RN125_MACFA
ID RN125_MACFA Reviewed; 232 AA.
AC Q95KF1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 99.
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; ORFNames=QtrA-14722;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; AB060918; BAB46910.1; -; mRNA.
DR RefSeq; NP_001272107.1; NM_001285178.1.
DR AlphaFoldDB; Q95KF1; -.
DR SMR; Q95KF1; -.
DR STRING; 9541.XP_005587015.1; -.
DR GeneID; 102122979; -.
DR CTD; 54941; -.
DR eggNOG; ENOG502RYGV; Eukaryota.
DR OrthoDB; 1097558at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233100; Unplaced.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
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; Golgi apparatus; Immunity; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT CHAIN 2..232
FT /note="E3 ubiquitin-protein ligase RNF125"
FT /id="PRO_0000056091"
FT ZN_FING 37..76
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 100..119
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 109..113
FT /note="Interaction with the RING-type zinc finger"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT REGION 120..128
FT /note="Linker region"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT REGION 210..224
FT /note="Required for interaction with ubiquitin and for
FT autoubiquitination"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
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 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ8"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 119
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"
SQ SEQUENCE 232 AA; 26204 MW; 0C134D21D84DDD7F CRC64;
MGSVLSSDSG KSAPPSATPR ALERRGDPEL PVTSFDCAVC LEVLHQPVRT RCGHVFCRSC
IATSLKNNKW TCPYCRAYLP SEGVPATDVA KRMKSEYKNC AECDTLVCLG EMRAHIRTCQ
KYIDKYGPLQ ELGETAARCV CPFCQRELDE DSLLDHCITH HRSERRPVFC PLCRLIPDEN
PSSFSGSLIR HLQVSHTLFY DDFIDFNIIE EALIRRVLDR SLLEYVNQSN AT
