ID A0A0Q3M3V2_BRADI Unreviewed; 1034 AA.
AC A0A0Q3M3V2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 08-NOV-2023, entry version 35.
DE RecName: Full=Retinoblastoma-related protein {ECO:0008006|Google:ProtNLM};
GN Name=100826156 {ECO:0000313|EnsemblPlants:KQJ99189};
GN ORFNames=BRADI_3g41630v3 {ECO:0000313|EMBL:KQJ99189.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ99189.1};
RN [1] {ECO:0000313|EMBL:KQJ99189.1, ECO:0000313|EnsemblPlants:KQJ99189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ99189.1,
RC ECO:0000313|EnsemblPlants:KQJ99189};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ99189.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ99189.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ99189}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ99189};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- FUNCTION: Regulator of biological processes that recruits a histone
CC deacetylase to control gene transcription. May play a role in the entry
CC into mitosis, negatively regulating the cell proliferation. Formation
CC of stable complexes with geminiviridae replication-associated proteins
CC may create a cellular environment which favors viral DNA replication.
CC {ECO:0000256|ARBA:ARBA00025018}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000256|ARBA:ARBA00009475}.
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DR EMBL; CM000882; KQJ99189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q3M3V2; -.
DR EnsemblPlants; KQJ99189; KQJ99189; BRADI_3g41630v3.
DR Gramene; KQJ99189; KQJ99189; BRADI_3g41630v3.
DR Proteomes; UP000008810; Chromosome 3.
DR ExpressionAtlas; A0A0Q3M3V2; baseline.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 1.10.472.140; -; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR002720; RB_A.
DR InterPro; IPR002719; RB_B.
DR InterPro; IPR015030; RB_C.
DR InterPro; IPR028309; RB_fam.
DR InterPro; IPR024599; RB_N.
DR PANTHER; PTHR13742:SF17; RETINOBLASTOMA-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR13742; RETINOBLASTOMA-ASSOCIATED PROTEIN RB -RELATED; 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 SMART; SM01369; Rb_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 100..240
FT /note="Retinoblastoma-associated protein N-terminal"
FT /evidence="ECO:0000259|SMART:SM01367"
FT DOMAIN 425..625
FT /note="Retinoblastoma-associated protein A-box"
FT /evidence="ECO:0000259|SMART:SM01368"
FT DOMAIN 884..1025
FT /note="Retinoblastoma-associated protein C-terminal"
FT /evidence="ECO:0000259|SMART:SM01369"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 114169 MW; CEE6DCF48C8A3FA3 CRC64;
MEGADAPPPG TPGAGDDGSR STAVSRTDDA ATAAAMEQRF ADLCKSKLAL NESMMRQAMQ
LFKETKKILL SSMSSLGSGS PEEIQRFWSA FVLFCVSRLG KAGKAKEDGG ITLHQILRAF
EIKLVDFFKE MPQFCIKVGC VLTGLYGSDW EKKLEELQAT VVHLCSLGRH YKRAYQELFL
SNDGKPADNP SEPNAQLASE YYRFGWLLFV LLRIQTNSRF KDLLTSITEL VSVLAVLIVH
IPVRLRKFSI EDSSFFAKKS DKGVNLIASL CEKHLTSADE LRKSLEKTNT LIMDILEKKP
CMDASECQQN NLSFIDPEGL TFFKNFMEED SLKSSLLILD KEYENAINTK GELDERMFAN
DDDSFLGSGS LSGGAIKLPG TKRKYDVLAS PSKSAISPSP MSPPRFCASP NGNSFGNSKM
APPLTPVSTA MTTAKWLRST ISPLPSRPSG ELLRFFSACD KDVTDDITRR AAIILGAIFT
GNSFGERMCT TVRSTNGFDA IWTEQRKMEA LKLYYRVLES MCRAESHVLS GSNLTSLLSN
ERFHRCMIAC SAELVLATHK TVTMMFPAVL EKTGITAFDL SKVIESFVRH EDTLPRELKR
HLNSLEERLL ESLAWEKGSS MYNSLIVARP TLSVEINRLG LLAEPMPSLD AIVAHHDISL
GGLPPLPFQK QERSPDKDEV RSPKRACTER RNVLVDSNSF RSPVKDTIKL KILPPLQSAF
ASPTRPNPAA GGETCAETGI GVFLSKIAKL AAIRIKGLCE RLQLPQQILE RVYSLVQQII
SQQTALFFNR HIDQIILCSI YGVAKISQLS LTFKEIIFSY RKQPQCKLQV FRSVFVHRPS
RSRTGKTGED HVDIITFYNE VFIPTVKPLL VDLGSGASPN KNNGEKNATD AVPFPESPRL
TRFPTLPDMS PKKVSATHNV YVSPLRSSKM DTLLSPSSKS YYACVGESTH AFQSPSKDLK
AINTRLNSGK KVSGRLNFDV VSDLDVARSL SDQNGASTSM VVLGARSLGD QNGGYTPMKV
LAAKPPVKCE QTDS
//
