RN138_XENLA
ID RN138_XENLA Reviewed; 222 AA.
AC Q1L721;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=E3 ubiquitin-protein ligase RNF138;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Nemo-like kinase-associated RING finger protein {ECO:0000303|PubMed:16714285};
DE Short=NLK-associated RING finger protein {ECO:0000303|PubMed:16714285};
DE Short=xNARF {ECO:0000303|PubMed:16714285};
DE AltName: Full=RING finger protein 138;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF138 {ECO:0000305};
GN Name=rnf138; Synonyms=narf {ECO:0000303|PubMed:16714285};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NLK.2 AND UBE2K,
RP DOMAIN, AND MUTAGENESIS OF CYS-17 AND CYS-53.
RC TISSUE=Oocyte;
RX PubMed=16714285; DOI=10.1074/jbc.m602089200;
RA Yamada M., Ohnishi J., Ohkawara B., Iemura S., Satoh K., Hyodo-Miura J.,
RA Kawachi K., Natsume T., Shibuya H.;
RT "NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates
RT the ubiquitylation and degradation of T cell factor/lymphoid enhancer
RT factor (TCF/LEF).";
RL J. Biol. Chem. 281:20749-20760(2006).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in DNA damage response
CC by promoting DNA resection and homologous recombination. Recruited to
CC sites of double-strand breaks following DNA damage and specifically
CC promotes double-strand break repair via homologous recombination (By
CC similarity). Together with nlk.2, involved in the ubiquitination and
CC degradation of TCF/LEF. Also exhibits auto-ubiquitination activity in
CC combination with ube2k. May act as a negative regulator in the
CC Wnt/beta-catenin-mediated signaling pathway (PubMed:16714285).
CC {ECO:0000250|UniProtKB:Q8WVD3, ECO:0000269|PubMed:16714285}.
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:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:16714285}.
CC -!- SUBUNIT: Interacts with nlk.2 (via C-terminus) and ube2k.
CC {ECO:0000269|PubMed:16714285}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8WVD3}.
CC Note=Recruited at DNA damage sites. Localizes to sites of double-strand
CC break: localization to double-strand break sites is mediated by the
CC zinc fingers. {ECO:0000250|UniProtKB:Q8WVD3}.
CC -!- DOMAIN: The zinc finger domains (C2H2-type and C2HC-type zinc fingers)
CC bind DNA and mediate recruitment to double-strand break sites. They
CC show strong preference for DNA with 5'- or 3'-single-stranded
CC overhangs, while they do not bind blunt-ended double-stranded DNA or
CC poly(ADP-ribose) (PAR) polymers. {ECO:0000250|UniProtKB:Q8WVD3}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:16714285}.
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DR EMBL; DQ011285; AAY68290.1; -; mRNA.
DR RefSeq; NP_001089974.1; NM_001096505.1.
DR AlphaFoldDB; Q1L721; -.
DR BioGRID; 592826; 3.
DR MaxQB; Q1L721; -.
DR DNASU; 735045; -.
DR GeneID; 735045; -.
DR KEGG; xla:735045; -.
DR CTD; 735045; -.
DR Xenbase; XB-GENE-1001378; rnf138.S.
DR OrthoDB; 1097558at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 735045; Expressed in egg cell and 9 other tissues.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR034734; ZF_C2HC_RNF.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF05605; zf-Di19; 1.
DR Pfam; PF18574; zf_C2HC_14; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS51803; ZF_C2HC_RNF; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA repair; DNA-binding; Metal-binding;
KW Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..222
FT /note="E3 ubiquitin-protein ligase RNF138"
FT /id="PRO_0000261610"
FT DOMAIN 202..220
FT /note="UIM"
FT /evidence="ECO:0000250|UniProtKB:Q8WVD3"
FT ZN_FING 17..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 85..104
FT /note="C2HC RNF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT ZN_FING 134..157
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 164..192
FT /note="C2H2-type 2"
FT /evidence="ECO:0000250|UniProtKB:Q8WVD3"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT MUTAGEN 17
FT /note="C->A: Prevents ubiquitination and auto-
FT ubiquitination; when associated with A-53."
FT /evidence="ECO:0000269|PubMed:16714285"
FT MUTAGEN 53
FT /note="C->A: Prevents ubiquitination and auto-
FT ubiquitination; when associated with A-17."
FT /evidence="ECO:0000269|PubMed:16714285"
SQ SEQUENCE 222 AA; 25480 MW; 3B8ACABEDB042DE6 CRC64;
MAEAMSCSSE ITEEFLCPVC QEILQTPVRT QTCRHVFCRK CFMLAMKSGG AYCPLCRGPV
NKSERSAPVR ATDIDLEMRM LSGGCMYCGK MMKLHYMKLH YKSCRKYQEE YGLSPKNVTI
QTGQNSTKCQ EPKYKCPLCS EHNLNQRSLL EHCNNVHYYE EVEMVCPICA TLPWGDPIQT
TGNVIAHLNA RHQFNYQEFM NINIDEEAQF QIAVANSYKI SR
