RN181_RAT
ID RN181_RAT Reviewed; 165 AA.
AC Q6AXU4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PROTEIN SEQUENCE OF 21-29, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
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; BC079313; AAH79313.1; -; mRNA.
DR RefSeq; NP_001007648.1; NM_001007647.1.
DR AlphaFoldDB; Q6AXU4; -.
DR SMR; Q6AXU4; -.
DR BioGRID; 255552; 1.
DR STRING; 10116.ENSRNOP00000016699; -.
DR PaxDb; Q6AXU4; -.
DR PRIDE; Q6AXU4; -.
DR Ensembl; ENSRNOT00000016699; ENSRNOP00000016699; ENSRNOG00000012035.
DR GeneID; 297337; -.
DR KEGG; rno:297337; -.
DR UCSC; RGD:1359698; rat.
DR CTD; 51255; -.
DR RGD; 1359698; Rnf181.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000160552; -.
DR HOGENOM; CLU_144247_0_0_1; -.
DR InParanoid; Q6AXU4; -.
DR OMA; EHLHGAM; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q6AXU4; -.
DR Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6AXU4; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000012035; Expressed in testis and 20 other tissues.
DR Genevisible; Q6AXU4; RN.
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:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:RGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..165
FT /note="E3 ubiquitin-protein ligase RNF181"
FT /id="PRO_0000295176"
FT ZN_FING 88..129
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 136..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0P0"
SQ SEQUENCE 165 AA; 19288 MW; D6D76C9926805C1C CRC64;
MASYFDEHDC EPLNPEREAR NNMLLELARR VRGAWSWAPG SRSLFNRMDF EDLGLVDWEH
HLPPPAAKAV VESLPRTVIR SSKAELKCPV CLLEFEEEET VIEMPCHHLF HSNCILPWLS
KTNSCPLCRH ELPTDDDSYE EHKKDKARRQ QQQHRLENLH GAMYT
