PCGF3_CAEEL
ID PCGF3_CAEEL Reviewed; 549 AA.
AC Q19336; D3YT24;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 4.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Polycomb group RING finger protein 3 homolog mig-32 {ECO:0000305};
DE AltName: Full=RING-domain-containing protein mig-32 {ECO:0000303|PubMed:19211678};
GN Name=mig-32 {ECO:0000312|WormBase:F11A10.3a};
GN ORFNames=F11A10.3 {ECO:0000312|WormBase:F11A10.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19211678; DOI=10.1242/dev.029363;
RA Karakuzu O., Wang D.P., Cameron S.;
RT "MIG-32 and SPAT-3A are PRC1 homologs that control neuronal migration in
RT Caenorhabditis elegans.";
RL Development 136:943-953(2009).
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, throughout development (By similarity).
CC Required for ubiquitination of histone H2A (PubMed:19211678). Plays a
CC role in the formation of the male-specific genital sensilla (simple
CC sense organs) known as rays (PubMed:19211678). Required for normal
CC migration of the hermaphrodite specific neurons (HSN) and for extension
CC of some neuronal processes (PubMed:19211678). Represses vulval fates in
CC hypodermal cells that do not normally contribute to vulval development
CC (PubMed:19211678). {ECO:0000250|UniProtKB:Q3KNV8,
CC ECO:0000269|PubMed:19211678}.
CC -!- SUBUNIT: Component of a PRC1-like complex.
CC {ECO:0000250|UniProtKB:Q3KNV8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19211678}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:19211678}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F11A10.3a};
CC IsoId=Q19336-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F11A10.3b};
CC IsoId=Q19336-2; Sequence=VSP_061240;
CC -!- DEVELOPMENTAL STAGE: Expression begins early in embryogenesis and
CC continues in larval development and into adulthood of males and
CC hermaphrodites. {ECO:0000269|PubMed:19211678}.
CC -!- DISRUPTION PHENOTYPE: Viable, but has defects in the male-specific
CC genital sensilla (simple sense organs) known as rays (PubMed:19211678).
CC Defects in the migration and axon extension of the hermaphrodite
CC specific neurons (HSN) during embryogenesis (PubMed:19211678).
CC Ubiquitin-modified histone H2A is not detected in mutants
CC (PubMed:19211678). RNAi-mediated knockdown in a lin-15 mutant
CC background causes a multiple vulva (Muv) phenotype (PubMed:19211678).
CC {ECO:0000269|PubMed:19211678}.
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DR EMBL; BX284604; CAA92594.4; -; Genomic_DNA.
DR EMBL; BX284604; CBK19423.1; -; Genomic_DNA.
DR RefSeq; NP_001255620.1; NM_001268691.1.
DR RefSeq; NP_001255621.1; NM_001268692.1.
DR AlphaFoldDB; Q19336; -.
DR SMR; Q19336; -.
DR IntAct; Q19336; 1.
DR STRING; 6239.F11A10.3a; -.
DR EPD; Q19336; -.
DR PaxDb; Q19336; -.
DR PeptideAtlas; Q19336; -.
DR EnsemblMetazoa; F11A10.3a.1; F11A10.3a.1; WBGene00008684. [Q19336-1]
DR EnsemblMetazoa; F11A10.3b.1; F11A10.3b.1; WBGene00008684. [Q19336-2]
DR GeneID; 178150; -.
DR KEGG; cel:CELE_F11A10.3; -.
DR UCSC; F11A10.3; c. elegans. [Q19336-1]
DR CTD; 178150; -.
DR WormBase; F11A10.3a; CE44973; WBGene00008684; mig-32.
DR WormBase; F11A10.3b; CE44701; WBGene00008684; mig-32.
DR eggNOG; KOG1040; Eukaryota.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000158395; -.
DR HOGENOM; CLU_020700_0_0_1; -.
DR InParanoid; Q19336; -.
DR OMA; RCYPLER; -.
DR OrthoDB; 1203951at2759; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00008684; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q19336; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0035102; C:PRC1 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033522; P:histone H2A ubiquitination; IMP:WormBase.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; IBA:GO_Central.
DR GO; GO:0040027; P:negative regulation of vulval development; IGI:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IMP:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
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 Alternative splicing; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..549
FT /note="Polycomb group RING finger protein 3 homolog mig-32"
FT /id="PRO_0000454045"
FT ZN_FING 329..368
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 206..260
FT /evidence="ECO:0000255"
FT COMPBIAS 13..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..509
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061240"
SQ SEQUENCE 549 AA; 63267 MW; 010FA1B1CE076FF8 CRC64;
MTRKRPALAE PVSSSRSRVT RRSTTGAPSS KKKRSPEPES DADSEDDYDG PSTSQTKKLK
RGNSSTNRGK AANKTKRGSF QVKQEIMDDD ENEEKIDGEV ENGITSREHS PDPSTFKKTA
KLQTKKKKKK ESPPETPPTS PSPSPSRSVS PSTTKSDISS KKGRKAVVNS VSKVKIEKES
TPVKTNGRNL PPKRKKKPVE EETAEEIKLR ERAERKARRI EEAKNRPKLT IEQKLAKLRK
KKERRERRKE QEKEESMRQK YGQRKIKAEA SKWNFGPISS INQRRRDEMM AYFPKANFLA
EDGVPKVMNN FRRATVKYNM EVLNPFITCG ICDGYIVDAT TIIDCMHTFC KSCLLTYFES
DNNTCPTCGT FIHGSHPTHY VTYDRAVNEL VNQFVPKMEN NELDVRKTFL RDCREALGID
TAAEDRERKE RLERERITGT NRCYPLERPR FSHHRDDCQV TVNLLPGTAN LPLITRPYVR
CSEMTTMNTL KKFLSLQIWD DQSRYSDLDM FCDGQLMGKD FSVRFVWMMK RRGQPKSEPL
IIRYHMTRT
