPVSGG MAPVSSMAGG GSFNTSLHSE PPVYANLSNF NPNALNSAPN
     YNANGMGYAP QHHINPQMPV QHPRLQALKE EPQTVPEMPG ETPPLSPIDM ESQERIKAER
     KRMRNRIAAS KCRKRKLERI ARLEEKVKTL KAQNSELAST ANMLREQVAQ LKQKVMNHVN
     SGCQLMLTQQ LQTF