ID RN182_RAT Reviewed; 247 AA.
AC D3ZBM4;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=E3 ubiquitin-protein ligase RNF182;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8N6D2};
DE AltName: Full=RING finger protein 182;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF182 {ECO:0000305};
GN Name=Rnf182;
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=30450663; DOI=10.1002/jcb.28038;
RA Wang J.H., Wei Z.F., Gao Y.L., Liu C.C., Sun J.H.;
RT "Activation of the mammalian target of rapamycin signaling pathway
RT underlies a novel inhibitory role of ring finger protein 182 in ventricular
RT remodeling after myocardial ischemia-reperfusion injury.";
RL J. Cell. Biochem. 0:0-0(2018).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination
CC of ATP6V0C and targets it to degradation via the ubiquitin-proteasome
CC pathway. Also plays a role in the inhibition of TLR-triggered innate
CC immune response by mediating 'Lys'-48-linked ubiquitination and
CC subsequent degradation of NF-kappa-B component RELA.
CC {ECO:0000250|UniProtKB:Q8N6D2}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q8N6D2}.
CC -!- SUBUNIT: Interacts with ATP6V0C. {ECO:0000250|UniProtKB:Q8N6D2}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8N6D2}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q8N6D2}. Cytoplasm
CC {ECO:0000269|PubMed:30450663}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Silencing prevents ventricular remodeling in rats
CC after myocardial ischemia-reperfusion injury by activating the mTOR
CC signaling pathway. {ECO:0000269|PubMed:30450663}.
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DR EMBL; CH473977; EDL98193.1; -; Genomic_DNA.
DR RefSeq; NP_001102587.1; NM_001109117.1.
DR RefSeq; XP_017456133.1; XM_017600644.1.
DR AlphaFoldDB; D3ZBM4; -.
DR SMR; D3ZBM4; -.
DR STRING; 10116.ENSRNOP00000024323; -.
DR PhosphoSitePlus; D3ZBM4; -.
DR PaxDb; 10116-ENSRNOP00000024323; -.
DR Ensembl; ENSRNOT00000024323.4; ENSRNOP00000024323.2; ENSRNOG00000018070.4.
DR Ensembl; ENSRNOT00000095392.1; ENSRNOP00000089379.1; ENSRNOG00000018070.4.
DR Ensembl; ENSRNOT00000119567.1; ENSRNOP00000092002.1; ENSRNOG00000018070.4.
DR GeneID; 498726; -.
DR KEGG; rno:498726; -.
DR UCSC; RGD:1560399; rat.
DR AGR; RGD:1560399; -.
DR CTD; 221687; -.
DR RGD; 1560399; Rnf182.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00730000111020; -.
DR HOGENOM; CLU_100624_0_0_1; -.
DR InParanoid; D3ZBM4; -.
DR OMA; QRNLHFH; -.
DR OrthoDB; 5352785at2759; -.
DR PhylomeDB; D3ZBM4; -.
DR TreeFam; TF331690; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:D3ZBM4; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000234681; Chromosome 17.
DR Bgee; ENSRNOG00000018070; Expressed in cerebellum and 6 other cell types or tissues.
DR Genevisible; D3ZBM4; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR CDD; cd16555; RING-HC_RNF182; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR042285; RNF182.
DR InterPro; IPR047986; RNF182_RING-HC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46675; E3 UBIQUITIN-PROTEIN LIGASE RNF182; 1.
DR PANTHER; PTHR46675:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF182; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Membrane; Metal-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..247
FT /note="E3 ubiquitin-protein ligase RNF182"
FT /id="PRO_0000395671"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 20..68
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 247 AA; 27546 MW; 43E7646C4A35BF49 CRC64;
MASQPPEEPA EFQVSDELEC KICYNRYNLK QRKPKVLECC HRVCAKCLYK IIDFGDSPQG
VIVCPFCRFE TCLPDDEVSS LPDDNNILVN LTCGSKGKKC LPENPTELLL TPKRLASLVS
PSHTSSNCLV ITIMEVQRES SPSLSSTPVV EFYRPASFDS VTTVSHNWTV WNCTSLLFQT
SIRVLVWLLG LLYFSSLPLG IYLLVSKKVT LGVVFVSLVP SSLVILMVYG FCQCVCHEFL
DCMALPS
//
