ID   R126B_XENLA             Reviewed;         312 AA.
AC   Q6IRP0;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF126-B {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9BV68};
DE   AltName: Full=RING finger protein 126-B {ECO:0000305};
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF126-B {ECO:0000305};
GN   Name=rnf126-b {ECO:0000305};
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 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; BC070697; AAH70697.1; -; mRNA.
DR   RefSeq; NP_001084974.1; NM_001091505.1.
DR   AlphaFoldDB; Q6IRP0; -.
DR   SMR; Q6IRP0; -.
DR   DNASU; 432033; -.
DR   GeneID; 432033; -.
DR   KEGG; xla:432033; -.
DR   CTD; 432033; -.
DR   Xenbase; XB-GENE-5960942; rnf126.S.
DR   OMA; MVPDPHC; -.
DR   OrthoDB; 1249953at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 432033; Expressed in egg cell and 19 other tissues.
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..312
FT                   /note="E3 ubiquitin-protein ligase RNF126-B"
FT                   /id="PRO_0000056096"
FT   ZN_FING         13..32
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV68"
FT   ZN_FING         228..269
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          41..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..119
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   312 AA;  34026 MW;  89E0B2557CEC15A2 CRC64;
     MAEALPEAGR YFCHSCTAEI TPRLPEYTCP RCDSGFIEEL PETSRNSESN SSNNSGTDQN
     RPSFENIESA QFTLPSGYGQ VTFGIFNEGL DFPMFGTSGP VEETRDGESR REHQSRQRYG
     ARQPRARMST RRGAGRNEGV PTLEGIIQQL VNGIIAPTAM SNLGVGPWGV LHSNPMDYAW
     GANGLDTIIT QLLNQFENTG PPPADTDKIQ ALPTIQITEE HVGFGLECPV CKEDYTVGES
     VRQLPCNHLF HNDCIIPWLE QHDTCPVCRK SLSGQNTATN PPGLTDMTFS SSSTSSSSST
     SPTDENNTAN NS