ID   RN181_BOVIN             Reviewed;         153 AA.
AC   Q3T0W3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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   -!- SUBUNIT: Directly interacts with ITGA2B and, as a result, with integrin
CC       ITGA2B/ITGB3. There is no evidence that integrin ITGA2B/ITGB3 is an
CC       endogenous substrate for RNF181-directed ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9P0P0}.
CC   -!- PTM: Auto-ubiquitinated as part of the enzymatic reaction.
CC       {ECO:0000250|UniProtKB:Q9P0P0}.
CC   -!- SIMILARITY: Belongs to the RNF181 family. {ECO:0000305}.
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DR   EMBL; BC102230; AAI02231.1; -; mRNA.
DR   RefSeq; NP_001029682.1; NM_001034510.2.
DR   AlphaFoldDB; Q3T0W3; -.
DR   SMR; Q3T0W3; -.
DR   STRING; 9913.ENSBTAP00000024336; -.
DR   PaxDb; Q3T0W3; -.
DR   PRIDE; Q3T0W3; -.
DR   Ensembl; ENSBTAT00000024336; ENSBTAP00000024336; ENSBTAG00000018286.
DR   GeneID; 515743; -.
DR   KEGG; bta:515743; -.
DR   CTD; 51255; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018286; -.
DR   VGNC; VGNC:34039; RNF181.
DR   eggNOG; KOG0800; Eukaryota.
DR   GeneTree; ENSGT00940000160552; -.
DR   HOGENOM; CLU_144247_0_0_1; -.
DR   InParanoid; Q3T0W3; -.
DR   OMA; EHLHGAM; -.
DR   OrthoDB; 1249953at2759; -.
DR   TreeFam; TF332127; -.
DR   Reactome; R-BTA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000018286; Expressed in cortex of kidney and 106 other tissues.
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:0051865; P:protein autoubiquitination; IEA:Ensembl.
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; Phosphoprotein; Reference proteome; Transferase;
KW   Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..153
FT                   /note="E3 ubiquitin-protein ligase RNF181"
FT                   /id="PRO_0000295173"
FT   ZN_FING         76..117
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          125..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..144
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         153
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0P0"
SQ   SEQUENCE   153 AA;  17949 MW;  DC732DE766E414CB CRC64;
     MASYFDEHDC EPLDRERDPR TNMLLELARS LFNRMDFEDL GLVVDWDHHL PPPAAKTAVE
     NLPRTVIRGS QAELKCPVCL LEFEEEETAI EMPCHHLFHS NCILPWLSKT NSCPLCRHEL
     PTDDDTYEEH KRDKARKQQQ KHRLENLHGA MYT