RN181_DANRE
ID RN181_DANRE Reviewed; 156 AA.
AC Q7ZW78; B0V3A5; B0V3A6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 131.
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;
GN ORFNames=si:ch211-102c2.10 {ECO:0000303|PubMed:23594743},
GN zgc:56424 {ECO:0000303|Ref.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2003) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7ZW78-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7ZW78-2; Sequence=VSP_036585;
CC -!- SIMILARITY: Belongs to the RNF181 family. {ECO:0000305}.
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DR EMBL; CU041374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050161; AAH50161.1; -; mRNA.
DR RefSeq; NP_956600.1; NM_200306.1.
DR AlphaFoldDB; Q7ZW78; -.
DR SMR; Q7ZW78; -.
DR STRING; 7955.ENSDARP00000038991; -.
DR PaxDb; Q7ZW78; -.
DR Ensembl; ENSDART00000029450; ENSDARP00000038991; ENSDARG00000023958. [Q7ZW78-1]
DR Ensembl; ENSDART00000134728; ENSDARP00000120112; ENSDARG00000023958. [Q7ZW78-2]
DR Ensembl; ENSDART00000140392; ENSDARP00000123250; ENSDARG00000023958. [Q7ZW78-1]
DR Ensembl; ENSDART00000189373; ENSDARP00000146932; ENSDARG00000023958. [Q7ZW78-2]
DR GeneID; 393276; -.
DR KEGG; dre:393276; -.
DR CTD; 51255; -.
DR ZFIN; ZDB-GENE-040426-1024; rnf181.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000160552; -.
DR HOGENOM; CLU_144247_0_0_1; -.
DR InParanoid; Q7ZW78; -.
DR OMA; EHLHGAM; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q7ZW78; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q7ZW78; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000023958; Expressed in granulocyte and 27 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: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 Alternative splicing; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..156
FT /note="E3 ubiquitin-protein ligase RNF181"
FT /id="PRO_0000295699"
FT ZN_FING 79..120
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 135..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 112..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036585"
FT CONFLICT 17
FT /note="E -> G (in Ref. 2; AAH50161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 18033 MW; DE46F627999230F9 CRC64;
MASYFDEHDC EPTNPEEQYR QNALLELARS LMQGLDIDSG SFDLSDWDQR LPPPAAKAVV
QSLPVVIISP EQADKGVKCP VCLLEFEEQE SVREMPCKHL FHTGCILPWL NKTNSCPLCR
LELPTDNADY EEFKKDKERR RQREHRLEDL HGAMYT
