RN125_MOUSE
ID RN125_MOUSE Reviewed; 233 AA.
AC Q9D9R0; Q0VG32; Q52KL4; Q8C7F2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=E3 ubiquitin-protein ligase RNF125;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q96EQ8};
DE AltName: Full=RING finger protein 125;
GN Name=Rnf125;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 69-233 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver, and Testis;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 79-233 (ISOFORM 1).
RC STRAIN=129; TISSUE=Brain, and Mammary tumor;
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 mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins, such as
CC DDX58/RIG-I, MAVS/IPS1, IFIH1/MDA5, JAK1 and p53/TP53. Acts as a
CC negative regulator of type I interferon production by mediating
CC ubiquitination of DDX58/RIG-I at 'Lys-181', leading to DDX58/RIG-I
CC degradation. Mediates ubiquitination and subsequent degradation of
CC p53/TP53. Mediates ubiquitination and subsequent degradation of JAK1.
CC Acts as a positive regulator of T-cell activation.
CC {ECO:0000250|UniProtKB:Q96EQ8}.
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:Q96EQ8};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q96EQ8}.
CC -!- SUBUNIT: Interacts with UBE2D1. Interacts with VCP/p97; leading to
CC recruit RNF125 to DDX58/RIG-I and promote ubiquitination of DDX58/RIG-
CC I. {ECO:0000250|UniProtKB:Q96EQ8}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q96EQ8}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q96EQ8}. Note=Shows a reticular staining pattern
CC within the cell and is probably expressed at other intracellular
CC membranes in addition to the Golgi membrane. Not detected at the plasma
CC membrane. {ECO:0000250|UniProtKB:Q96EQ8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D9R0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D9R0-2; Sequence=VSP_015216;
CC -!- DOMAIN: The C2HC RNF-type zinc finger and the linker region stabilize
CC the RING-type zinc finger, leading to promote binding of the RING-type
CC zinc finger to the ubiquitin-conjugating enzyme E2 (donor ubiquitin).
CC {ECO:0000250|UniProtKB:Q96EQ8}.
CC -!- PTM: Autoubiquitinated, leading to its subsequent proteasomal
CC degradation. {ECO:0000250|UniProtKB:Q96EQ8}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24656.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK006569; BAB24656.1; ALT_FRAME; mRNA.
DR EMBL; AK050395; BAC34234.1; -; mRNA.
DR EMBL; AC138611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094290; AAH94290.1; -; mRNA.
DR EMBL; BC116883; AAI16884.1; -; mRNA.
DR EMBL; BC116887; AAI16888.1; -; mRNA.
DR CCDS; CCDS29088.1; -. [Q9D9R0-2]
DR CCDS; CCDS89199.1; -. [Q9D9R0-1]
DR RefSeq; NP_080577.1; NM_026301.2. [Q9D9R0-2]
DR RefSeq; XP_006526251.1; XM_006526188.3.
DR AlphaFoldDB; Q9D9R0; -.
DR SMR; Q9D9R0; -.
DR BioGRID; 212348; 2.
DR STRING; 10090.ENSMUSP00000058251; -.
DR iPTMnet; Q9D9R0; -.
DR PhosphoSitePlus; Q9D9R0; -.
DR MaxQB; Q9D9R0; -.
DR PaxDb; Q9D9R0; -.
DR PRIDE; Q9D9R0; -.
DR ProteomicsDB; 300533; -. [Q9D9R0-1]
DR ProteomicsDB; 300534; -. [Q9D9R0-2]
DR Antibodypedia; 22188; 218 antibodies from 30 providers.
DR DNASU; 67664; -.
DR Ensembl; ENSMUST00000050004; ENSMUSP00000058251; ENSMUSG00000033107. [Q9D9R0-2]
DR Ensembl; ENSMUST00000234316; ENSMUSP00000157304; ENSMUSG00000033107. [Q9D9R0-1]
DR GeneID; 67664; -.
DR KEGG; mmu:67664; -.
DR UCSC; uc008eez.1; mouse. [Q9D9R0-1]
DR CTD; 54941; -.
DR MGI; MGI:1914914; Rnf125.
DR VEuPathDB; HostDB:ENSMUSG00000033107; -.
DR eggNOG; ENOG502RYGV; Eukaryota.
DR GeneTree; ENSGT00950000182909; -.
DR HOGENOM; CLU_092448_2_1_1; -.
DR InParanoid; Q9D9R0; -.
DR OMA; FKNCTEC; -.
DR OrthoDB; 1097558at2759; -.
DR PhylomeDB; Q9D9R0; -.
DR TreeFam; TF331012; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 67664; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Rnf125; mouse.
DR PRO; PR:Q9D9R0; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9D9R0; protein.
DR Bgee; ENSMUSG00000033107; Expressed in spermatid and 60 other tissues.
DR Genevisible; Q9D9R0; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; ISS:UniProtKB.
DR GO; GO:0032480; P:negative regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
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 Adaptive immunity; Alternative splicing; Golgi apparatus; Immunity;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT CHAIN 2..233
FT /note="E3 ubiquitin-protein ligase RNF125"
FT /id="PRO_0000056092"
FT ZN_FING 37..77
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 101..120
FT /note="C2HC RNF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..45
FT /note="Interaction with the C2HC RNF-type zinc finger"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT REGION 110..114
FT /note="Interaction with the RING-type zinc finger"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT REGION 121..129
FT /note="Linker region"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT REGION 211..225
FT /note="Required for interaction with ubiquitin and for
FT autoubiquitination"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015216"
FT CONFLICT 84
FT /note="G -> R (in Ref. 1; BAC34234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 233 AA; 26362 MW; 1B92E1F4F6C0113A CRC64;
MGSLLSSDSS KSAPASATPR TLERSGDSEL PITSFDCSVC LEVLHQPVRT RCGHVFCRSC
IATSIKNNNK WTCPYCRAYL PSEGVPATDI AKRMKSEYQN CAECGTLVCL SDMRAHIRTC
EKYIDKYGPL LELGDTTARC VCPFCQRELD EDCLLDHCII HHRSERRPVF CPLCHSRPDE
SPSTFNGSLI RHLQVSHTLF YDDFIDFDII EEAIIRRVLD RSLLEYVNQS NTT
