RB_CHICK
ID RB_CHICK Reviewed; 921 AA.
AC Q90600; Q788Q6; Q90599; Q91016;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Retinoblastoma-associated protein;
DE AltName: Full=p104;
DE AltName: Full=pRb;
DE Short=Rb;
GN Name=RB1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RC STRAIN=SPAFAS;
RX PubMed=8180136;
RA Boehmelt G., Ulrich E., Kurzbauer R., Mellitzer G., Bird A., Zenke M.;
RT "Structure and expression of the chicken retinoblastoma gene.";
RL Cell Growth Differ. 5:221-230(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8193168; DOI=10.1016/0167-4781(94)90103-1;
RA Feinstein R., Bolton W.K., Quinones J.N., Mosialos G., Sif S., Huff J.L.,
RA Capobianco A.J., Gilmore T.D.;
RT "Characterization of a chicken cDNA encoding the retinoblastoma gene
RT product.";
RL Biochim. Biophys. Acta 1218:82-86(1994).
RN [3]
RP INTERACTION WITH FOWL ADENOVIRUS 1 PROTEIN GAM-1 (MICROBIAL INFECTION).
RX PubMed=10400747; DOI=10.1128/jvi.73.8.6517-6525.1999;
RA Lehrmann H., Cotten M.;
RT "Characterization of CELO virus proteins that modulate the pRb/E2F
RT pathway.";
RL J. Virol. 73:6517-6525(1999).
CC -!- FUNCTION: Tumor suppressor that is a key regulator of the G1/S
CC transition of the cell cycle. The hypophosphorylated form binds
CC transcription regulators of the E2F family, preventing transcription of
CC E2F-responsive genes. Both physically blocks E2Fs transactivating
CC domain and recruits chromatin-modifying enzymes that actively repress
CC transcription. Cyclin and CDK-dependent phosphorylation of RB1 induces
CC its dissociation from E2Fs, thereby activating transcription of E2F
CC responsive genes and triggering entry into S phase. RB1 also promotes
CC the G0-G1 transition upon phosphorylation and activation by
CC CDK3/cyclin-C. {ECO:0000250|UniProtKB:P06400,
CC ECO:0000250|UniProtKB:P13405, ECO:0000250|UniProtKB:P33568}.
CC -!- SUBUNIT: Interacts with and sequesters the E2F1 transcription factor.
CC Interacts with SUV39H1, KMT5B and KMT5C (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: (Microbial infection) Interacts with, and is inhibited by fowl
CC adenovirus 1 protein GAM-1. {ECO:0000269|PubMed:10400747}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P13405}.
CC -!- PTM: Phosphorylated in G1, thereby releasing E2F1 which is then able to
CC activate cell growth. Dephosphorylated at the late M phase.
CC Phosphorylation of domain C promotes interaction between the C-terminal
CC domain C and the Pocket domain, and thereby inhibits interactions with
CC heterodimeric E2F/DP transcription factor complexes (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA19644.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X72218; CAA51019.1; -; mRNA.
DR EMBL; U00113; AAA19644.1; ALT_FRAME; mRNA.
DR EMBL; X72217; CAA51018.1; -; Genomic_DNA.
DR PIR; S45298; S45298.
DR RefSeq; NP_989750.1; NM_204419.1.
DR AlphaFoldDB; Q90600; -.
DR SMR; Q90600; -.
DR STRING; 9031.ENSGALP00000027407; -.
DR PaxDb; Q90600; -.
DR GeneID; 386582; -.
DR KEGG; gga:386582; -.
DR CTD; 5925; -.
DR VEuPathDB; HostDB:geneid_386582; -.
DR eggNOG; KOG1010; Eukaryota.
DR InParanoid; Q90600; -.
DR OrthoDB; 113612at2759; -.
DR PhylomeDB; Q90600; -.
DR PRO; PR:Q90600; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035189; C:Rb-E2F complex; ISS:UniProtKB.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR013763; Cyclin-like.
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; PTHR13742; 1.
DR Pfam; PF11934; DUF3452; 1.
DR Pfam; PF01858; RB_A; 1.
DR Pfam; PF01857; RB_B; 1.
DR Pfam; PF08934; Rb_C; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SMART; SM01367; DUF3452; 1.
DR SMART; SM01368; RB_A; 1.
DR SMART; SM01369; Rb_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Chromatin regulator; DNA-binding; Host-virus interaction;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor.
FT CHAIN 1..921
FT /note="Retinoblastoma-associated protein"
FT /id="PRO_0000331619"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 853..869
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P13405"
FT COMPBIAS 610..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 63
FT /note="Q -> E (in Ref. 2; AAA19644)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="E -> S (in Ref. 2; AAA19644)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="S -> C (in Ref. 2; AAA19644)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="N -> G (in Ref. 2; AAA19644)"
FT /evidence="ECO:0000305"
FT CONFLICT 791..792
FT /note="VP -> A (in Ref. 2; AAA19644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 921 AA; 104436 MW; 8527B7B4ACB12F36 CRC64;
MPPKPLRRAG AARSQRTSPE GGAGTASPPG GTRLEVGEAE FVALCDALKA PDSVREKAWM
TYQSLAAADG ASAYNKKKKE TWGVCIFIVA IDLDEMTFTF TELLKSLSIS VCTFFQFLKE
VDVNMDTVST KVDSTVSRLK KKYDVLLALY HKFERTCGLI YLEQPSSEIS AELSSVLVLK
NYWITFLLAK GKVLQMEDDL VISFQLLLCV LDYFIKLSPP AMLKEPYKSA VTALTVNGST
RTPRRGQNRN ARASKQIDTD TKVIEILCKE HDCNLDEVKN VYFTSFIPFL NSLGVVASNG
LPEVDVLSKQ YDELYLKNKD IDARLFLDHD ETLQPDVIAC SQLERTPRKN NPDEEVNHVL
PQTPVRAAMN TIQQLMMILN SATDKPSDTL IAYFNNCTVN PEDSILKRVE SLGHIFKKKF
AEAVGQGCAE IGSQRYQLGV RLYYRVMESM LKSEEERLSV HNFSKLLNDN IFHTSLLACA
LEIVMATYGR TASQSDGTSA ETDLSFPWIL NVFDLKAFDF YKVIESFIKV EPSLTRDMIK
HLERCEHRIM ESLAWQSDSP LFDLIKQSKE REGQTDQPEP TSTLNLPLQH NHTAADLYLS
PVRSPKKKAS GHPQSGTSNP DAQPSATSQT QKPQKSTSLS LFYKKVFRLA YLRLHTLFFR
LLSEHPDLEP LIWTLFQHTL QNESELMRDR HLDQIMMCSM YGICKVKNVD LRFKTIVSAY
KELPNTNQET FKRVLIREEQ YDSIIVFYNL VFMQKLKTNI LQYASNRPPT LSPIPHIPRS
PYQFSNSPRR VPAGNNIYIS PLKSPYKFSD GFHSPTKMTP RSRILVSIGE TFGTSEKFQK
INQMVCNSES HVKRSAEPSD APKPLKRLRF DIEGQDEADG GKHLPQESKF QQKLAEMTST
RTRMQKQKLN DGNDTSANEE K
