R111C_XENLA
ID R111C_XENLA Reviewed; 967 AA.
AC Q66J97;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=E3 ubiquitin-protein ligase arkadia-C;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 111-C;
DE AltName: Full=RING-type E3 ubiquitin transferase arkadia-C {ECO:0000305};
GN Name=rnf111-c;
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].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase required for mesoderm patterning
CC during embryonic development (By similarity). Acts as an enhancer of
CC the transcriptional responses of the smad2/smad3 effectors, which are
CC activated downstream of BMP. Acts by mediating ubiquitination and
CC degradation of SMAD inhibitors such as smad7, inducing their
CC proteasomal degradation and thereby enhancing the transcriptional
CC activity of TGF-beta and BMP. Specifically binds polysumoylated chains
CC via SUMO interaction motifs (SIMs) and mediates ubiquitination of
CC sumoylated substrates (By similarity). The regulation of the BMP-SMAD
CC signaling is however independent of sumoylation and is not dependent of
CC SUMO interaction motifs (SIMs) (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZNA4, ECO:0000250|UniProtKB:Q99ML9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q6ZNA4};
CC -!- ACTIVITY REGULATION: Binds free ubiquitin non-covalently via its RING-
CC type zinc finger. Ubiquitin-binding leads to enhance the E3 ubiquitin-
CC protein ligase activity by stabilizing the ubiquitin-conjugating enzyme
CC E2 (donor ubiquitin) in the 'closed' conformation and activating
CC ubiquitin transfer. {ECO:0000250|UniProtKB:Q6ZSG1}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q6ZNA4}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6ZNA4,
CC ECO:0000250|UniProtKB:Q99ML9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6ZNA4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q6ZNA4}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:Q99ML9}. Note=Upon TGF-beta treatment,
CC translocates from nucleus to cytosol. {ECO:0000250|UniProtKB:Q6ZNA4}.
CC -!- DOMAIN: The SUMO interaction motifs (SIMs) mediates the binding to
CC polysumoylated substrate. {ECO:0000250|UniProtKB:Q6ZNA4}.
CC -!- DOMAIN: The RING-type zinc finger mediates the E3 ubiquitin-protein
CC ligase activity and binds directly to free ubiquitin (By similarity).
CC Non-covalent ubiquitin-binding stabilizes the ubiquitin-conjugating
CC enzyme E2 (donor ubiquitin) in the 'closed' conformation and stimulates
CC ubiquitin transfer (By similarity). {ECO:0000250|UniProtKB:Q6ZNA4,
CC ECO:0000250|UniProtKB:Q6ZSG1}.
CC -!- SIMILARITY: Belongs to the Arkadia family. {ECO:0000305}.
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DR EMBL; BC081009; AAH81009.1; -; mRNA.
DR RefSeq; NP_001087624.1; NM_001094155.1.
DR AlphaFoldDB; Q66J97; -.
DR SMR; Q66J97; -.
DR DNASU; 447448; -.
DR GeneID; 447448; -.
DR KEGG; xla:447448; -.
DR CTD; 447448; -.
DR Xenbase; XB-GENE-854138; rnf111.L.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 447448; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR029306; RNF111_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF15303; RNF111_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; DNA damage; DNA repair; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..967
FT /note="E3 ubiquitin-protein ligase arkadia-C"
FT /id="PRO_0000280695"
FT ZN_FING 915..956
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 57..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..882
FT /note="Ubiquitin binding"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT REGION 930..934
FT /note="Ubiquitin binding"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT MOTIF 280..284
FT /note="SUMO interaction motif 1 (SIM)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT MOTIF 305..311
FT /note="SUMO interaction motif 2 (SIM)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT MOTIF 360..364
FT /note="SUMO interaction motif 3 (SIM)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT COMPBIAS 78..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..499
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..657
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..687
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 915
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT BINDING 918
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT BINDING 938
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT BINDING 941
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
SQ SEQUENCE 967 AA; 106177 MW; 849FCADD67EFBBDB CRC64;
MKSEVSSDAP KRQENLKGVL LNPEAIGASK SFPGEVEMIT SKVSNEFSHL CSDTNKQQID
LNSDGTEQEK NLVVHKKRKS QQAGTSYAQS CEVKENQRLL RLQPQSDEDN DSSFSDCISS
PSSSSHFGDS DTMTSDEDKD NPRRYSPAGI NSTPRTQSAR AQKWPRPHTD SVSSLVMKRP
CYQVSSLRRP LHRKRFVKNV SSQRTQKQKE RIMLQRKKRE VLARQKYALL PSSSSSSEND
LSSESSSSSS TEGEEDLFVS PGENHQDGTT LPSGGMDEDV VVIEASSTPQ VTANEEINVT
STDSEVEIVT VGETYRSRAT LGHPRSHWGQ NSQSGRTQEH RTRNRVSTII QPLRQNTTEV
VDLTVDEDDP TVVPTTSGRV ESQPVSTVSS NTSTSEPASD SVSGLLGSRG CAVSETPAIP
PNSNTVGTIA DDSRTSTSGT NADGGPPAMP RLPSCCPQHS PCGGSSQNHV LGHPHSSCFQ
PHSHHFPHHH HHHHHHSSHP GVPLSPSFRD SHCPVERNAA VPPPCGATSG SGSTYHDPQA
LPVDLSNNGI RNHGSVSFHS TSAFDPCCPG SSSRSTVYGH QSTTSNAQTM AIDGYGSSMV
AQAQPQTPSP LSSCRHYMHA SYTSLTRPLH HQTSACPHSN PASQPPPPPP PPPMDYVIAH
QVPFISPLPS LTSTHAVPPP PPSHHLSTAA APLPQHLSTS HQSMSHHISA TAPATQRLHA
HEVIQRMEVQ RRRMMQHPTR AHERPPPHPH RMHPNYGHGH HIHVPQTMSS HPRQGPERSA
WEIAIETGVT AAPYQTGPLH THLAHYHPPP RLHHLQIGAL PLMVPDMAGY PHIRYISSGL
DGRSFRVPFR GNFEELIHLE ERLGNVNRGA SQGTIERCTY PHKYKKVSTD WFSQRKLHSK
QDGEEAPEED TEEKCTICLS ILEEGEDVRR LPCMHLFHQV CVDQWLITNK KCPICRVDID
TQLPTES
