RN169_DANRE
ID RN169_DANRE Reviewed; 630 AA.
AC E7FAP1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=E3 ubiquitin-protein ligase RNF169;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 169;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF169 {ECO:0000305};
GN Name=rnf169;
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).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase that acts as a negative
CC regulator of double-strand breaks (DSBs) repair following DNA damage.
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
CC Note=Localizes to sites of double-strand breaks (DSBs) following DNA
CC damage. {ECO:0000250}.
CC -!- DOMAIN: The MIU motif (motif interacting with ubiquitin) mediates the
CC interaction with both 'Lys-48'- and 'Lys-63'-linked ubiquitin chains.
CC The UMI motif also mediates interaction with ubiquitin. The specificity
CC for different types of ubiquitin is mediated by juxtaposition of
CC ubiquitin-binding motifs (MIU and UMI motifs) with LR motifs (LRMs) (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNF169 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CT027729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001336012.2; XM_001335976.4.
DR AlphaFoldDB; E7FAP1; -.
DR SMR; E7FAP1; -.
DR STRING; 7955.ENSDARP00000062855; -.
DR PaxDb; E7FAP1; -.
DR Ensembl; ENSDART00000062856; ENSDARP00000062855; ENSDARG00000042825.
DR GeneID; 795748; -.
DR KEGG; dre:795748; -.
DR CTD; 254225; -.
DR ZFIN; ZDB-GENE-030131-4336; rnf169.
DR eggNOG; KOG4159; Eukaryota.
DR GeneTree; ENSGT00940000153680; -.
DR HOGENOM; CLU_034296_0_0_1; -.
DR InParanoid; E7FAP1; -.
DR OMA; QMTQTHR; -.
DR OrthoDB; 1189777at2759; -.
DR PhylomeDB; E7FAP1; -.
DR TreeFam; TF332796; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:E7FAP1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 15.
DR Bgee; ENSDARG00000042825; Expressed in testis and 24 other tissues.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:2000780; P:negative regulation of double-strand break repair; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW DNA damage; Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..630
FT /note="E3 ubiquitin-protein ligase RNF169"
FT /id="PRO_0000418009"
FT ZN_FING 36..75
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 155..163
FT /note="UMI motif"
FT MOTIF 565..582
FT /note="MIU motif"
FT MOTIF 599..611
FT /note="LR motif"
SQ SEQUENCE 630 AA; 71358 MW; 7C54E548E2B98A78 CRC64;
MKMAAVGSAK STGPGQRSKS RPGALSAPLS LEEARCPVCS EILLEPVTMP CGHSVCLHCF
QRTVKLISLC CPLCRLRVSS WARKQSREKS LVNAELWELV RLSHPERCKR RMEQRDGEIP
DGEIFRAPVP VHKVGEMRQE YEKQKMKSGR SEETDERKKK MHIKEECVLL KHCQYPFCGV
SDSENEEPVG RRTRHVSAFV RKTRCSPAFN KSCLHSSAAQ RSRSCTDSED GRGKSRGHTN
QAVPEKANIA HSYNAGILLS SENSRSFSAP LLSLDKRHHW RGIHTSSATL VLQTKPERSI
SPESNDSISE ELNHFKPIVC SPCTPPKRLP DGRLLEPMIV KSTPRNLTRA LHKSTSYEAS
PTILQKWKQI EVDRQCIKVT SKGTVTSPIA EDLNLKLSPV EERDCQPCSC SVAKDRLLDL
QCICGSNAHK SKSRKDKPII YNKRRLIFDP YNKGEEKTQV AALIKTFGDS STPKACKELC
EPSEMGPPML DSNAGHCNQG TVDPDHNIKI NEPTTMSCVL NRPTSRRGKK RSQKTKHMEE
TLQTKISRTN RYDSLDDLIV QRMSQEKEDR ELALKLQRQF DRECKKVDRH KTSRNKYELR
SWGSKDGIVG YNTRRSGRVS KQNEHFNYTC
