ID A0A452FA55_CAPHI Unreviewed; 741 AA.
AC A0A452FA55;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=BTB domain and CNC homolog 1 {ECO:0000313|Ensembl:ENSCHIP00000021144.1};
GN Name=BACH1 {ECO:0000313|Ensembl:ENSCHIP00000021144.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000021144.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000021144.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000021144.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; LWLT01000001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017904623.1; XM_018049134.1.
DR RefSeq; XP_017904664.1; XM_018049175.1.
DR AlphaFoldDB; A0A452FA55; -.
DR STRING; 9925.ENSCHIP00000021144; -.
DR Ensembl; ENSCHIT00000028985.1; ENSCHIP00000021144.1; ENSCHIG00000019566.1.
DR GeneID; 102171277; -.
DR KEGG; chx:102171277; -.
DR CTD; 571; -.
DR GeneTree; ENSGT00940000158923; -.
DR OrthoDB; 382726at2759; -.
DR Proteomes; UP000291000; Chromosome 1.
DR Bgee; ENSCHIG00000019566; Expressed in spleen and 16 other cell types or tissues.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0098531; F:ligand-activated transcription factor activity; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR CDD; cd14719; bZIP_BACH; 1.
DR Gene3D; 1.10.880.10; Transcription factor, Skn-1-like, DNA-binding domain; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR043321; bZIP_BACH.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR46105; AGAP004733-PA; 1.
DR PANTHER; PTHR46105:SF1; TRANSCRIPTION REGULATOR PROTEIN BACH1; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR SMART; SM00338; BRLZ; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 34..100
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT DOMAIN 563..621
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 286..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 576..610
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 286..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 81353 MW; 393947625A383F39 CRC64;
MWLGENAVFA YESSVHGAHV LRCLDEQRRK DELCDVTVLV EGRPFRAHRA VLAACSAYFH
ARLAGAAGAE PRITLPGEVT VKGFEPLIQF AYTAKLILSK DNVDEVYKCV EFLGVPDIEE
SCFQFLKYKF LDSTADQQEC PRKKCFSSPC QKPDFKFSLL DQKDLEIDEV EEFLDNKNVQ
TPHCKLRRYQ GSAKATPPLQ DSASQTCESM CLEKDAPLAL PSLCPKYRKF QKAFGTDRVR
TVESSVKDIQ AASVQPHEPS ESECLGGIQD CADLQAVLKC EERKSVMEHE EAKKKDPASQ
GSSGKTEATP CPPSSADPHG LYSLSLLHTY DQYGDLNFAG MQNTTVLTEK PSSGSSVREE
KAFGESPDVK SDSGPRKESG LAASDLSSVE REVAEHLAKG FWSDICSADS PCQMQLSPAV
AKDGPEQNYP QKRSECPWLG IRISESPEPG QRTFTTLSSV NCPFISTLSP EGCSSSLEIG
TDDYVSEPQQ EPCPYACVIS LGDDSETDTE GDSEPCSARE QECEVKLPFN AQRIISLSRN
DFQSLLKMHK LTPEQLDCIH DIRRRSKNRI AAQRCRKRKL DCIQNLESEI EKLQNEKESL
LKERDHILST LGETKQNLTG LCQQVCKEAA LSQEQIQILA KYSASDCPLS LLISEKGKSA
PDGELALPSI LSLSESPAAG LPAGEPSPCY PSTKGGEAGG VRGQESQTAA STLSEPREPC
RQSGGISDFC QQMTDKCTTD E
//
