SOP2_CAEEL
ID SOP2_CAEEL Reviewed; 735 AA.
AC Q965H3; A3QMA2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Polycomb protein sop-2;
DE AltName: Full=Suppressor of pal-1 protein 2;
GN Name=sop-2; ORFNames=C50E10.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DIMERIZATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF PRO-633.
RX PubMed=12791274; DOI=10.1016/s1534-5807(03)00136-9;
RA Zhang H., Azevedo R.B.R., Lints R., Doyle C., Teng Y., Haber D.,
RA Emmons S.W.;
RT "Global regulation of Hox gene expression in C. elegans by a SAM domain
RT protein.";
RL Dev. Cell 4:903-915(2003).
RN [3]
RP RNA-BINDING.
RX PubMed=15200961; DOI=10.1016/j.molcel.2004.06.001;
RA Zhang H., Christoforou A., Aravind L., Emmons S.W., Van Den Heuvel S.,
RA Haber D.A.;
RT "The C. elegans Polycomb gene sop-2 encodes an RNA binding protein.";
RL Mol. Cell 14:841-847(2004).
RN [4]
RP SUBCELLULAR LOCATION, INTERACTION WITH UBC-9, AND SUMOYLATION.
RX PubMed=15107848; DOI=10.1038/ng1336;
RA Zhang H., Smolen G.A., Palmer R., Christoforou A., van den Heuvel S.,
RA Haber D.A.;
RT "SUMO modification is required for in vivo Hox gene regulation by the
RT Caenorhabditis elegans Polycomb group protein SOP-2.";
RL Nat. Genet. 36:507-511(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH SOR-1.
RX PubMed=16501168; DOI=10.1242/dev.02275;
RA Zhang T., Sun Y., Tian E., Deng H., Zhang Y., Luo X., Cai Q., Wang H.,
RA Chai J., Zhang H.;
RT "RNA-binding proteins SOP-2 and SOR-1 form a novel PcG-like complex in C.
RT elegans.";
RL Development 133:1023-1033(2006).
CC -!- FUNCTION: Polycomb group (PcG) protein. PcG proteins act by forming
CC multiprotein complexes, which are required to maintain the
CC transcriptionally repressive state of homeotic genes throughout
CC development. PcG proteins are not required to initiate repression, but
CC to maintain it during later stages of development. Also required to
CC repress expression of other genes and for localization of sor-1. Binds
CC RNA. {ECO:0000269|PubMed:12791274, ECO:0000269|PubMed:16501168}.
CC -!- SUBUNIT: Homodimer. Interacts with ubc-9. Binds through its N-terminal
CC region to the N-terminal region of sor-1. {ECO:0000269|PubMed:15107848,
CC ECO:0000269|PubMed:16501168}.
CC -!- INTERACTION:
CC Q965H3; P34619: sor-1; NbExp=4; IntAct=EBI-331594, EBI-326963;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12791274,
CC ECO:0000269|PubMed:15107848}. Note=Forms subnuclear bodies.
CC -!- TISSUE SPECIFICITY: Widely expressed. Weakly expressed in most somatic
CC cells of 50-cell stage embryos. At 200 cell stage, it is strongly
CC expressed. By comma stage, it is expressed in most somatic cells.
CC {ECO:0000269|PubMed:12791274}.
CC -!- DOMAIN: The RNA-binding region is essential for the localization to
CC subnuclear bodies and its function.
CC -!- DOMAIN: The SAM-like domain, although only slightly related to the SAM
CC domain, apparently displays a similar function. It is essential for
CC homodimerization, the interaction with ubc-9, and the formation of
CC subnuclear bodies.
CC -!- PTM: Sumoylated by ubc-9. Sumoylation is required for the
CC transcriptional regulation of homeotic genes.
CC {ECO:0000269|PubMed:15107848}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU457740; CAM36334.1; -; Genomic_DNA.
DR RefSeq; NP_001254341.1; NM_001267412.1.
DR AlphaFoldDB; Q965H3; -.
DR BioGRID; 40175; 13.
DR DIP; DIP-25161N; -.
DR IntAct; Q965H3; 6.
DR STRING; 6239.C50E10.4b; -.
DR EPD; Q965H3; -.
DR PaxDb; Q965H3; -.
DR PRIDE; Q965H3; -.
DR EnsemblMetazoa; C50E10.4a.1; C50E10.4a.1; WBGene00004945.
DR GeneID; 174874; -.
DR UCSC; C50E10.4; c. elegans.
DR CTD; 174874; -.
DR WormBase; C50E10.4a; CE32334; WBGene00004945; sop-2.
DR eggNOG; ENOG502SA26; Eukaryota.
DR GeneTree; ENSGT00970000198327; -.
DR InParanoid; Q965H3; -.
DR SignaLink; Q965H3; -.
DR PRO; PR:Q965H3; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004945; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q965H3; baseline and differential.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:WormBase.
DR GO; GO:0019899; F:enzyme binding; IPI:WormBase.
DR GO; GO:0042802; F:identical protein binding; IPI:WormBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IGI:WormBase.
DR GO; GO:0007411; P:axon guidance; IMP:WormBase.
DR GO; GO:0010607; P:negative regulation of cytoplasmic mRNA processing body assembly; IMP:WormBase.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0048665; P:neuron fate specification; IMP:WormBase.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0042659; P:regulation of cell fate specification; IMP:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:0040034; P:regulation of development, heterochronic; IMP:WormBase.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Chromatin regulator; Nucleus; Reference proteome; Repressor; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..735
FT /note="Polycomb protein sop-2"
FT /id="PRO_0000072039"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..503
FT /note="RNA-binding"
FT REGION 300..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..712
FT /note="SAM-like"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 633
FT /note="P->S: In bx91; induces derepression of homeotic
FT genes and affects sumoylation at 25 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:12791274"
SQ SEQUENCE 735 AA; 80814 MW; BE95913E04329519 CRC64;
MSSNLTSNEM SSTSAIVEPP EAVKGNERDK STRRSTSQVV RPEKHEVENA LEDQCSSSSL
PKEAQYYAKL DKKLEGKDPR SQFYEAVRLS ADIFAHKFEK AVCSRQTFEP TNSIIKVLNT
AEEEMLHEKV VPLPVSSKLQ YYLNRGRYDT IFDRDEQLQR TADPMADEPD HVEKRVTSIL
EQASREMEEG EVEPVFYDGS DEDQELPIDL GAMRNLQRTN KFAARSSRMA ARRGGRPGYR
GAFRGAARGA PSRRPAPAAE VAPETPVAAP MAPAAPAAPA TPEAAPAAEV MDTSIATEMP
QESAVDLSNV SAATEMDTSK EGEASRPTSE KKKKIRTTEM DRLMSMDLGP KDGGRVGELG
HMWPESRRRP AAPLPETPAA QPRKSLPRRA AEKKKPEDSD AAEEQEVEME VDNDASTSTP
RNARGGRGGG NRRGSRRGQK RTSGGSGKLV EPKKEPVDEP AEKIPKRSEA APEVPATATT
KEAPPSTSSS PPDAPATPAT PASSDSRDSP RKIRAMIFSL TGSPPESETP PVLQQEQVIS
TAAPTAGRHP NIIQQVPHIN RIPPQPLRRL TAPQAPPASQ PEEPPVQQTV PVVKVELASA
PAPIVRDPQS TEPVPPAMPT LVENNHEATL ILPPNKTSDY TRWNAQDLIN WVRLLITNNV
DSTIAIMVRE EFDGETLACL VLDDDFRKEV PIPYGHYKKM KIYGTEVLNH YRTEKYQADL
RKFHEELAAW KAQQR
