ID   RN166_XENLA             Reviewed;         241 AA.
AC   Q3KPU8;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF166;
DE            EC=2.3.2.27;
DE   AltName: Full=RING finger protein 166;
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF166;
GN   Name=rnf166;
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=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination
CC       of different substrates. {ECO:0000250|UniProtKB:Q96A37}.
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:Q96A37};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q96A37}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96A37}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC106547; AAI06548.1; -; mRNA.
DR   RefSeq; NP_001089778.1; NM_001096309.1.
DR   AlphaFoldDB; Q3KPU8; -.
DR   SMR; Q3KPU8; -.
DR   DNASU; 734843; -.
DR   GeneID; 734843; -.
DR   KEGG; xla:734843; -.
DR   CTD; 734843; -.
DR   Xenbase; XB-GENE-17341062; rnf166.L.
DR   OrthoDB; 1097558at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 734843; Expressed in testis and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR008598; Di19_Zn-bd.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR034734; ZF_C2HC_RNF.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF05605; zf-Di19; 1.
DR   Pfam; PF18574; zf_C2HC_14; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS51803; ZF_C2HC_RNF; 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; Reference proteome; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..241
FT                   /note="E3 ubiquitin-protein ligase RNF166"
FT                   /id="PRO_0000245592"
FT   DOMAIN          225..241
FT                   /note="UIM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   ZN_FING         37..77
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         102..121
FT                   /note="C2HC RNF-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT   REGION          8..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
SQ   SEQUENCE   241 AA;  26774 MW;  E79EAB6330E4DBAA CRC64;
     MAMFRNLVAS SQHRQHHSHQ SLATPSSADS LETQFGCPIC LEVYYKPVAI GSCGHTFCGE
     CLQPCLQVSS PLCPLCRMPF DPKKVDKASN VDKQLSSYKA PCRGCSKKVT LAKMRAHISS
     CPKVQEQMAN CPKFVPVLPT SQPIPSNIPN RSTFVCPYCG ARNLDQQELV KHCMENHRND
     PNKVVCPICS AMPWGDPSYK SANFLQHLLH RHKFSYDTFV DYSIDEEAAL QAALALSLSE
     N