ID   RN181_XENTR             Reviewed;         156 AA.
AC   Q5M974;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF181 {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9P0P0};
DE   AltName: Full=RING finger protein 181;
GN   Name=rnf181; ORFNames=TEgg007l03.1 {ECO:0000303|Ref.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC       E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC       directly transfers the ubiquitin to targeted substrates. Catalyzes
CC       monoubiquitination of 26S proteasome subunit PSMC2/RPT1.
CC       {ECO:0000250|UniProtKB:Q9P0P0}.
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:Q9P0P0};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9P0P0}.
CC   -!- SIMILARITY: Belongs to the RNF181 family. {ECO:0000305}.
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DR   EMBL; CR762012; CAJ81968.1; -; mRNA.
DR   EMBL; BC087570; AAH87570.1; -; mRNA.
DR   RefSeq; NP_001011200.1; NM_001011200.2.
DR   RefSeq; XP_012814375.1; XM_012958921.2.
DR   RefSeq; XP_012814377.1; XM_012958923.2.
DR   RefSeq; XP_012814378.1; XM_012958924.2.
DR   AlphaFoldDB; Q5M974; -.
DR   SMR; Q5M974; -.
DR   STRING; 8364.ENSXETP00000002719; -.
DR   DNASU; 496625; -.
DR   GeneID; 496625; -.
DR   KEGG; xtr:496625; -.
DR   CTD; 51255; -.
DR   Xenbase; XB-GENE-964051; rnf181.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_144247_0_0_1; -.
DR   InParanoid; Q5M974; -.
DR   OrthoDB; 1249953at2759; -.
DR   PhylomeDB; Q5M974; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..156
FT                   /note="E3 ubiquitin-protein ligase RNF181"
FT                   /id="PRO_0000295701"
FT   ZN_FING         79..120
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   156 AA;  18001 MW;  027DD14B14EABF0E CRC64;
     MASYFDEHNC EPTVPEEQYR QNALLELARS LLSGMDIDLG ALDFTEWDQR LPPPAAKKVV
     ESLPKVTVTP EQADAALKCP VCLLEFEEGE TVRQLPCEHL FHSSCILPWL GKTNSCPLCR
     HELPTDSPEY EEYKQEKERR QQKEHRLECL HDAMYT