DIMB_DICDI
ID DIMB_DICDI Reviewed; 602 AA.
AC Q54ER9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Basic-leucine zipper transcription factor B;
GN Name=dimB; ORFNames=DDB_G0291372;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16396914; DOI=10.1242/dev.02190;
RA Zhukovskaya N.V., Fukuzawa M., Yamada Y., Araki T., Williams J.G.;
RT "The Dictyostelium bZIP transcription factor DimB regulates prestalk-
RT specific gene expression.";
RL Development 133:439-448(2006).
RN [3]
RP FUNCTION, INTERACTION WITH DIMA, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=16410410; DOI=10.1242/dev.02240;
RA Huang E., Blagg S.L., Keller T., Katoh M., Shaulsky G., Thompson C.R.L.;
RT "bZIP transcription factor interactions regulate DIF responses in
RT Dictyostelium.";
RL Development 133:449-458(2006).
RN [4]
RP FUNCTION.
RX PubMed=16819464; DOI=10.1038/sj.embor.7400714;
RA Williams J.G.;
RT "Transcriptional regulation of Dictyostelium pattern formation.";
RL EMBO Rep. 7:694-698(2006).
CC -!- FUNCTION: Transcriptional regulator involved in DIF-1 signaling. DIF-1
CC (Differentiation Inducing Factor-1) is a signal molecule involved in
CC the differentiation of pstO (prestalk-O) cells (By similarity). May be
CC a direct activator of ecmA. {ECO:0000250, ECO:0000269|PubMed:16396914,
CC ECO:0000269|PubMed:16410410, ECO:0000269|PubMed:16819464}.
CC -!- SUBUNIT: Binds DNA as a dimer (By similarity). Heterodimerizes with
CC dimA; in vitro. Also able to form homodimer; in vitro. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:16396914, ECO:0000269|PubMed:16410410}. Note=In
CC response to DIF-1, it accumulates rapidly in the nucleus.
CC -!- DEVELOPMENTAL STAGE: Developmentally regulated with levels peaking at
CC culmination. {ECO:0000269|PubMed:16396914,
CC ECO:0000269|PubMed:16410410}.
CC -!- DISRUPTION PHENOTYPE: Following starvation, development proceeds
CC normally only until the finger stage, when extremely long and thin
CC fingers/slugs are produced. DimA and dimB double mutant has the same
CC phenotype. {ECO:0000269|PubMed:16396914, ECO:0000269|PubMed:16410410}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AAFI02000177; EAL61670.1; -; Genomic_DNA.
DR RefSeq; XP_635171.1; XM_630079.1.
DR AlphaFoldDB; Q54ER9; -.
DR STRING; 44689.DDB0220084; -.
DR PaxDb; Q54ER9; -.
DR EnsemblProtists; EAL61670; EAL61670; DDB_G0291372.
DR GeneID; 8628117; -.
DR KEGG; ddi:DDB_G0291372; -.
DR dictyBase; DDB_G0291372; dimB.
DR eggNOG; ENOG502REN0; Eukaryota.
DR HOGENOM; CLU_453776_0_0_1; -.
DR InParanoid; Q54ER9; -.
DR OMA; YISEAQI; -.
DR PhylomeDB; Q54ER9; -.
DR PRO; PR:Q54ER9; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:dictyBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:dictyBase.
DR GO; GO:0045184; P:establishment of protein localization; IMP:dictyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:dictyBase.
DR GO; GO:0060547; P:negative regulation of necrotic cell death; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:0031287; P:positive regulation of sorocarp stalk cell differentiation; IMP:dictyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1903013; P:response to differentiation-inducing factor 1; HDA:dictyBase.
DR GO; GO:0031153; P:slug development involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IEP:dictyBase.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..602
FT /note="Basic-leucine zipper transcription factor B"
FT /id="PRO_0000384444"
FT DOMAIN 113..176
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..135
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 138..145
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 328..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 58..94
FT /evidence="ECO:0000255"
FT COILED 509..552
FT /evidence="ECO:0000255"
FT COMPBIAS 1..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 68452 MW; 421BB044C02B5D16 CRC64;
MNQFYQSTTG GQQNNNNGNQ FQQYQPQQQQ QFQQYSPSNA NNNNTTTTTT TSTSKKGKNK
DNQSKQQQIQ QQQIQQQQQQ QQQQQQQIQQ QSVDTPSSYN GDGSDDGSDT ERENKKNRNR
VNQNLASRNY RQRKKEYIKE IEEKLAVLAL ENDQLKKENI NLKKGGGVEI MKPDPAFITM
MMEAKQIIIQ LDVAIKKNDE RSLIYLLQLF HLSIEKRHTI VEREVEKMVH PYTQAKLAAM
GYVPSLENPM ISSISGPSSD GWWTMYISEA QITEEQAKAI KQLRSNHWKA DIELRNEREK
LDRSIKEFYL NRVMVFPTNE RLNKSFATNL SLSDGPNPTS PNSSSVTQST LVRPSPGLTL
LNNLNEENNN SNNSSNSSNN NTTTNNNNNN SLTPTPNQNN NISNIAVNGT ISVVNELGFS
PINGNIDISE ILEFTRKLEA LKKNFVKQRT LMEDTHSALS SILTPKQEAM LLVRVHSSTR
YDFANMEMLK NVWGSVIAKD TTSYPQPPTF SQQTQQLQQA QLQLQNQTKQ QQQQLQNNNN
NNNNNNNNNN SFNNSNNNNV QNNSSNPSTP GGNNDQQNIY YTSSPSIPSS PYNHHQQQPS
RQ
