RN138_BOVIN
ID RN138_BOVIN Reviewed; 245 AA.
AC Q32LN5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=E3 ubiquitin-protein ligase RNF138;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING finger protein 138;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF138 {ECO:0000305};
GN Name=RNF138;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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; BC109497; AAI09498.1; -; mRNA.
DR RefSeq; NP_001033263.1; NM_001038174.2.
DR RefSeq; XP_015315540.1; XM_015460054.1.
DR AlphaFoldDB; Q32LN5; -.
DR SMR; Q32LN5; -.
DR STRING; 9913.ENSBTAP00000026851; -.
DR PaxDb; Q32LN5; -.
DR PRIDE; Q32LN5; -.
DR Ensembl; ENSBTAT00000026851; ENSBTAP00000026851; ENSBTAG00000020160.
DR GeneID; 538445; -.
DR KEGG; bta:538445; -.
DR CTD; 51444; -.
DR VEuPathDB; HostDB:ENSBTAG00000020160; -.
DR VGNC; VGNC:34022; RNF138.
DR eggNOG; ENOG502RP2G; Eukaryota.
DR GeneTree; ENSGT00950000182909; -.
DR HOGENOM; CLU_092448_0_0_1; -.
DR InParanoid; Q32LN5; -.
DR OMA; HHYKTCK; -.
DR OrthoDB; 1097558at2759; -.
DR TreeFam; TF331012; -.
DR Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000020160; Expressed in semen and 106 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; IEA:Ensembl.
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: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; 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; 2.
DR PROSITE; PS51803; ZF_C2HC_RNF; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; DNA damage; DNA repair; DNA-binding;
KW Metal-binding; Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Wnt signaling pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WVD3"
FT CHAIN 2..245
FT /note="E3 ubiquitin-protein ligase RNF138"
FT /id="PRO_0000261606"
FT DOMAIN 225..243
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 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 187..215
FT /note="C2H2-type 2"
FT /evidence="ECO:0000250|UniProtKB:Q8WVD3"
FT REGION 128..153
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 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVD3"
SQ SEQUENCE 245 AA; 28157 MW; 05144A143455988F CRC64;
MAEELSAATS YTEDDFYCPV CQEVLKTPVR TAACQHVFCR KCFLTAMRES GIHCPLCRGN
VTRRERACPE RALDLENIMR KFSGSCRCCA KQIKFYRMRH HYKSCKKYQD EYGVSSIIPN
FQISQDSVGN SNRSETSASD NIETYQENTG SSGHPTFKCP LCQESNFTRQ RLLDHCNSNH
LFQIVPVTCP ICVSLPWGDP SQVTRNFVSH LNQRHQFDYG EFVNLQLDEE TQYQTAVEES
FQVNI
