RN166_RAT
ID RN166_RAT Reviewed; 237 AA.
AC Q6J1I7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Ma Y., Wang C., Wu Q., Zhang S.Z., Hong Z., Li N., Peng Y.;
RT "Molecular cloning of a novel rat zinc finger protein gene.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination
CC of different substrates. In turn, participates in different biological
CC processes including interferon production or autophagy. Plays a role in
CC the activation of RNA virus-induced interferon-beta production by
CC promoting the ubiquitination of TRAF3 and TRAF6. Also plays a role in
CC the early recruitment of autophagy adapters to bacteria. Mediates 'Lys-
CC 29' and 'Lys-33'-linked ubiquitination of SQSTM1 leading to xenophagic
CC targeting of bacteria and inhibition of their replication.
CC {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; AY606065; AAT36621.1; -; mRNA.
DR EMBL; BC100057; AAI00058.1; -; mRNA.
DR RefSeq; NP_001002279.1; NM_001002279.1.
DR AlphaFoldDB; Q6J1I7; -.
DR SMR; Q6J1I7; -.
DR STRING; 10116.ENSRNOP00000018591; -.
DR PaxDb; Q6J1I7; -.
DR Ensembl; ENSRNOT00000018591; ENSRNOP00000018591; ENSRNOG00000013777.
DR GeneID; 365022; -.
DR KEGG; rno:365022; -.
DR UCSC; RGD:1302950; rat.
DR CTD; 115992; -.
DR RGD; 1302950; Rnf166.
DR eggNOG; ENOG502RB47; Eukaryota.
DR GeneTree; ENSGT00950000182909; -.
DR HOGENOM; CLU_092448_1_0_1; -.
DR InParanoid; Q6J1I7; -.
DR OMA; FCGDCLQ; -.
DR OrthoDB; 1097558at2759; -.
DR PhylomeDB; Q6J1I7; -.
DR TreeFam; TF331012; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6J1I7; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000013777; Expressed in testis and 19 other tissues.
DR Genevisible; Q6J1I7; RN.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; 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; 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 Autophagy; Cytoplasm; Immunity; Innate immunity; Metal-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..237
FT /note="E3 ubiquitin-protein ligase RNF166"
FT /id="PRO_0000245590"
FT DOMAIN 221..237
FT /note="UIM"
FT /evidence="ECO:0000305"
FT ZN_FING 33..73
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 98..117
FT /note="C2HC RNF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 113
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"
SQ SEQUENCE 237 AA; 26064 MW; C4042304E2A5E88E CRC64;
MAMFRSLVAS AQQRQPPAGP AGGDSGLEAQ FSCPICLEVY HRPVAIGSCG HTFCGECLQP
CLQVPSPLCP LCRLPFDPKK VDKATHVEKQ LSSYKAPCRG CNKKVTLAKM RAHISSCLKV
QEQMANCPKF VPVVPTSQPI PSNIPNRSTF ACPYCGARNL DQQELVKHCV ESHRSDPNRV
VCPICSAMPW GDPSYKSANF LQHLLHRHKF SYDTFVDYSI DEEAAFQAAL ALSLSEN
