RN182_AILME
ID RN182_AILME Reviewed; 247 AA.
AC D2H788;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
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; ORFNames=PANDA_005987;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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:0000250|UniProtKB:Q8N6D2}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL192549; EFB20934.1; -; Genomic_DNA.
DR RefSeq; XP_002917648.1; XM_002917602.3.
DR AlphaFoldDB; D2H788; -.
DR SMR; D2H788; -.
DR STRING; 9646.ENSAMEP00000021351; -.
DR Ensembl; ENSAMET00000022120; ENSAMEP00000021351; ENSAMEG00000020297.
DR GeneID; 100469497; -.
DR KEGG; aml:100469497; -.
DR CTD; 221687; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00730000111020; -.
DR HOGENOM; CLU_100624_0_0_1; -.
DR InParanoid; D2H788; -.
DR OMA; FLDCMAL; -.
DR OrthoDB; 1216224at2759; -.
DR TreeFam; TF331690; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042285; RNF182.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46675; PTHR46675; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 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_0000395670"
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; 27287 MW; 012C276C5A06AED7 CRC64;
MASQSPDEAA EAQVSDELEC KICYNRYNLK QRKPKVLECC HRVCAKCLYK IIDFGDSPQG
VIVCPFCRFE TCLPDEEVSS LPDDSNILVN LTCGGKGKKG LPENPTELLL TPKRLASLVS
PSHTSSNCLV ITIMEVQRES SPSLSSTPVV EFYRPASFDS VTTVSHNWTV WKCTSLLFQT
SIRVLVWLLG LLYFSSLPLG IYLLVSKKVT LGVVFVSLVP SSLVILMVYG FCQCVCHEFL
DCVAPSS
