PCGF3_MOUSE
ID PCGF3_MOUSE Reviewed; 241 AA.
AC Q8BTQ0; Q8BZT0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Polycomb group RING finger protein 3;
DE AltName: Full=RING finger protein 3A;
GN Name=PcgF3; Synonyms=Rnf3, Rnf3a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH RNF2, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=28596365; DOI=10.1126/science.aal2512;
RA Almeida M., Pintacuda G., Masui O., Koseki Y., Gdula M., Cerase A.,
RA Brown D., Mould A., Innocent C., Nakayama M., Schermelleh L.,
RA Nesterova T.B., Koseki H., Brockdorff N.;
RT "PCGF3/5-PRC1 initiates Polycomb recruitment in X chromosome
RT inactivation.";
RL Science 356:1081-1084(2017).
CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like
CC complex, a complex class required to maintain the transcriptionally
CC repressive state of many genes, including Hox genes, throughout
CC development. PcG PRC1 complex acts via chromatin remodeling and
CC modification of histones; it mediates monoubiquitination of histone H2A
CC 'Lys-119', rendering chromatin heritably changed in its expressibility
CC (PubMed:28596365). Within the PRC1-like complex, regulates RNF2
CC ubiquitin ligase activity (By similarity). Plays a redundant role with
CC PCGF5 as part of a PRC1-like complex that mediates monoubiquitination
CC of histone H2A 'Lys-119' on the X chromosome and is required for normal
CC silencing of one copy of the X chromosome in XX females
CC (PubMed:28596365). {ECO:0000250|UniProtKB:Q3KNV8,
CC ECO:0000269|PubMed:28596365}.
CC -!- SUBUNIT: Component of a PRC1-like complex that contains PCGF3, RNF2 and
CC RYBP (PubMed:28596365). Interacts with RNF2 (PubMed:28596365).
CC Interacts with CBX6, CBX7 and CBX8 (By similarity). Interacts with
CC BCORL1 (By similarity). {ECO:0000250|UniProtKB:Q3KNV8,
CC ECO:0000269|PubMed:28596365}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28596365}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:28596365}. Note=Recruited by the non-
CC coding RNA Xist to specific nuclear foci that probably correspond to
CC the inactivated X chromosome. {ECO:0000269|PubMed:28596365}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BTQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BTQ0-2; Sequence=VSP_023116, VSP_023117;
CC -!- DISRUPTION PHENOTYPE: Combined disruption of both Pcgf3 and Pcgf5
CC causes embryonic lethality; there are no live progeny. Male embryos are
CC detected at 9.5 and 10.5 dpc, but are smaller than normal. Female
CC embryos are already extensively degraded at 9.5 dpc. Placentas from
CC male embryos have some parietal trophoblast giant cells, but fail to
CC form a labyrinth. Placentas from female embryos lack trophoblasts
CC altogether and fail to form a labyrinth. Defects can be attributed to
CC the observed lack of monoubiquitination of histone H2A 'Lys-119' and
CC lack of Xist-mediated silencing of one copy of the X chromosome.
CC {ECO:0000269|PubMed:28596365}.
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DR EMBL; AK033609; BAC28388.1; -; mRNA.
DR EMBL; AK089091; BAC40745.1; -; mRNA.
DR EMBL; BC049266; AAH49266.1; -; mRNA.
DR CCDS; CCDS19512.1; -. [Q8BTQ0-1]
DR RefSeq; NP_766304.2; NM_172716.4. [Q8BTQ0-1]
DR AlphaFoldDB; Q8BTQ0; -.
DR SMR; Q8BTQ0; -.
DR BioGRID; 213553; 1.
DR IntAct; Q8BTQ0; 1.
DR STRING; 10090.ENSMUSP00000041790; -.
DR PhosphoSitePlus; Q8BTQ0; -.
DR MaxQB; Q8BTQ0; -.
DR PaxDb; Q8BTQ0; -.
DR PRIDE; Q8BTQ0; -.
DR ProteomicsDB; 287889; -. [Q8BTQ0-1]
DR ProteomicsDB; 287890; -. [Q8BTQ0-2]
DR Antibodypedia; 4972; 162 antibodies from 29 providers.
DR DNASU; 69587; -.
DR Ensembl; ENSMUST00000046975; ENSMUSP00000041790; ENSMUSG00000033623. [Q8BTQ0-1]
DR Ensembl; ENSMUST00000112597; ENSMUSP00000108216; ENSMUSG00000033623. [Q8BTQ0-2]
DR GeneID; 69587; -.
DR KEGG; mmu:69587; -.
DR UCSC; uc008yod.1; mouse. [Q8BTQ0-2]
DR UCSC; uc008yoe.1; mouse. [Q8BTQ0-1]
DR CTD; 10336; -.
DR MGI; MGI:1916837; Pcgf3.
DR VEuPathDB; HostDB:ENSMUSG00000033623; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000158395; -.
DR HOGENOM; CLU_046427_4_3_1; -.
DR InParanoid; Q8BTQ0; -.
DR OMA; ILCNNEL; -.
DR OrthoDB; 1203951at2759; -.
DR PhylomeDB; Q8BTQ0; -.
DR TreeFam; TF324206; -.
DR BioGRID-ORCS; 69587; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Pcgf3; mouse.
DR PRO; PR:Q8BTQ0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BTQ0; protein.
DR Bgee; ENSMUSG00000033623; Expressed in superior cervical ganglion and 236 other tissues.
DR ExpressionAtlas; Q8BTQ0; baseline and differential.
DR Genevisible; Q8BTQ0; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031519; C:PcG protein complex; IDA: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:0036353; P:histone H2A-K119 monoubiquitination; IMP:UniProtKB.
DR GO; GO:0060819; P:inactivation of X chromosome by genomic imprinting; IMP:UniProtKB.
DR GO; GO:0006357; P: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 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..241
FT /note="Polycomb group RING finger protein 3"
FT /id="PRO_0000277865"
FT ZN_FING 17..56
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 115..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..241
FT /note="Interaction with BCORL1"
FT /evidence="ECO:0000250|UniProtKB:Q3KNV8"
FT VAR_SEQ 155..178
FT /note="SICLECNSSKLRGLKRKWIRCSAQ -> NTRPLWIFWHQFIPCLRTSFENVT
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023116"
FT VAR_SEQ 179..241
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023117"
SQ SEQUENCE 241 AA; 28046 MW; 1F4645C6E7A3DEA5 CRC64;
MLTRKIKLWD INAHITCRLC SGYLIDATTV TECLHTFCRS CLVKYLEENN TCPTCRIVIH
QSHPLQYIGH DRTMQDIVYK LVPGLQEAEM RKQREFYHKL GMEVPGDIKG EACSAKQHLD
PRNGETKADD NSNKETAEEK QEEDNDYHRS DEQVSICLEC NSSKLRGLKR KWIRCSAQAT
VLHLKKFIAK KLNLSSFNEL DILCNEEILG KDHTLKFVVV TRWRFKKAPL LLHYRPKMDL
L
