R111B_XENLA
ID R111B_XENLA Reviewed; 959 AA.
AC Q6NRV8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=E3 ubiquitin-protein ligase arkadia-B;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 111-B;
DE AltName: Full=RING-type E3 ubiquitin transferase arkadia-B {ECO:0000305};
GN Name=rnf111-b;
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 (MAY-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; BC070603; AAH70603.1; -; mRNA.
DR RefSeq; NP_001090211.1; NM_001096742.1.
DR AlphaFoldDB; Q6NRV8; -.
DR SMR; Q6NRV8; -.
DR DNASU; 779113; -.
DR GeneID; 779113; -.
DR KEGG; xla:779113; -.
DR CTD; 779113; -.
DR Xenbase; XB-GENE-6251809; rnf111.S.
DR OrthoDB; 1570520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 779113; Expressed in blastula 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..959
FT /note="E3 ubiquitin-protein ligase arkadia-B"
FT /id="PRO_0000280694"
FT ZN_FING 907..948
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 51..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..874
FT /note="Ubiquitin binding"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT REGION 922..926
FT /note="Ubiquitin binding"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT MOTIF 275..279
FT /note="SUMO interaction motif 1 (SIM)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT MOTIF 300..306
FT /note="SUMO interaction motif 2 (SIM)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT MOTIF 355..359
FT /note="SUMO interaction motif 3 (SIM)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT COMPBIAS 51..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..649
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..679
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT BINDING 910
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT BINDING 930
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT BINDING 933
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
SQ SEQUENCE 959 AA; 105433 MW; D86BF2545F7CEFF0 CRC64;
MKSEVSSDAP KRQENFKGVL LNPETIGASK SFPKEVEMIA SKVSNEFNHL CSDTNKQQSD
LNSNGTEQDK SLVVHKKRKS QQAGTSYAQS CEVKEYQRLL RLQPKSDEDN DSSFSDCISS
PSSSSHFGDS DTMTSDEDKD NPLSSVNSTP RTQSARAQKW PRPHTDSVSS LLMKRPCYQV
SSLRRPLHRK RFVKNVSSQR TQKQKERMML QRKKREVLAR QKYALLPSSS SSSENDLSSE
SSSSSSTEGE DLFVSTGENR QDGTTLPSGG MDEDVVVIEA SSTPQVTANE EINVTSTDSE
VEIVTVGETY RSRATLRHPR SHWGQNSQSG RTQEQRTRNR VSTVIQPLRQ NTTEVVDLTV
DEDDPTVVQT TSGRVESQPV SIVSSLTSTS EPASDSMSGL MGSAVPEIPA IPPNTVGTIA
DDSRTCTSGA NADGGPPAMP RLPSCCPQHS PCGGSSQNHV LGHPHSSCFP PHSHHFPHHH
HHHHHSSHPG VPLSPSFRDS HCTVERNAAV PPPCGVSSSS GSTYHDPQAL PVDLSNNGIR
SHGSVGFHST SAFDPCCPGS SSRSTVYGHQ ATTSTAQTMA IDGYGSSMVA QAQPPPPTPL
SSCRHYMHAS YTSLPRPLHH QTSSCPHSNS ASQPPPPPPP PPPPPMDYVI AHQVPFISPL
PSLTSTHAVP PPPPSHHLSA AAAPLPQHLS TSHQSMSHHI SATAPVTQRL HAHEVIQRME
VQRRRMMQHP TRAHERPPPH PHRMHPNYGH GHHIHVPQTM SSHPRQGPER SAWEIAIETG
VTAATYQTGP LHTHLAHYHP PPRLHHLQIG ALPLMVPDMA GYPHIRYISS GLDGRSFRVP
FRGNFEELIH LEERLGNVNR GASQGTIERC TYPHKYKKVS TDWFSQRKLH SKQDGEEATE
EDTEEKCTIC LSILEEGEDV RRLPCMHLFH QVCVDQWLIT NKKCPICRVD IDTQLPTES
