PCGF1_RAT
ID PCGF1_RAT Reviewed; 243 AA.
AC Q6DLV9;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Polycomb group RING finger protein 1;
DE AltName: Full=Nervous system Polycomb-1;
DE Short=NSPc1;
DE Flags: Fragment;
GN Name=Pcgf1; Synonyms=Nspc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gong Y., Wang X., Yuan J.;
RT "Rattus norvegicus similar to Nspc1 protein full length cDNA.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=15620699; DOI=10.1016/j.febslet.2004.11.056;
RA Gong Y., Wang X., Liu J., Shi L., Yin B., Peng X., Qiang B., Yuan J.;
RT "NSPc1, a mainly nuclear localized protein of novel PcG family members, has
RT a transcription repression activity related to its PKC phosphorylation site
RT at S183.";
RL FEBS Lett. 579:115-121(2005).
CC -!- FUNCTION: Component of the Polycomb group (PcG) multiprotein BCOR
CC complex, a complex required to maintain the transcriptionally
CC repressive state of some genes, such as BCL6 and the cyclin-dependent
CC kinase inhibitor, CDKN1A. Transcriptional repressor that may be
CC targeted to the DNA by BCL6; this transcription repressor activity may
CC be related to PKC signaling pathway. Represses CDKN1A expression by
CC binding to its promoter, and this repression is dependent on the
CC retinoic acid response element (RARE element). Promotes cell cycle
CC progression and enhances cell proliferation as well. May have a
CC positive role in tumor cell growth by down-regulating CDKN1A. Component
CC of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex
CC class required to maintain the transcriptionally repressive state of
CC many genes, including Hox genes, throughout development. PcG PRC1
CC complex acts via chromatin remodeling and modification of histones; it
CC mediates monoubiquitination of histone H2A 'Lys-119', rendering
CC chromatin heritably changed in its expressibility. Within the PRC1-like
CC complex, regulates RNF2 ubiquitin ligase activity. Regulates the
CC expression of DPPA4 and NANOG in the NT2 embryonic carcinoma cells.
CC {ECO:0000250|UniProtKB:Q9BSM1}.
CC -!- SUBUNIT: Interacts with BCORL1, forming heterodimers (By similarity).
CC The PCGF1-BCORL1 heterodimeric complex interacts with the KDM2B-SKP1
CC heterodimeric complex to form a homotetrameric polycomb repression
CC complex 1 (PRC1.1) (By similarity). Component of the repressive BCOR
CC complex containing a Polycomb group subcomplex at least composed of
CC RYBP, RING1 and RNF2/RING2 (By similarity). Specifically interacts with
CC BCOR, RING1 and RNF2/RING2 (By similarity). Component of a PRC1-like
CC complex (By similarity). Interacts with CBX6, CBX7 and CBX8 (By
CC similarity). Interacts with DPPA4, NANOG, POU5F1 and RYBP (By
CC similarity). {ECO:0000250|UniProtKB:Q9BSM1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BSM1}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, cerebellum, heart and
CC testis. {ECO:0000269|PubMed:15620699}.
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DR EMBL; AY662670; AAT74859.1; -; mRNA.
DR RefSeq; NP_001007001.1; NM_001007000.1.
DR AlphaFoldDB; Q6DLV9; -.
DR SMR; Q6DLV9; -.
DR STRING; 10116.ENSRNOP00000011173; -.
DR PhosphoSitePlus; Q6DLV9; -.
DR PaxDb; Q6DLV9; -.
DR GeneID; 312480; -.
DR KEGG; rno:312480; -.
DR UCSC; RGD:1549782; rat.
DR CTD; 84759; -.
DR RGD; 1549782; Pcgf1.
DR eggNOG; KOG2660; Eukaryota.
DR InParanoid; Q6DLV9; -.
DR OrthoDB; 1203951at2759; -.
DR PhylomeDB; Q6DLV9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0035518; P:histone H2A monoubiquitination; ISO:RGD.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF16207; RAWUL; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN <1..243
FT /note="Polycomb group RING finger protein 1"
FT /id="PRO_0000277857"
FT ZN_FING 35..74
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 74..231
FT /note="Necessary for repressor activity"
FT /evidence="ECO:0000250"
FT REGION 138..239
FT /note="Required for the interaction with the KDM2B-SKP1
FT heterodimeric complex"
FT /evidence="ECO:0000250|UniProtKB:Q9BSM1"
FT REGION 151..239
FT /note="RING-finger and WD40-associated ubiquitin-like
FT domain (RAWUL); sufficient for interaction with BCOR and
FT BCORL1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSM1"
FT CROSSLNK 12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BSM1"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BSM1"
FT NON_TER 1
SQ SEQUENCE 243 AA; 28782 MW; 8D6630932F503A55 CRC64;
MRLRNQLQSV YKMDPLRNEE EVRVKIKDLN EHIVCCLCAG YFVDATTITE CLHTFCKSCI
VKYLQTSKYC PMCNIKIHET QPLLNLKLDR VMQDIVYKLV PGLQDSEEKR IRDFYQSRGL
DRVSQPSGEE PALRGLGLPF TSFDHYYRYD EQLSLCLERL SSGKDKNKNV LQNKYVRCSV
RAEVRHLRRV LCHRLMLNPQ HVQLLFDNEV LPDHMTMKQL WLSRWFGKPS PLLLQYSVKE
KRR
