RBLA_DICDI
ID RBLA_DICDI Reviewed; 1312 AA.
AC Q54FX2; Q53U28;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Retinoblastoma-like protein A;
GN Name=rblA {ECO:0000303|PubMed:16495312};
GN Synonyms=Rb {ECO:0000312|dictyBase:DDB_G0290551};
GN ORFNames=DDB0188949 {ECO:0000312|dictyBase:DDB_G0290551};
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mayanagi T., Amagai A., Maeda Y.;
RT "Identification of a retinoblastoma homologue gene in Dictyostelium
RT cells.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16495312; DOI=10.1242/dev.02287;
RA MacWilliams H., Doquang K., Pedrola R., Dollman G., Grassi D., Peis T.,
RA Tsang A., Ceccarelli A.;
RT "A retinoblastoma ortholog controls stalk/spore preference in
RT Dictyostelium.";
RL Development 133:1287-1297(2006).
RN [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=20300194; DOI=10.1371/journal.pone.0009676;
RA Conte D., MacWilliams H.K., Ceccarelli A.;
RT "BTG interacts with retinoblastoma to control cell fate in Dictyostelium.";
RL PLoS ONE 5:E9676-E9676(2010).
RN [5]
RP FUNCTION.
RX PubMed=22768168; DOI=10.1371/journal.pone.0039914;
RA Strasser K., Bloomfield G., MacWilliams A., Ceccarelli A., MacWilliams H.,
RA Tsang A.;
RT "A retinoblastoma orthologue is a major regulator of S-phase, mitotic, and
RT developmental gene expression in Dictyostelium.";
RL PLoS ONE 7:E39914-E39914(2012).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=24390142; DOI=10.1128/ec.00306-13;
RA Bakthavatsalam D., White M.J., Herlihy S.E., Phillips J.E., Gomer R.H.;
RT "A retinoblastoma orthologue is required for the sensing of a chalone in
RT Dictyostelium discoideum.";
RL Eukaryot. Cell 13:376-382(2014).
CC -!- FUNCTION: Key regulator of entry into cell division. Directly involved
CC in heterochromatin formation by maintaining overall chromatin structure
CC and, in particular, that of constitutive heterochromatin by stabilizing
CC histone methylation. Controls histone H4 'Lys-20' trimethylation.
CC Probably acts as a transcription repressor by recruiting chromatin-
CC modifying enzymes to promoters (By similarity). Plays a dual role,
CC regulating cell-cycle progression and transcriptional events leading to
CC terminal differentiation. In the absence of a G1 phase, functions in
CC late G2 controlling the expression of both S-phase and mitotic genes.
CC Controls stalk/spore preference by suppressing the DIF response in
CC cells destined for the spore pathway. DIF is a chlorinated
CC hydroxyphenone made by cells of spore pathway that promotes stalk
CC differentiation. {ECO:0000250|UniProtKB:Q08999,
CC ECO:0000269|PubMed:16495312, ECO:0000269|PubMed:20300194,
CC ECO:0000269|PubMed:22768168, ECO:0000269|PubMed:24390142}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q08999}.
CC -!- INDUCTION: In the growth phase, expression is correlated with several
CC factors that lead to preference for the spore pathway. During
CC multicellular development, expression increases 200-fold in
CC differentiating spores. {ECO:0000269|PubMed:16495312}.
CC -!- DISRUPTION PHENOTYPE: In shaking culture, leads to a higher density, a
CC faster dying after reaching stationary density, and, after starvation,
CC a lower spore viability. However, shows abnormal slow proliferation on
CC bacterial lawns. Leads also to hypersensitivity to the stalk morphogen
CC DIF. {ECO:0000269|PubMed:16495312, ECO:0000269|PubMed:20300194,
CC ECO:0000269|PubMed:24390142}.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000305}.
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DR EMBL; AB211596; BAD95800.1; -; Genomic_DNA.
DR EMBL; AAFI02000164; EAL62136.1; -; Genomic_DNA.
DR RefSeq; XP_635645.1; XM_630553.1.
DR AlphaFoldDB; Q54FX2; -.
DR SMR; Q54FX2; -.
DR STRING; 44689.DDB0232004; -.
DR PaxDb; Q54FX2; -.
DR EnsemblProtists; EAL62136; EAL62136; DDB_G0290551.
DR GeneID; 8627717; -.
DR KEGG; ddi:DDB_G0290551; -.
DR dictyBase; DDB_G0290551; rblA.
DR eggNOG; KOG1010; Eukaryota.
DR HOGENOM; CLU_260636_0_0_1; -.
DR InParanoid; Q54FX2; -.
DR OMA; AILCELH; -.
DR PhylomeDB; Q54FX2; -.
DR Reactome; R-DDI-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-DDI-1538133; G0 and Early G1.
DR Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DDI-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DDI-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
DR Reactome; R-DDI-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-DDI-69231; Cyclin D associated events in G1.
DR Reactome; R-DDI-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR PRO; PR:Q54FX2; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; ISS:dictyBase.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:dictyBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; IGI:dictyBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:dictyBase.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:dictyBase.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEP:dictyBase.
DR GO; GO:0031156; P:regulation of sorocarp development; IEP:dictyBase.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR002720; RB_A.
DR InterPro; IPR002719; RB_B.
DR InterPro; IPR028309; RB_fam.
DR InterPro; IPR024599; RB_N.
DR PANTHER; PTHR13742; PTHR13742; 1.
DR Pfam; PF11934; DUF3452; 1.
DR Pfam; PF01858; RB_A; 1.
DR Pfam; PF01857; RB_B; 1.
DR SMART; SM01367; DUF3452; 1.
DR SMART; SM01368; RB_A; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 2: Evidence at transcript level;
KW Cell cycle; Chromatin regulator; Coiled coil; DNA-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1312
FT /note="Retinoblastoma-like protein A"
FT /id="PRO_0000431811"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 36..117
FT /evidence="ECO:0000255"
FT COILED 195..230
FT /evidence="ECO:0000255"
FT COMPBIAS 201..219
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1312 AA; 149427 MW; A6F8547005994AC6 CRC64;
MMAHNKNDLT NINTKTTAPT TTTTEQQPEQ QQQQPEQQQQ EKQNNNNNNN NNNNNNNNIN
NNENNENNNN DIINNKINLL DELVAAAELK GRYTQIQLEE LKSKLDRTSS ALNVDQDTIK
LAWCLLENMQ LVSVDTSEQF QKQIVACSLF ICGNKKFSSL LYNLNQPSSS SFQPDNNSKI
KGRKIRKTNN SKNKNNDSNE EEEETTTDTE EEEEEDTLLN ENNNSINKNS SNNNELLVSI
RSCINESGGD SQFLQNSVFL SQLLKHFEGE IKLSQFFDTL RSFISNLRLG NAFEEQGRQL
EQSFNTLNNL YRKYEQIFFT LFHPTENYIL KTTQQHNYNN NSNNNNNNNN NNNNNNNNNR
TNEDYLLSIG WLIFLFCKNK LFTKDSPDFV QSLHLLLCII NFIYVNTSIS ELKKIPQGVQ
IIDTATGDIL LYLAKSIPCN LDDLSNVNQN IFSTYSNLLI NNSILKLFDN NNNNNNNNNN
NNNNSDGIKS IFNNSSIIKD NYNSLNKSYE LYYYANGDID ERLFYSFDHD IYVLNNNNNN
QNNNNNNNNH NNNYYNNNNN NNNNNNNNNH LNYQYSSLLP PSTPTTPSRY GSSSSSGGGG
GGNLRKNIYG TPSKSLSAGN LGSVIPQTPI SLTLTLESWL KVEIQNYRDP NPSLNLINIL
KSADQPQQTS EVDKMIERVS SLTNNTDSLF SIGGIDDHQQ QQQQQQEVKQ RRKNMAIQLY
YCLLEKLIKF EQNTSSNINV LLNHEDFHKS LLSNSFEIIA YVYKMEGLYF PHFINVFKLH
PFSYLRLIDL VLKVDADLPK LLAQHFSQIE EKILEKYVWS NNSTVFSTIK SHDFQNIFNS
NGVGAAITTH LRPTQVFSTP TKNQNNNPFR NQQLINTNIP NTPTKKNPFI QNFIKKVSTL
IIAKCRKLIH AMGLSSDYVV QIYQVMIKIL IDETLLFKNR EIDVLLICSI YAICKVNSKN
ITFKAIIDKS CISAKVYKEV YIGNDENNNN NNNNNNNNNN NNNNNNNNIN NNNNNNENNN
NNNNPVKGDI ILFYNKIFLT KMDPYIHEVF SKYQQQQQHQ YQQPLQNLPP PLLNQNSPKK
WNPLFHTPTK NQNNNPYNSN NNTPNKFSSS IPLSPQKGVN YNSSFSVNSM VTISPMKQHT
PISSSYTYIV AKSPSKELFQ INQCLNKKKN DEMVPPPPTT PSSINNNNNN NNNNNNNNNN
NNNNNSNDNN NNNNNNNNNN NNNNSNNNSN NNNNTEKKMV GKRLLFDYEE SPSTPSSSSS
PTILNNNKKN NNNNKSENVD DPGNNSPSSS PLSSSSSSSS SSSSGGRKRL KS
