RN166_CHICK
ID RN166_CHICK Reviewed; 244 AA.
AC Q5F3B2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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; ORFNames=RCJMB04_23k19;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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}.
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DR EMBL; AJ851738; CAH65372.1; -; mRNA.
DR RefSeq; NP_001012953.1; NM_001012935.1.
DR AlphaFoldDB; Q5F3B2; -.
DR STRING; 9031.ENSGALP00000011768; -.
DR PaxDb; Q5F3B2; -.
DR GeneID; 425360; -.
DR KEGG; gga:425360; -.
DR CTD; 115992; -.
DR VEuPathDB; HostDB:geneid_425360; -.
DR eggNOG; ENOG502RB47; Eukaryota.
DR HOGENOM; CLU_092448_1_0_1; -.
DR InParanoid; Q5F3B2; -.
DR OrthoDB; 1097558at2759; -.
DR PhylomeDB; Q5F3B2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5F3B2; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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..244
FT /note="E3 ubiquitin-protein ligase RNF166"
FT /id="PRO_0000245591"
FT DOMAIN 228..244
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 40..80
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 105..124
FT /note="C2HC RNF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT REGION 10..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
SQ SEQUENCE 244 AA; 26644 MW; 15437E8DD817123D CRC64;
MFRSLLVAAA QRPQAPGPGP PRPPPPAGPA AEALEAQFSC PICLEVFHRA VGIAGCGHTF
CGECLQPCLQ VPSPLCPLCR MPFDPKKVEK ASSVEKQLSS YKAPCRGCSK KVTLAKMRSH
VSSCAKVQEQ MANCPKFVPV VPTSQPIPSN IPNRSTFVCP YCGARNLDQQ ELVKHCMENH
RNDPNKVVCP VCSAMPWGDP SYKSANFLQH LLHRHKFSYD TFVDYNIDEE AALQAALALS
LSEN
