RN126_BOVIN
ID RN126_BOVIN Reviewed; 313 AA.
AC Q0II22;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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. May also play a role in the endosomal
CC recycling of IGF2R, the cation-independent mannose-6-phosphate
CC receptor. May play a role in the endosomal sorting and degradation of
CC several membrane receptors including EGFR, FLT3, MET and CXCR4, by
CC mediating their ubiquitination. By ubiquitinating CDKN1A/p21 and
CC targeting it for degradation, may also promote cell proliferation. May
CC monoubiquitinate AICDA. {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 -!- SUBUNIT: Interacts with CCDC50, EGFR, FLT3 and SCAMP3. Interacts with
CC BAG6 (via ubiquitin-like domain); required for BAG6-dependent
CC ubiquitination of proteins mislocalized to the cytosol. Interacts with
CC CDKN1A. Interacts with AICDA. {ECO:0000250|UniProtKB:Q9BV68}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BV68}. Nucleus
CC {ECO:0000250|UniProtKB:Q9BV68}.
CC -!- DOMAIN: The C4-type zinc finger is required for interaction with BAG6.
CC {ECO:0000250|UniProtKB:Q9BV68}.
CC -!- PTM: Ubiquitinated. May undergo autoubiquitination.
CC {ECO:0000250|UniProtKB:Q9BV68}.
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DR EMBL; BC122844; AAI22845.1; -; mRNA.
DR RefSeq; NP_001068782.1; NM_001075314.1.
DR AlphaFoldDB; Q0II22; -.
DR SMR; Q0II22; -.
DR STRING; 9913.ENSBTAP00000019080; -.
DR PaxDb; Q0II22; -.
DR Ensembl; ENSBTAT00000019080; ENSBTAP00000019080; ENSBTAG00000014349.
DR GeneID; 507447; -.
DR KEGG; bta:507447; -.
DR CTD; 55658; -.
DR VEuPathDB; HostDB:ENSBTAG00000014349; -.
DR VGNC; VGNC:34018; RNF126.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000157113; -.
DR HOGENOM; CLU_034892_0_0_1; -.
DR InParanoid; Q0II22; -.
DR OMA; MVPDPHC; -.
DR OrthoDB; 1249953at2759; -.
DR TreeFam; TF317985; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000014349; Expressed in digestive system secreted substance and 105 other tissues.
DR ExpressionAtlas; Q0II22; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
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:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; ISS:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; 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 Acetylation; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BV68"
FT CHAIN 2..313
FT /note="E3 ubiquitin-protein ligase RNF126"
FT /id="PRO_0000285084"
FT ZN_FING 13..32
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:Q9BV68"
FT ZN_FING 232..273
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 5..101
FT /note="Required for interaction with BAG6"
FT /evidence="ECO:0000250|UniProtKB:Q9BV68"
FT REGION 42..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..306
FT /note="Sufficient for interaction with AICDA"
FT /evidence="ECO:0000250|UniProtKB:Q9BV68"
FT REGION 280..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..123
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"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV68"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV68"
SQ SEQUENCE 313 AA; 33954 MW; 429687DF025D12D4 CRC64;
MAEASPQPGR YFCHCCSVEI VPRLPDYICP RCESGFIEEL PEETRSAENG SAPSTASADQ
SRQQPFENVD QPLFTLPQGY GHFAFGIFDD SFEIPTFPPG AQADDSRDPE SRREREQHSR
HRYGARQPRA RLTARRATGR HEGVPTLEGI IQQLVNGIIT PATIPNLGLG PWGVLHSNPM
DYAWGANGLD AIITQLLNQF ENTGPPPADK EKIQALPTVP VTEEHVGSGL ECPVCKDDYG
LGEHVRQLPC NHLFHDGCIV PWLEQHDSCP VCRKSLTGQN TATDPPGLAG VSFSSSSSSS
SSSPGNENPA SSS
