ID   R126A_XENLA             Reviewed;         312 AA.
AC   Q7T0Q3;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF126-A {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9BV68};
DE   AltName: Full=RING finger protein 126-A {ECO:0000305};
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF126-A {ECO:0000305};
GN   Name=rnf126-a {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=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2003) 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; BC056088; AAH56088.1; -; mRNA.
DR   RefSeq; NP_001079878.1; NM_001086409.1.
DR   AlphaFoldDB; Q7T0Q3; -.
DR   SMR; Q7T0Q3; -.
DR   DNASU; 379568; -.
DR   GeneID; 379568; -.
DR   KEGG; xla:379568; -.
DR   CTD; 379568; -.
DR   Xenbase; XB-GENE-6255465; rnf126.L.
DR   OrthoDB; 1249953at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 379568; 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-A"
FT                   /id="PRO_0000056095"
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          40..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..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;  34099 MW;  DB5FDA2CF17CEBEA CRC64;
     MAEALPKAGR YFCHSCTAEI TPRLPEYTCP RCDSGFIEEL PETSRNSENN SSNNSRTDQN
     RPSFENLESA QFTLPSGYGQ VTFGIFNEGL DFPIFGTSGP VEETRDGESR REHQSRQRYG
     ARQPRARLST RRAAGRNEGV PTLEGIIQQL VNGIIAPTAM SNLGVGPWGV LHSNPMDYAW
     GANGLDTIIT QLLNQFENTG PPPADNEKIQ ALPTIQITEE HVGSGLECPV CKEDYTVGEC
     VRQLPCNHLF HNDCIIPWLE QHDTCPVCRK SLSGQNTATN PPGLSEMTFS SSSTSSSSST
     SPTDENNSAN NS