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Database: UniProt
Entry: A0A3Q1EUY0_9TELE
LinkDB: A0A3Q1EUY0_9TELE
Original site: A0A3Q1EUY0_9TELE 
ID   A0A3Q1EUY0_9TELE        Unreviewed;       615 AA.
AC   A0A3Q1EUY0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   18-JUN-2025, entry version 28.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF220 {ECO:0000256|ARBA:ARBA00067773};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=RING finger protein 220 {ECO:0000256|ARBA:ARBA00083046};
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF220 {ECO:0000256|ARBA:ARBA00079756};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000007854.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000007854.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
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:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBUNIT: Interacts with SIN3B. Interacts with CTNNB1 (via Armadillo
CC       repeats 2-8). Interacts with USP7 (via MATH domain).
CC       {ECO:0000256|ARBA:ARBA00063526}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   RefSeq; XP_022060795.1; XM_022205103.2.
DR   AlphaFoldDB; A0A3Q1EUY0; -.
DR   Ensembl; ENSAPOT00000004234.1; ENSAPOP00000007854.1; ENSAPOG00000009927.1.
DR   GeneID; 110958524; -.
DR   GeneTree; ENSGT00390000016573; -.
DR   Proteomes; UP000257200; Unplaced.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR   CDD; cd16563; RING-HC_RNF220; 1.
DR   FunFam; 3.30.40.10:FF:000195; E3 ubiquitin-protein ligase RNF220; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR052443; E3_ubiq-ligase_RNF220-like.
DR   InterPro; IPR031824; RNF220_mid.
DR   InterPro; IPR040178; RNF220_RING.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13459; E3 UBIQUITIN-PROTEIN LIGASE RNF220 ISOFORM X1; 1.
DR   PANTHER; PTHR13459:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNF220 ISOFORM X1; 1.
DR   Pfam; PF15926; RNF220; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          563..602
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          490..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..520
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  67134 MW;  D314D91396210C9F CRC64;
     MDLHRAAFKM ESSSYLPNPL ASPALMVLAS TAEASRDASI PCQQPRPFGV PVSVEKDVHL
     PFNNGSYTFA SMYHRQGAVP PGFPNRDFPP SLLHLHHQFA PPNLDCSPIS MLNHSGVGAF
     RPFASPPEDR DGAPGGYQSA FTPAKRLKGC LDAEASPHLR YSDAEGKEYD FGGAQIPPGG
     SPSSALKAVE DSGKKIFAVS GLLSDRETSS SPEDRIERCK KKMSLYDSQA PVCPICQVLL
     RPGELQEHME TEIERLANIC LSKNTSPKDS AATPGTPKSM LLSVHIKREG ESPVVSPLSS
     EDAHHSDRYQ TFLRVRANRQ TRLNARIGKM KRRKPEDGGQ VCPLCSAPLA GSEEEMSRHV
     EQCLIQREGA LGDDDSADMD GENGRGFEEY EWAGQKRIRA TALLEGGFRG TGFATCSIKE
     SAADSDADLD VDGDDTLEYG KAQYTEADII PCSGAGEDQG EAREREALRG AVLNGGMPSN
     RITPEFSKWA SDEMPSTSNG ESSKTDPSTP SSSSSSCCVP RTCKNSEIEK VTEEESTATT
     MEALKARIRE LEKQILRGDR YKCLICMDSY TMPLTSIQCW HVHCEECWLR TLGNKKLCPQ
     CNTITSPGDL RRVYL
//
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