RN138_RAT
ID RN138_RAT Reviewed; 209 AA.
AC Q99PD2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=E3 ubiquitin-protein ligase RNF138 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING finger protein 138 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF138 {ECO:0000305};
GN Name=Rnf138 {ECO:0000312|RGD:621485}; ORFNames=RSD-4 {ECO:0000303|Ref.1};
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 [MRNA].
RC TISSUE=Testis;
RA Wang L., Gou D., Zhang X.;
RT "A rat testis-specific gene including a RING finger domain homolog to HSD-
RT 4.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
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. Two
CC different, non-exclusive, mechanisms have been proposed. According to a
CC report, regulates the choice of double-strand break repair by favoring
CC homologous recombination over non-homologous end joining (NHEJ): acts
CC by mediating ubiquitination of XRCC5/Ku80, leading to remove the Ku
CC complex from DNA breaks, thereby promoting homologous recombination.
CC According to another report, cooperates with UBE2Ds E2 ubiquitin
CC ligases (UBE2D1, UBE2D2, UBE2D3 or UBE2D4) to promote homologous
CC recombination by mediating ubiquitination of RBBP8/CtIP. Together with
CC NLK, involved in the ubiquitination and degradation of TCF/LEF. Also
CC exhibits auto-ubiquitination activity in combination with UBE2K. May
CC act as a negative regulator in the Wnt/beta-catenin-mediated signaling
CC pathway. {ECO:0000250|UniProtKB:Q8WVD3}.
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:0000250|UniProtKB:Q8WVD3}.
CC -!- SUBUNIT: Interacts with NLK. Interacts with XRCC5/Ku80. Interacts with
CC RBBP8/CtIP. {ECO:0000250|UniProtKB:Q8WVD3}.
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:0000250|UniProtKB:Q8WVD3}.
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DR EMBL; AF315468; AAK11282.1; -; mRNA.
DR EMBL; BC061821; AAH61821.1; -; mRNA.
DR RefSeq; NP_446040.1; NM_053588.2.
DR AlphaFoldDB; Q99PD2; -.
DR SMR; Q99PD2; -.
DR BioGRID; 250176; 2.
DR PRIDE; Q99PD2; -.
DR Ensembl; ENSRNOT00000102423; ENSRNOP00000084639; ENSRNOG00000015645.
DR GeneID; 94196; -.
DR KEGG; rno:94196; -.
DR CTD; 51444; -.
DR RGD; 621485; Rnf138.
DR GeneTree; ENSGT00950000182909; -.
DR InParanoid; Q99PD2; -.
DR OrthoDB; 1097558at2759; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q99PD2; -.
DR Proteomes; UP000002494; Chromosome 18.
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; ISO:RGD.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
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:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR034734; ZF_C2HC_RNF.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 2: Evidence at transcript level;
KW Chromosome; DNA damage; DNA repair; DNA-binding; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..209
FT /note="E3 ubiquitin-protein ligase RNF138"
FT /id="PRO_0000261609"
FT DOMAIN 189..207
FT /note="UIM"
FT /evidence="ECO:0000250|UniProtKB:Q8WVD3"
FT ZN_FING 18..58
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 86..105
FT /note="C2HC RNF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT ZN_FING 157..180
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 125..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVD3"
SQ SEQUENCE 209 AA; 24072 MW; 8C3A06E4EB24CFDB CRC64;
MSEELSADTS YTEDDFYCPV CQEVLKTPVR TAACQHVFCR KCFLTAMRES GIHCPLCRGS
VTRRERACPE RAIDLENIMR RVSGSCRCCS KKIKFYRMRH HYKSCKKYQD EYGVSSVIPN
VKISQDSVRS SNRSETSASD NTETYQEDTS SSGHPTFKCP LCQESNFTRQ RLLDHCNSNH
LFQIVPVNLQ LDEETQYQTA VEESFQVNM
