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   03-AUG-2022, entry version 94.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC075492; AAH75492.1; -; mRNA.
DR   RefSeq; NP_001006735.1; NM_001006734.1.
DR   AlphaFoldDB; Q6DIP3; -.
DR   SMR; Q6DIP3; -.
DR   DNASU; 448402; -.
DR   GeneID; 448402; -.
DR   KEGG; xtr:448402; -.
DR   CTD; 55658; -.
DR   Xenbase; XB-GENE-5960892; rnf126.
DR   InParanoid; Q6DIP3; -.
DR   OrthoDB; 1249953at2759; -.
DR   Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
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:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   CDD; cd16801; RING-H2_RNF126; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR039572; RNF126.
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:SF21; PTHR15710:SF21; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   Pfam; PF14369; zinc_ribbon_9; 1.
DR   SMART; SM00184; RING; 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