ID   RN220_BOVIN             Reviewed;         566 AA.
AC   Q08DV5; Q0V8F6;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF220;
DE            EC=2.3.2.27;
DE   AltName: Full=RING finger protein 220;
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF220 {ECO:0000305};
GN   Name=RNF220;
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=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-566.
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination
CC       and proteasomal degradation of SIN3B (By similarity). Independently of
CC       its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7-
CC       mediated deubiquitination of CTNNB1 promoting Wnt signaling (By
CC       similarity). {ECO:0000250|UniProtKB:Q5VTB9,
CC       ECO:0000250|UniProtKB:Q6PDX6}.
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 SIN3B (By similarity). Interacts with CTNNB1
CC       (via Armadillo repeats 2-8) (By similarity). Interacts with USP7 (via
CC       MATH domain) (By similarity). {ECO:0000250|UniProtKB:Q5VTB9,
CC       ECO:0000250|UniProtKB:Q6PDX6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Auto-ubiquitinated; leads to proteasomal degradation.
CC       {ECO:0000250}.
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DR   EMBL; BC123549; AAI23550.1; -; mRNA.
DR   EMBL; BT026262; ABG67101.1; -; mRNA.
DR   RefSeq; NP_001070409.1; NM_001076941.2.
DR   AlphaFoldDB; Q08DV5; -.
DR   SMR; Q08DV5; -.
DR   STRING; 9913.ENSBTAP00000016395; -.
DR   PaxDb; Q08DV5; -.
DR   GeneID; 616005; -.
DR   KEGG; bta:616005; -.
DR   CTD; 55182; -.
DR   eggNOG; ENOG502QR1N; Eukaryota.
DR   InParanoid; Q08DV5; -.
DR   OrthoDB; 1583675at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
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:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   CDD; cd16563; RING-HC_RNF220; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR031824; RNF220_mid.
DR   InterPro; IPR040178; RNF220_RING.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF15926; RNF220; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Isopeptide bond; Metal-binding; Phosphoprotein;
KW   Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..566
FT                   /note="E3 ubiquitin-protein ligase RNF220"
FT                   /id="PRO_0000277656"
FT   ZN_FING         514..553
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          277..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..522
FT                   /note="Required for targeting to the cytoplasm"
FT                   /evidence="ECO:0000250"
FT   COILED          485..513
FT                   /evidence="ECO:0000255"
FT   MOD_RES         390
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VTB9"
FT   CROSSLNK        277
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VTB9"
FT   CONFLICT        553
FT                   /note="Y -> N (in Ref. 2; ABG67101)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   566 AA;  62729 MW;  0460900108DDFDCD CRC64;
     MDLHRAAFKM ENSSYLPNPL ASPALMVLAS TAEASRDASI PCQQPRPFGV PVSVDKDVHI
     PFTNGSYTFA SMYHRQGGVP GTFANRDFPP SLLHLHPQFA PPNLDCTPIS MLNHSGVGAF
     RPFASTEDRE SYQSAFTPAK RLKNCHDTES PHLRFSDADG KEYDFGTQLP SSSPGSLKVD
     DTGKKIFAVS GLISDREASS SPEDRNDRCK KKAAALFDSQ APICPICQVL LRPSELQEHM
     EQELEQLAQL PASKNSLLKD AMAPGTPKSL LLSASIKREG ESPTASPHSS ATDDLHHSDR
     YQTFLRVRAN RQTRLNARIG KMKRRKQDEG QREGSCMAED DAADIEHENS NRFEEYEWCG
     QKRIRATTLL EGGFRGSGFV MCSGKENPDS DADLDVDGDD TLEYGKPQYT EADVIPCTGE
     EPGEAKEREA LRGAVLNGGP PSTRITPEFS KWASDEMPST SNGESSKQEA MQKTCKNSDI
     EKITEDSAVT TFEALKARVR ELERQLSRGD RYKCLICMDS YSMPLTSIQC WHVHCEECWL
     RTLGAKKLCP QCYTITAPGD LRRIYL