R146A_BOVIN
ID R146A_BOVIN Reviewed; 346 AA.
AC E1B7X3;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=E3 ubiquitin-protein ligase RNF146-A;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 146-A;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF146-A {ECO:0000305};
GN Name=RNF146A;
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 GENOMIC DNA].
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that specifically binds poly-ADP-
CC ribosylated proteins and mediates their ubiquitination and subsequent
CC degradation. Acts as an activator of the Wnt signaling pathway by
CC mediating the ubiquitination of poly-ADP-ribosylated AXIN1 and AXIN2, 2
CC key components of the beta-catenin destruction complex. Acts in
CC cooperation with tankyrase proteins (TNKS and TNKS2), which mediate
CC poly-ADP-ribosylation of target proteins AXIN1, AXIN2, BLZF1, CASC3,
CC TNKS and TNKS2. Recognizes and binds tankyrase-dependent poly-ADP-
CC ribosylated proteins via its WWE domain and mediates their
CC ubiquitination (By similarity). {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 -!- SUBUNIT: Interacts with poly-ADP-ribosylated AXIN1, AXIN2, BLZF1 and
CC CASC3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC -!- DOMAIN: The WWE domain mediates non-covalent poly(ADP-ribose)-binding.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated; autoubiquitinated. Autoubiquitination is enhanced
CC upon poly(ADP-ribose)-binding (By similarity). {ECO:0000250}.
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DR EMBL; AAFC03114389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1B7X3; -.
DR BMRB; E1B7X3; -.
DR SMR; E1B7X3; -.
DR STRING; 9913.ENSBTAP00000047470; -.
DR PaxDb; E1B7X3; -.
DR PRIDE; E1B7X3; -.
DR eggNOG; KOG0824; Eukaryota.
DR HOGENOM; CLU_067425_0_0_1; -.
DR InParanoid; E1B7X3; -.
DR TreeFam; TF318925; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..346
FT /note="E3 ubiquitin-protein ligase RNF146-A"
FT /id="PRO_0000409502"
FT DOMAIN 91..167
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT ZN_FING 37..75
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 195..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 346 AA; 37543 MW; 62DFEAF6DBFFB9BF CRC64;
MMAGCGETDH SINMLPTNRK ANESCSNTAP SLTVPECAIC LQTCVHPVSL PCKHVFCYLC
VKGASWLGKR CALCRQEIPE DFLDRPTLLS PELKAASRGN GEYAWYYEGR NGWWQYDERT
SRELEDAFSK GKKSTEMLIA GFLYVADLEN MVQYRRNEHG RRRKIKRDII DIPKKGVAGL
RLDCDANTVN LARESSADGA DSVPAQSGAS VQSSSVRPLT SVDGQLTSPA TPSPDVGTSL
EDSFAHLQLG GDSIAERSHR GEGEEEHESP SSGRVPAPDT SIEETESDAS SDSEDVSALV
AQHSLTQQRL LVPNPSQTVS DRSVAAGGIV SVRSRRPDGQ CTVTEV
