ID RN126_XENTR Reviewed; 311 AA.
AC Q6DIP3;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=E3 ubiquitin-protein ligase RNF126 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9BV68};
DE AltName: Full=RING finger protein 126 {ECO:0000305};
GN Name=rnf126 {ECO:0000305};
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination oF
CC target proteins. Depending on the associated E2 ligase, mediates 'Lys-
CC 48'- and 'Lys-63'-linked polyubiquitination of substrates. Part of a
CC BAG6-dependent quality control process ensuring that proteins of the
CC secretory pathway that are mislocalized to the cytosol are degraded by
CC the proteasome. Probably acts by providing the ubiquitin ligase
CC activity associated with the BAG6 complex and be responsible for
CC ubiquitination of the hydrophobic mislocalized proteins and their
CC targeting to the proteasome. {ECO:0000250|UniProtKB:Q91YL2,
CC ECO:0000250|UniProtKB:Q9BV68}.
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:Q9BV68};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9BV68}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BV68}. Nucleus
CC {ECO:0000250|UniProtKB:Q9BV68}.
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DR EMBL; BC075492; AAH75492.1; -; mRNA.
DR RefSeq; NP_001006735.1; NM_001006734.1.
DR AlphaFoldDB; Q6DIP3; -.
DR SMR; Q6DIP3; -.
DR STRING; 8364.ENSXETP00000032349; -.
DR DNASU; 448402; -.
DR GeneID; 448402; -.
DR KEGG; xtr:448402; -.
DR AGR; Xenbase:XB-GENE-5960892; -.
DR CTD; 55658; -.
DR Xenbase; XB-GENE-5960892; rnf126.
DR InParanoid; Q6DIP3; -.
DR OMA; DERSADN; -.
DR OrthoDB; 5474929at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd16801; RING-H2_RNF126; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR039571; RNF126_RING-H2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF21; E3 UBIQUITIN-PROTEIN LIGASE RNF126; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..311
FT /note="E3 ubiquitin-protein ligase RNF126"
FT /id="PRO_0000056097"
FT ZN_FING 13..32
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:Q9BV68"
FT ZN_FING 227..268
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 42..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9BV68"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9BV68"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9BV68"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9BV68"
SQ SEQUENCE 311 AA; 33890 MW; AAD264550ED65972 CRC64;
MAEALPEAGR YFCHSCTAEI IPRLPEYTCP RCDSGFIEEL PETRNSENNS SNNSGTDQNR
PSFENLESAQ FTLPSGYGQV TFGIFNEGLD FPIFGTSGPV EEPRDGESRR EHQSRQRYGA
RQPRARLSTR RAAGRNEGVP TLEGIIQQLV NGIIAPTAMS NLGVGPWGVL HSNPMDYAWG
ANGLDTIITQ LLNQFENTGP PPADTEKIQA LPTIQITEEH VGSGLECPVC KEDYTVGESV
RQLPCNHLFH NDCIIPWLEQ HDTCPVCRKS LSGQNTATNP PGLTEMTFSS SSTSSSSSTS
PTDENNAANN S
//
