RN146_XENLA
ID RN146_XENLA Reviewed; 314 AA.
AC Q6GQD5;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=E3 ubiquitin-protein ligase rnf146;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 146;
DE AltName: Full=RING-type E3 ubiquitin transferase rnf146 {ECO:0000305};
GN Name=rnf146;
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that specifically binds poly-ADP-
CC ribosylated proteins and mediates their ubiquitination and subsequent
CC degradation. May regulate many important biological processes, such as
CC cell survival and DNA damage response. Acts as an activator of the Wnt
CC signaling pathway by mediating the ubiquitination of poly-ADP-
CC ribosylated proteins. Neuroprotective protein. Protects against cell
CC death induced by DNA damaging agents and rescues cells from G1 arrest.
CC Promotes cell survival after gamma-irradiation. Facilitates DNA repair.
CC {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=Translocates to the nucleus after DNA damage.
CC {ECO:0000250}.
CC -!- DOMAIN: The WWE domain mediates non-covalent poly(ADP-ribose)-binding.
CC {ECO:0000250}.
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DR EMBL; BC072810; AAH72810.1; -; mRNA.
DR RefSeq; NP_001085469.1; NM_001092000.1.
DR AlphaFoldDB; Q6GQD5; -.
DR SMR; Q6GQD5; -.
DR BioGRID; 102058; 1.
DR IntAct; Q6GQD5; 1.
DR MaxQB; Q6GQD5; -.
DR DNASU; 443895; -.
DR GeneID; 443895; -.
DR KEGG; xla:443895; -.
DR CTD; 443895; -.
DR Xenbase; XB-GENE-974784; rnf146.S.
DR OrthoDB; 1469576at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 443895; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0072572; F:poly-ADP-D-ribose binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd16546; RING-HC_RNF146; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR InterPro; IPR044110; RING-HC_RNF146.
DR InterPro; IPR033509; RNF146.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13417:SF2; PTHR13417:SF2; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF117839; SSF117839; 1.
DR PROSITE; PS50918; WWE; 1.
DR PROSITE; PS00518; ZF_RING_1; 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; Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..314
FT /note="E3 ubiquitin-protein ligase rnf146"
FT /id="PRO_0000409507"
FT DOMAIN 91..167
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT ZN_FING 36..74
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 281..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
SQ SEQUENCE 314 AA; 34771 MW; 3FAF256C14E0F227 CRC64;
MAGCGEVSHS ANMLPTNKKL DEPCSNNAPS LSVPECAICL QICVHPVSLP CKHIFCYLCV
KGASWLGRRC ALCRQEIPED FLDKPTLLSP EDLKSASRGN GEYAWYYEGR NGWWQYDERT
SRELEDAFTK GKKSTEMLIA GFLYVADLEN MVQYRRNEHG RRRKIKRDIV DIPKKGVAGL
RLECDAANLN LARESSADGA DSMAALGDSS SQPAHVLPAR LHTSLSTTTS QVLSHSDVTT
SLENSFTQLQ IGDPVINRNY IGEEGRPLII ARMQATNAVL EEQEPSDRND HGSPALQHNS
FLVPQSNRLP FGNP
