CBFA_DICDI
ID CBFA_DICDI Reviewed; 1000 AA.
AC O97101; Q54WK2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=C-module-binding factor A {ECO:0000303|PubMed:10491202, ECO:0000312|EMBL:AAD17489.2};
GN Name=cbfA {ECO:0000303|PubMed:10491202, ECO:0000312|EMBL:AAD17489.2};
GN Synonyms=cbf {ECO:0000312|dictyBase:DDB_G0279409},
GN cmbF {ECO:0000303|PubMed:8898890};
GN ORFNames=DDB_G0279409 {ECO:0000312|dictyBase:DDB_G0279409};
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689 {ECO:0000312|EMBL:AAD17489.2};
RN [1] {ECO:0000312|EMBL:AAD17489.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 4-21; 32-50; 88-103;
RP 119-133; 205-235; 293-301 AND 968-975, FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-812.
RC STRAIN=AX2 {ECO:0000312|EMBL:AAD17489.2};
RX PubMed=10491202; DOI=10.1046/j.1432-1327.1999.00768.x;
RA Horn J., Dietz-Schmidt A., Zundorf I., Garin J., Dingermann T.,
RA Winckler T.;
RT "A Dictyostelium protein binds to distinct oligo(dA) x oligo(dT) DNA
RT sequences in the C-module of the retrotransposable element DRE.";
RL Eur. J. Biochem. 265:441-448(1999).
RN [2] {ECO:0000312|EMBL:EAL67643.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL67643.1};
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 [3]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=8898890; DOI=10.1111/j.1432-1033.1996.0070t.x;
RA Geier A., Horn J., Dingermann T., Winckler T.;
RT "A nuclear protein factor binds specifically to the 3'-regulatory module of
RT the long-interspersed-nuclear-element-like Dictyostelium repetitive
RT element.";
RL Eur. J. Biochem. 241:70-76(1996).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11162086; DOI=10.1006/jmbi.2000.4341;
RA Winckler T., Trautwein C., Tschepke C., Neuhaeuser C., Zuendorf I.,
RA Beck P., Vogel G., Dingermann T.;
RT "Gene function analysis by amber stop codon suppression: CMBF is a nuclear
RT protein that supports growth and development of Dictyostelium amoebae.";
RL J. Mol. Biol. 305:703-714(2001).
RN [5]
RP FUNCTION.
RX PubMed=15470262; DOI=10.1128/ec.3.5.1349-1358.2004;
RA Winckler T., Iranfar N., Beck P., Jennes I., Siol O., Baik U., Loomis W.F.,
RA Dingermann T.;
RT "CbfA, the C-module DNA-binding factor, plays an essential role in the
RT initiation of Dictyostelium discoideum development.";
RL Eukaryot. Cell 3:1349-1358(2004).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16607013; DOI=10.1128/ec.5.4.658-664.2006;
RA Siol O., Dingermann T., Winckler T.;
RT "The C-module DNA-binding factor mediates expression of the dictyostelium
RT aggregation-specific adenylyl cyclase ACA.";
RL Eukaryot. Cell 5:658-664(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 1-MET--ASP-723;
RP LYS-799; ARG-800; PRO-801; ARG-812 AND 999-ILE-ILE-1000.
RX PubMed=19343174; DOI=10.1371/journal.pone.0005012;
RA Lucas J., Bilzer A., Moll L., Zuendorf I., Dingermann T., Eichinger L.,
RA Siol O., Winckler T.;
RT "The carboxy-terminal domain of Dictyostelium C-module-binding factor is an
RT independent gene regulatory entity.";
RL PLoS ONE 4:E5012-E5012(2009).
RN [8]
RP FUNCTION, AND DOMAIN.
RX PubMed=21076008; DOI=10.1128/ec.00205-10;
RA Bilzer A., Doelz H., Reinhardt A., Schmith A., Siol O., Winckler T.;
RT "The C-module-binding factor supports amplification of TRE5-A
RT retrotransposons in the Dictyostelium discoideum genome.";
RL Eukaryot. Cell 10:81-86(2011).
RN [9]
RP FUNCTION, AND DOMAIN.
RX PubMed=23355006; DOI=10.1128/ec.00329-12;
RA Schmith A., Groth M., Ratka J., Gatz S., Spaller T., Siol O., Gloeckner G.,
RA Winckler T.;
RT "Conserved gene regulatory function of the carboxy-terminal domain of
RT dictyostelid C-module-binding factor.";
RL Eukaryot. Cell 12:460-468(2013).
RN [10]
RP FUNCTION, AND DOMAIN.
RX PubMed=26339297; DOI=10.1186/s13100-015-0045-5;
RA Schmith A., Spaller T., Gaube F., Fransson A., Boesler B., Ojha S.,
RA Nellen W., Hammann C., Soederbom F., Winckler T.;
RT "A host factor supports retrotransposition of the TRE5-A population in
RT Dictyostelium cells by suppressing an Argonaute protein.";
RL Mob. DNA 6:14-14(2015).
CC -!- FUNCTION: Transcriptional regulator involved in phagocytosis and
CC pinocytosis. Both activates and represses transcription. Regulates
CC expression of acaA, carA, pkaC, csaA, cotB and lagC (PubMed:11162086,
CC PubMed:15470262, PubMed:16607013, PubMed:19343174, PubMed:23355006,
CC PubMed:26339297). Promotes amplification of the tRNA gene-associated
CC retrotransposon TRE5-A, a mobile genetic element formerly called as
CC Dictyostelium repetitive element (DRE). Suppresses agnC and agnE
CC encoding argonaute proteins which are part of a RNA interference
CC pathway controlling TRE5-A amplification. Required for amplification of
CC both sense and antisense RNA transcripts, but does not activate their
CC promoters found in A-module and C-module of the TRE5-A, respectively
CC (PubMed:21076008, PubMed:26339297). Nevertheless, binds to distinct DNA
CC sequences containing A and T stretches within the C-module in vitro
CC (PubMed:10491202, PubMed:8898890, PubMed:11162086).
CC {ECO:0000269|PubMed:10491202, ECO:0000269|PubMed:11162086,
CC ECO:0000269|PubMed:15470262, ECO:0000269|PubMed:16607013,
CC ECO:0000269|PubMed:19343174, ECO:0000269|PubMed:21076008,
CC ECO:0000269|PubMed:23355006, ECO:0000269|PubMed:26339297,
CC ECO:0000269|PubMed:8898890}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8898890}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10491202,
CC ECO:0000269|PubMed:11162086, ECO:0000269|PubMed:16607013,
CC ECO:0000269|PubMed:19343174, ECO:0000269|PubMed:8898890}.
CC -!- DOMAIN: The C-terminal domain (724-998) alone is able to regulate gene
CC expression (PubMed:19343174, PubMed:23355006, PubMed:26339297). The C-
CC terminal domain (724-998) is required and sufficient to maintain high
CC steady-state levels of both sense and antisense RNA transcripts of the
CC tRNA gene-associated retrotransposon TRE5-A (PubMed:21076008).
CC {ECO:0000269|PubMed:19343174, ECO:0000269|PubMed:21076008,
CC ECO:0000269|PubMed:23355006, ECO:0000269|PubMed:26339297}.
CC -!- DOMAIN: A.T hook involved in DNA-binding is important for the gene
CC regulatory function in vivo. {ECO:0000269|PubMed:10491202,
CC ECO:0000269|PubMed:19343174}.
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DR EMBL; AF052006; AAD17489.2; -; Genomic_DNA.
DR EMBL; AAFI01000060; EAL67643.1; -; Genomic_DNA.
DR RefSeq; XP_641715.1; XM_636623.1.
DR AlphaFoldDB; O97101; -.
DR STRING; 44689.DDB0216196; -.
DR PaxDb; O97101; -.
DR GeneID; 8622125; -.
DR KEGG; ddi:DDB_G0279409; -.
DR dictyBase; DDB_G0279409; cbfA.
DR eggNOG; ENOG502RSTP; Eukaryota.
DR HOGENOM; CLU_299856_0_0_1; -.
DR InParanoid; O97101; -.
DR OMA; YCNGETI; -.
DR PhylomeDB; O97101; -.
DR PRO; PR:O97101; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045905; P:positive regulation of translational termination; IBA:GO_Central.
DR GO; GO:0010527; P:positive regulation of transposition, RNA-mediated; IMP:UniProtKB.
DR GO; GO:0018126; P:protein hydroxylation; IBA:GO_Central.
DR GO; GO:0032196; P:transposition; IEA:UniProtKB-KW.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR018866; Znf-4CXXC_R1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF10497; zf-4CXXC_R1; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; Direct protein sequencing; DNA-binding;
KW Endocytosis; Metal-binding; Nucleus; Phagocytosis; Transcription;
KW Transcription regulation; Transposition; Zinc; Zinc-finger.
FT CHAIN 1..1000
FT /note="C-module-binding factor A"
FT /id="PRO_0000445586"
FT DOMAIN 113..280
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 489..544
FT /note="PHD-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 492..542
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT DNA_BIND 810..818
FT /note="A.T hook"
FT /evidence="ECO:0000305|PubMed:19343174"
FT REGION 561..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1..723
FT /note="Missing: Present in the cytoplasm but also
FT accumulates in the nucleus, and a decreased ability to
FT regulate gene expression; when associated with N-799; G-800
FT and 999-I-I-1000. Accummulates in the nucleus, and a full
FT ability to regulate gene expression; when associated with
FT K-801 and 999-I-I-1000. Accummulates in the nucleus, but a
FT decreased ability to regulate gene expression; when
FT associated with K-801; A-812 and 999-I-I-1000. A
FT significantly high amount present in the cytoplasm in
FT addition to nucleus, and a decreased ability to regulate
FT gene expression; when associated with A-812 and 999-I-I-
FT 1000."
FT /evidence="ECO:0000269|PubMed:19343174"
FT MUTAGEN 799
FT /note="K->N: Present in the cytoplasm but also accumulates
FT in the nucleus, and a decreased ability to regulate gene
FT expression; when associated with 1-M--D-723; G-800 and 999-
FT I-I-1000."
FT /evidence="ECO:0000269|PubMed:19343174"
FT MUTAGEN 800
FT /note="R->G: Present in the cytoplasm but also accumulates
FT in the nucleus, and a decreased ability to regulate gene
FT expression; when associated with 1-M--D-723; N-799 and 999-
FT I-I-1000."
FT /evidence="ECO:0000269|PubMed:19343174"
FT MUTAGEN 801
FT /note="P->K: Accummulates in the nucleus, and a full
FT ability to regulate gene expression; when associated with
FT 1-M--D-723 and 999-I-I-1000. Accummulates in the nucleus,
FT but a decreased ability to regulate gene expression; when
FT associated with 1-M--D-723; A-812 and 999-I-I-1000."
FT /evidence="ECO:0000269|PubMed:19343174"
FT MUTAGEN 812
FT /note="R->A: Loss of the interaction with promoter of the
FT C-module of the tRNA gene-associated retrotransposon TRE5-
FT A. Accummulates in the nucleus, but a decreased ability to
FT regulate gene expression; when associated with 1-M--D-723;
FT K-801 and 999-I-I-1000. A significantly high amount present
FT in the cytoplasm in addition to nucleus, and a decreased
FT ability to regulate gene expression; when associated with
FT 1-M--D-723 and 999-I-I-1000."
FT /evidence="ECO:0000269|PubMed:10491202,
FT ECO:0000269|PubMed:19343174"
FT MUTAGEN 999..1000
FT /note="Missing: Present in the cytoplasm but also
FT accumulates in the nucleus, and a decreased ability to
FT regulate gene expression; when associated with 1-M--D-723;
FT N-799 and G-800. Accummulates in the nucleus, and a full
FT ability to regulate gene expression; when associated with
FT 1-M--D-723 and K-801. Accummulates in the nucleus, but a
FT decreased ability to regulate gene expression; when
FT associated with 1-M--D-723; K-801 and A-812. A
FT significantly high amount present in the cytoplasm in
FT addition to nucleus, and a decreased ability to regulate
FT gene expression; when associated with 1-M--D-723 and A-
FT 812."
FT /evidence="ECO:0000269|PubMed:19343174"
SQ SEQUENCE 1000 AA; 114270 MW; 33CFC020E951294A CRC64;
MEELIKAPNS NFIIMSNQPY QTTSPEIVED YIIKRGQPFV LTGTTQGWSR SNMFTLDFLS
ERYSEMELIN SPRNNETHTD LQGWRMKDFI SYLQVSPEER NPKHLYGKDI ACPREWQEYL
SHKLQPQYSY KSRFDLVSHL PDYLQPETLL VYIGSNGTYT PGHIDMCGSL SQNLMVSSDQ
DAFAWWFIVP TEYKDEALKF WGDKGGDVYN ESRFIRPIDL LGAPFPIYVF KQRPGDFIFV
PPDSVHQVVN CGPGISTKVA WNSISLKSLP ISYFSSLPHT RRMAKPELFR IKAIAYYTLR
KIMGDVENTN FNTIDVNDVI DIIAPLLEIF HNILQTESIL IPKPNYPYCN GETIPFLQPF
KYFNGDRIQD RRCDHCNSDI FNRCYHCETC KTDDGQGKDF CFDCVSSGIG CEFHFKVMVL
KEFISHSKLK KELSSFYEIY KNLLAHSGRR PKEVDDIITK STDRVSDECG FLTTATVAYH
VVFYSSQKKI KCHRCEKRFK KFSIIFCTNC NARFCEQCVV NTFGQNFQVL MKRNEWECFC
CKGLCDCSNC TSNSNSSNHP RILNNNQQLG LPYNNNNNSN NNNNNNINNN NNNNNNNINN
NNNNMNNNNS INNNNNNNNN NNINNNNINN NNHHNNNGNN NLNSSYSSLN ALSSLSQQQS
YGSYDNYNNN NNNNNYNNNN NNNGHIQILK SGRQYDDEQS SSSGSGSSNS TPTKPRPRNG
GDDGLMSHFS GNNNNNNNHH NNNNNNNNNH HMMSHHHHNN NNNNNNNNNP TTSSLSSLST
SLSSSSTSTQ KPMDVHSKKR PIVLDNDKPK GRPPKNLKEW TSTHKFIISL IELFRSSNNA
ILGKPNPHYK PIENLPPLVQ LYLSQRKAFG GVLWAKTNSC PLLPCIWVKD LSVIPPNTKL
LPSLIQGKKI VVLFFGDQDQ EEYVGIVGKK SIFSFDEVNQ TLLLKCGEVP LAQLEDLFNT
TEPEIAMKKD IAAFNYKNQI EEKEEGLYVK QELYNNKKII
