RN111_XENTR
ID RN111_XENTR Reviewed; 954 AA.
AC Q0V9R0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=E3 ubiquitin-protein ligase arkadia;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 111;
DE AltName: Full=RING-type E3 ubiquitin transferase arkadia {ECO:0000305};
GN Name=rnf111;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) 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; BC121428; AAI21429.1; -; mRNA.
DR RefSeq; NP_001072805.1; NM_001079337.1.
DR RefSeq; XP_012826020.1; XM_012970566.2.
DR RefSeq; XP_012826021.1; XM_012970567.2.
DR RefSeq; XP_012826022.1; XM_012970568.1.
DR AlphaFoldDB; Q0V9R0; -.
DR SMR; Q0V9R0; -.
DR PaxDb; Q0V9R0; -.
DR GeneID; 780266; -.
DR KEGG; xtr:780266; -.
DR CTD; 54778; -.
DR Xenbase; XB-GENE-854131; rnf111.
DR eggNOG; KOG0800; Eukaryota.
DR InParanoid; Q0V9R0; -.
DR OrthoDB; 1098052at2759; -.
DR Reactome; R-XTR-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000010842; Expressed in blastula and 12 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046332; F:SMAD binding; IBA:GO_Central.
DR GO; GO:0032184; F:SUMO polymer binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0055113; P:epiboly involved in gastrulation with mouth forming second; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0021501; P:prechordal plate formation; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0030579; P:ubiquitin-dependent SMAD protein catabolic process; IBA:GO_Central.
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..954
FT /note="E3 ubiquitin-protein ligase arkadia"
FT /id="PRO_0000280696"
FT ZN_FING 902..943
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 50..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 318..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..869
FT /note="Ubiquitin binding"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT REGION 917..921
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 50..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 150..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..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 902
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT BINDING 905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT BINDING 925
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT BINDING 928
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
SQ SEQUENCE 954 AA; 104889 MW; E00D10121434A69B CRC64;
MKSEVSSDAP KRQENLKGVL LNPEAIGASK SFPKEVEMIA SKVSNEFSHL CSDTNKQQRD
LNSNGTEQEK NLVVHKKRKN QQAGTSYAQS CEVKENQRLL RLQPQSDEDN DSSFSDCISS
PSSSSHFGDS DTMTSDEDKD NPRRYSPAGV NATPRTQSAR AQKWPRPHTD SVSSLVMKRP
CYQVSSLRRP LHRKRFVKNV SSQRTQKQKE RMMLQRKKRE VLARQKYALL PSSSSSSEND
LSSESSSSSS TEGEEDLFVS PGENHQDGTT LPSGGMDEDV VVIEASSTPQ VTANEEINVT
STDSEVEIVT VGETYRSRTT LGHPRSHWGQ NTQSGRTQEQ RTRNRVSTVI QPLRQNTTEV
VDLTVDEDDP TVVPTTSGRV ESQPVSTVSS NTSTSEPASD SASGPLGSRG SAIPEIPPIP
PNSNTVGTIA DDSRTSTSGT NVDGGPPAMP RLPSCCPQHS PCGGSSQNHV LGHPHSSCFP
PHSHHFPHHH HHHHQSSHPG VPLSPSFRDS HCPVERNAAV PPPCGATSSS GSTYHDPQAL
PVDLSNNGIR SHGSVSFHST SAFDPCCPGS SSRSTVYGHQ STTSTAQTMA IDGYGSSMVA
QAQPPPPTPL SSCRHYMHAP YTSLTRPLHH QTSSCPHSHS NVGDYVIAHQ VPFISPLPSL
AATHAVPPPP PSHHLSTAAA PQHLSTSHQS MSHHISATAP ATQRLHTHEV IQRMEVQRRR
MMQHPTRAHE RPPPHPHRMH PNYGHGHHIH VPQTMSSHPR QGPERSAWEI AIETGVTAAP
YQTGPLHTHL AHYHAPPRLH HLQIGALPLM VPDMAGYPHI RYISSGLDGR SFRVPFRGNF
EELIHLEERL GNVNRGASQG TIERCTYPHK YEKVSTDWFS QRKLHSKQDG EEATEEDTEE
KCTICLSILE EGEDVRRLPC MHLFHQVCVD QWLITNKKCP ICRVDIDTQL PTES
