RBR1_MAIZE
ID RBR1_MAIZE Reviewed; 867 AA.
AC Q9LKX9; O22344; Q7DLV4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Retinoblastoma-related protein 1;
DE Short=Rb1;
DE Short=ZmRBR1;
GN Name=RBR1; Synonyms=RRB1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-654, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TOMATO GOLDEN MOSAIC VIRUS REP
RP AND ARABIDOPSIS CYCD3-1.
RC STRAIN=cv. B73;
RX PubMed=9271385; DOI=10.1128/mcb.17.9.5077;
RA Ach R.A., Durfee T., Miller A.B., Taranto P., Hanley-Bowdoin L.,
RA Zambryski P.C., Gruissem W.;
RT "RRB1 and RRB2 encode maize retinoblastoma-related proteins that interact
RT with a plant D-type cyclin and geminivirus replication protein.";
RL Mol. Cell. Biol. 17:5077-5086(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-654, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=12602870; DOI=10.1023/a:1022090916446;
RA Rossi V., Locatelli S., Lanzanova C., Boniotti M.B., Varotto S., Pipal A.,
RA Goralik-Schramel M., Lusser A., Gatz C., Gutierrez C., Motto M.;
RT "A maize histone deacetylase and retinoblastoma-related protein physically
RT interact and cooperate in repressing gene transcription.";
RL Plant Mol. Biol. 51:401-413(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 180-867, TISSUE SPECIFICITY, AND INTERACTION
RP WITH WHEAT DWARF VIRUS REPA.
RX PubMed=8890163; DOI=10.1002/j.1460-2075.1996.tb00870.x;
RA Xie Q., Sanz-Burgos A.P., Hannon G.J., Gutierrez C.;
RT "Plant cells contain a novel member of the retinoblastoma family of growth
RT regulatory proteins.";
RL EMBO J. 15:4900-4908(1996).
RN [4]
RP INTERACTION WITH WHEAT DWARF VIRUS REPA.
RX PubMed=14741123; DOI=10.1016/j.vetmic.2003.10.012;
RA Gutierrez C., Ramirez-Parra E., Mar Castellano M., Sanz-Burgos A.P.,
RA Luque A., Missich R.;
RT "Geminivirus DNA replication and cell cycle interactions.";
RL Vet. Microbiol. 98:111-119(2004).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17389586; DOI=10.1093/jxb/erm022;
RA Lendvai A., Pettko-Szandtner A., Csordas-Toth E., Miskolczi P.,
RA Horvath G.V., Gyoergyey J., Dudits D.;
RT "Dicot and monocot plants differ in retinoblastoma-related protein
RT subfamilies.";
RL J. Exp. Bot. 58:1663-1675(2007).
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 -!- SUBUNIT: Interacts with RPD3I, RBAP1, the Arabidopsis cyclin CYCD3-1,
CC the mastrevirus replication-associated protein A (RepA) and the
CC begomovirus replication-associated protein (Rep).
CC {ECO:0000269|PubMed:14741123, ECO:0000269|PubMed:8890163,
CC ECO:0000269|PubMed:9271385}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9271385}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8890163,
CC ECO:0000269|PubMed:9271385}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 5 to 8 days after pollination
CC endosperm and does not change significantly during later developmental
CC stages. {ECO:0000269|PubMed:12602870}.
CC -!- DOMAIN: The C-terminal domain (743-867) is required for binding of
CC RPD3I and RBAP1.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA67422.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF250050; AAF97520.1; -; mRNA.
DR EMBL; AF007793; AAB69649.1; -; mRNA.
DR EMBL; X98923; CAA67422.1; ALT_INIT; mRNA.
DR PIR; T01171; T01171.
DR RefSeq; NP_001104876.1; NM_001111406.1.
DR RefSeq; XP_008668606.1; XM_008670384.1.
DR AlphaFoldDB; Q9LKX9; -.
DR SMR; Q9LKX9; -.
DR ELM; Q9LKX9; -.
DR STRING; 4577.GRMZM2G003043_P01; -.
DR PaxDb; Q9LKX9; -.
DR GeneID; 541651; -.
DR KEGG; zma:541651; -.
DR MaizeGDB; 273689; -.
DR eggNOG; KOG1010; Eukaryota.
DR OrthoDB; 113612at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9LKX9; baseline and differential.
DR Genevisible; Q9LKX9; ZM.
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; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:InterPro.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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 InterPro; IPR015652; RBR.
DR PANTHER; PTHR13742; PTHR13742; 1.
DR PANTHER; PTHR13742:SF22; PTHR13742:SF22; 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 1: Evidence at protein level;
KW Cell cycle; Host-virus interaction; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..867
FT /note="Retinoblastoma-related protein 1"
FT /id="PRO_0000335246"
FT REGION 275..722
FT /note="Pocket; binds RPD3I and RBAP1"
FT REGION 275..476
FT /note="Domain A"
FT REGION 477..594
FT /note="Spacer"
FT REGION 512..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..722
FT /note="Domain B"
FT REGION 734..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 654
FT /note="C->F: Loss of interaction with RPD3I or CYCD3-1, but
FT not with RBAP1."
FT /evidence="ECO:0000269|PubMed:12602870,
FT ECO:0000269|PubMed:9271385"
FT CONFLICT 15
FT /note="Missing (in Ref. 1; AAB69649)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="C -> Y (in Ref. 2; AAF97520)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="I -> V (in Ref. 2; AAF97520)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="A -> S (in Ref. 2; AAF97520)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="S -> F (in Ref. 2; AAF97520)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="V -> L (in Ref. 2; AAF97520)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 867 AA; 96200 MW; 3B2DB7A1E5A3BEEF CRC64;
MSSLDPSPAT STQQQKQLES LVNLLTQGSR FYRKAYNELF SGVTTEQDPD SSTNIPEYML
FGWHLFLMLH LRSPELFKDL VSCIHGLVAV LAILLIHVPA KFRSFTIEGS SHLIKQTEKG
VDLIASLCHN YHTSEERLKE MLHKSHNAIE DIFHMKALSA SECKPENLDK IDTDDLMYFK
GLIDMECFQS NLEKMEKLCN SNSCKGELDF KSILINNDYI PYDENSTGDS TNLGHSKCAF
ETLASPTKTI KNMLTVPSSP LSPATGGSVK IVQMTPVTSA MTTAKWLREV ISSLPDKPSS
KLQQFLSSCD RDLTNAVTER VSIVLEAIFP TKSSANRGVS LGLNCANAFD IPWAEARKVE
ASKLYYRVLE AICRAELQNS NVNNLTPLLS NERFHRCLIA CSADLVLATH KTVIMMFPAV
LESTGLTAFD LSKIIENFVR HEETLPRELK RHLNSLEEQL LESMAWEKGS SLYNSLIVAR
PSVASEINRL GLLAEPMPSL DDLVSRQNVR IEGLPATPSK KRAAGPDDNA DPRSPKRSCN
ESRNTVVERN LQTPPPKQSH MVSTSLKAKC HPLQSTFASP TVCNPVGGNE KCADVTIHIF
FSKILKLAAI RIRNLCERVQ CVEQTERVYN VFKQILEQQT TLFFNRHIDQ LILCCLYGVA
KVCQLELTFR EILNNYKREA QCKPEVFSSI YIGSTNRNGV LVSRHVGIIT FYNEVFVPAA
KPFLVSLISS GTHPEDKKNA SGQIPGSPKP SPFPNLPDMS PKKVSASHNV YVSPLRQTKL
DLLLSPSSRS FYACIGEGTH AYQSPSKDLA AINSRLNYNG RKVNSRLNFD MVSDSVVAGS
LGQINGGSTS DPAAAFSPLS KKRETDT
