PHC2_XENLA
ID PHC2_XENLA Reviewed; 344 AA.
AC Q4V7W5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Polyhomeotic-like protein 2;
GN Name=phc2;
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 [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a PRC1-like complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; BC097691; AAH97691.1; -; mRNA.
DR RefSeq; NP_001089479.1; NM_001096010.1.
DR RefSeq; XP_018097321.1; XM_018241832.1.
DR RefSeq; XP_018097322.1; XM_018241833.1.
DR AlphaFoldDB; Q4V7W5; -.
DR SMR; Q4V7W5; -.
DR DNASU; 734530; -.
DR GeneID; 734530; -.
DR KEGG; xla:734530; -.
DR CTD; 734530; -.
DR Xenbase; XB-GENE-997001; phc2.L.
DR OrthoDB; 298184at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 734530; Expressed in oocyte and 11 other tissues.
DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.30.60.160; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..344
FT /note="Polyhomeotic-like protein 2"
FT /id="PRO_0000076289"
FT DOMAIN 280..344
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 114..148
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 25..53
FT /note="HD1"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
SQ SEQUENCE 344 AA; 37932 MW; 1FFB6C62686C85D2 CRC64;
MTSGNGSSPV PTAATGNRTQ NGENKPPQAV VKPQILTHFI EGFVIQEGAQ PFPSHRSRAV
LEVGHSSLLT GAQEKYQQSL LAEKVPQQDN NTTTTTTDSE MEETLVPGFP ESKGDGDPPK
LKCELCGRVD FEYKFKRSKR FCSMACAKRY NVGCTKRVGL FHPDRSKLQK PTVAKHARRR
SRKTPLQTVG ADPKKQQAAP VTPMNPGPIP SPSALKLSNS QEDSSRCSDN SSYEEPLSPM
SASSSLSRAR QEHNVEPPNL HSRDPIAMSQ DFLPSDPTKW NVEDVYDFVR SLPGCQEISE
EFRAQEIDGQ ALLLLKEDHL MSAMNIKLGP ALKLYARISM LKDS