RN182_MOUSE
ID RN182_MOUSE Reviewed; 247 AA.
AC Q8C432;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
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 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=Hippocampus;
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 MRNA].
RC TISSUE=Tooth;
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).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=18298843; DOI=10.1186/1750-1326-3-4;
RA Liu Q.Y., Lei J.X., Sikorska M., Liu R.;
RT "A novel brain-enriched E3 ubiquitin ligase RNF182 is up regulated in the
RT brains of Alzheimer's patients and targets ATP6V0C for degradation.";
RL Mol. Neurodegener. 3:4-4(2008).
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 -!- TISSUE SPECIFICITY: Expressed in the cortex, hippocampus, cerebellum
CC and spinal cord, but not in the heart, liver, kidney or skeletal
CC muscle. {ECO:0000269|PubMed:18298843}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000250}.
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DR EMBL; AK083175; BAC38795.1; -; mRNA.
DR EMBL; BC089488; AAH89488.1; -; mRNA.
DR CCDS; CCDS26480.1; -.
DR RefSeq; NP_899027.1; NM_183204.4.
DR RefSeq; XP_006516996.1; XM_006516933.3.
DR AlphaFoldDB; Q8C432; -.
DR SMR; Q8C432; -.
DR STRING; 10090.ENSMUSP00000062005; -.
DR PhosphoSitePlus; Q8C432; -.
DR PaxDb; Q8C432; -.
DR PRIDE; Q8C432; -.
DR Antibodypedia; 1547; 133 antibodies from 19 providers.
DR DNASU; 328234; -.
DR Ensembl; ENSMUST00000059986; ENSMUSP00000062005; ENSMUSG00000044164.
DR GeneID; 328234; -.
DR KEGG; mmu:328234; -.
DR UCSC; uc007qgh.2; mouse.
DR CTD; 221687; -.
DR MGI; MGI:3045355; Rnf182.
DR VEuPathDB; HostDB:ENSMUSG00000044164; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00730000111020; -.
DR HOGENOM; CLU_100624_0_0_1; -.
DR InParanoid; Q8C432; -.
DR OMA; FLDCMAL; -.
DR OrthoDB; 1216224at2759; -.
DR PhylomeDB; Q8C432; -.
DR TreeFam; TF331690; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 328234; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8C432; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8C432; protein.
DR Bgee; ENSMUSG00000044164; Expressed in olfactory epithelium and 137 other tissues.
DR ExpressionAtlas; Q8C432; baseline and differential.
DR Genevisible; Q8C432; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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; ISS:UniProtKB.
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 2: Evidence at transcript level;
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_0000261621"
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; 27444 MW; F6CC9BEAFF18781E CRC64;
MASQPLEEPA ESQASDELEC KICYNRYNLK QRKPKVLECC HRVCAKCLYK IIDFGDSPQG
VIVCPFCRFE TCLPDDEVSS LPDDNNILVN LTCGGKGKKC LPENPTELLL TPKRLASLVS
PSHTSSNCLV ITIMEVQRES SPSLSSTPVV EFYRPASFDS VTTVSHNWTV WNCTSLLFQT
SIRVLVWLLG LLYFSSLPLG IYLLVSKKVT LGVVFVSLVP SSLVILMVYG FCQCVCHEFL
DCMALPS
