RN182_XENLA
ID RN182_XENLA Reviewed; 246 AA.
AC Q6INB3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=E3 ubiquitin-protein ligase RNF182;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 182;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF182 {ECO:0000305};
GN Name=rnf182;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination
CC of atp6v0c and targets it to degradation via the ubiquitin-proteasome
CC pathway. {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 -!- SUBUNIT: Interacts with ATP6V0C. {ECO:0000250|UniProtKB:Q8N6D2}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q8N6D2}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000250}.
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DR EMBL; BC072370; AAH72370.1; -; mRNA.
DR RefSeq; NP_001085077.1; NM_001091608.1.
DR AlphaFoldDB; Q6INB3; -.
DR SMR; Q6INB3; -.
DR PRIDE; Q6INB3; -.
DR DNASU; 432148; -.
DR GeneID; 432148; -.
DR KEGG; xla:432148; -.
DR CTD; 432148; -.
DR Xenbase; XB-GENE-17336205; rnf182.S.
DR OrthoDB; 1216224at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 432148; Expressed in camera-type eye and 1 other tissue.
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; 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 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..246
FT /note="E3 ubiquitin-protein ligase RNF182"
FT /id="PRO_0000261622"
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 22..70
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 246 AA; 27604 MW; BFFDA2F535460856 CRC64;
MTSQLSEDNS ESPNLNSDEL ECKICYNRYN LRQRKPKVLG CCHRVCAKCL YKLVDCGESP
QCVIVCPFCR FETRMPEDEV SSLPDDNNIL LNLACGGRGK CVGDNPTELL LTPKRLSTIV
TPSHTSTNCL VITIMEVQRE SSPALNTTPM VEFYRPSNYD PVSIPQNWTV WNCTSLICKT
SVRVFVWLLG LLYFSSLPLG IYLLVSKKVT LGVVFVSLVP SSLVILMIYG FCQCMCHEFL
DCMSTP