ID   BMI1A_XENLA             Reviewed;         326 AA.
AC   Q91648; Q6GQ56;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Polycomb complex protein BMI-1-A;
DE   AltName: Full=Polycomb group RING finger protein 4-A;
GN   Name=bmi1a; Synonyms=pcgf4, xbmi-1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CBX4, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=8555110; DOI=10.1016/0925-4773(95)00422-x;
RA   Reijnen M.J., Hamer K.M., den Blaauwen J.L., Lambrechts C., Schoneveld I.,
RA   van Driel R., Otte A.P.;
RT   "Polycomb and bmi-1 homologs are expressed in overlapping patterns in
RT   Xenopus embryos and are able to interact with each other.";
RL   Mech. Dev. 53:35-46(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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       In the PRC1 complex, it is required to stimulate the E3 ubiquitin-
CC       protein ligase activity of rnf2 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of a PRC1-like complex (By similarity). Interacts
CC       with cbx4. {ECO:0000250, ECO:0000269|PubMed:8555110}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Maternally derived transcript is detected at high
CC       levels in blastula. Detected at intermediate levels in the head region,
CC       the rhombencephalon, otic vesicle, mesencephalon, optic vesicle and in
CC       the anterior parts of the spinal cord in late neurula stages.
CC       {ECO:0000269|PubMed:8555110}.
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DR   EMBL; U39959; AAC59729.1; -; mRNA.
DR   EMBL; BC072892; AAH72892.1; -; mRNA.
DR   PIR; I51694; I51694.
DR   RefSeq; NP_001081790.1; NM_001088321.1.
DR   AlphaFoldDB; Q91648; -.
DR   SMR; Q91648; -.
DR   DNASU; 398052; -.
DR   GeneID; 398052; -.
DR   KEGG; xla:398052; -.
DR   CTD; 398052; -.
DR   Xenbase; XB-GENE-6252040; bmi1.S.
DR   OrthoDB; 1344247at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 398052; Expressed in blastula and 19 other tissues.
DR   GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISS:UniProtKB.
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   Chromatin regulator; Metal-binding; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..326
FT                   /note="Polycomb complex protein BMI-1-A"
FT                   /id="PRO_0000296632"
FT   ZN_FING         18..57
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          239..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           81..95
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        239..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        160
FT                   /note="I -> T (in Ref. 2; AAH72892)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   326 AA;  36945 MW;  8D11B4C5EC6C2F59 CRC64;
     MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IIECLHSFCK TCIVRYLETS KYCPICDVQV
     HKTRPLLNIR ADKTLQDIVY KLVPGLFKGE MKRRRDFYAA HPSADVANGS NEDRGEVADE
     DKRIITDDEI ISLSIEFFDQ NKADRKGSKD KDKEKSKDEI NDKRYLRCPA ALTIMHLRKF
     LRSKMDIPSN FQIDVMYEEE ALKDYYTLMD IAYIYTWRRN GPLPLKYRVR PTCKRVKINP
     HTDRINHTSG DMESDSGSDK AGSLGVVIPS TSSCIPSPPV QSPHPHFPHI SSTINGTSSS
     SSSHQNPFTN RARKISLNGV SAISSG