RN166_MOUSE
ID RN166_MOUSE Reviewed; 237 AA.
AC Q3U9F6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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; AK151813; BAE30711.1; -; mRNA.
DR CCDS; CCDS22740.1; -.
DR RefSeq; NP_001028314.1; NM_001033142.2.
DR AlphaFoldDB; Q3U9F6; -.
DR SMR; Q3U9F6; -.
DR BioGRID; 213009; 2.
DR STRING; 10090.ENSMUSP00000014614; -.
DR iPTMnet; Q3U9F6; -.
DR PhosphoSitePlus; Q3U9F6; -.
DR MaxQB; Q3U9F6; -.
DR PaxDb; Q3U9F6; -.
DR PRIDE; Q3U9F6; -.
DR ProteomicsDB; 300416; -.
DR Antibodypedia; 30751; 126 antibodies from 20 providers.
DR Ensembl; ENSMUST00000014614; ENSMUSP00000014614; ENSMUSG00000014470.
DR GeneID; 68718; -.
DR KEGG; mmu:68718; -.
DR UCSC; uc009nsx.1; mouse.
DR CTD; 115992; -.
DR MGI; MGI:1915968; Rnf166.
DR VEuPathDB; HostDB:ENSMUSG00000014470; -.
DR eggNOG; ENOG502RB47; Eukaryota.
DR GeneTree; ENSGT00950000182909; -.
DR HOGENOM; CLU_092448_1_0_1; -.
DR InParanoid; Q3U9F6; -.
DR OMA; FCGDCLQ; -.
DR OrthoDB; 1097558at2759; -.
DR PhylomeDB; Q3U9F6; -.
DR TreeFam; TF331012; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 68718; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Rnf166; mouse.
DR PRO; PR:Q3U9F6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3U9F6; protein.
DR Bgee; ENSMUSG00000014470; Expressed in granulocyte and 263 other tissues.
DR ExpressionAtlas; Q3U9F6; baseline and differential.
DR Genevisible; Q3U9F6; MM.
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_0000245589"
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
