ID A0A8S3YTR5_9EUPU Unreviewed; 302 AA.
AC A0A8S3YTR5;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE RecName: Full=E3 ubiquitin-protein ligase RNF144B {ECO:0000256|ARBA:ARBA00069720};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE AltName: Full=RING finger protein 144B {ECO:0000256|ARBA:ARBA00078867};
GN ORFNames=CUNI_LOCUS4540 {ECO:0000313|EMBL:CAG5118982.1};
OS Candidula unifasciata.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC Helicina; Helicoidea; Geomitridae; Candidula.
OX NCBI_TaxID=100452 {ECO:0000313|EMBL:CAG5118982.1, ECO:0000313|Proteomes:UP000678393};
RN [1] {ECO:0000313|EMBL:CAG5118982.1}
RP NUCLEOTIDE SEQUENCE.
RG Molecular Ecology Group;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2
CC ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a
CC thioester and then directly transfers the ubiquitin to targeted
CC substrates such as LCMT2, thereby promoting their degradation. Induces
CC apoptosis via a p53/TP53-dependent but caspase-independent mechanism.
CC Plays a crucial role in maintaining the genomic stability by
CC controlling the degradation of multiple proteins involved in mitotic
CC progression and DNA damage. Regulates epithelial homeostasis by
CC mediating degradation of CDKN1A and isoform 2 of TP63. Plays a
CC regulatory role in innate immunity by negatively regulating IRF3
CC activation and IFN-beta production. Mechanistically, inhibits TBK1
CC phosphorylation and 'Lys-63'-linked polyubiquitination independently of
CC its E3 ligase activity. Alternatively, promotes 'Lys-27' and 'Lys-33'-
CC linked ubiquitination of IFIH1/MDA5, promoting selective autophagic
CC degradation of IFIH1/MDA5 to inhibit antiviral response.
CC {ECO:0000256|ARBA:ARBA00060040}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Interacts with UBE2L3, UBE2L6 and LCMT2, as well as with BAX.
CC Interacts with TBK1; this interaction inhibits TBK1 phosphorylation and
CC 'Lys-63'-linked polyubiquitination. {ECO:0000256|ARBA:ARBA00061765}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004304}; Single-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004304}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF144 subfamily.
CC {ECO:0000256|ARBA:ARBA00038342}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAG5118982.1}.
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; CAJHNH020000639; CAG5118982.1; -; Genomic_DNA.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000678393; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20349; BRcat_RBR_RNF144; 1.
DR CDD; cd16632; mRING-HC-C4C4_RBR_RNF144; 1.
DR CDD; cd20352; Rcat_RBR_RNF144; 1.
DR FunFam; 1.20.120.1750:FF:000010; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000051; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000678393};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 256..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..242
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
SQ SEQUENCE 302 AA; 33998 MW; CA1025C8B734C067 CRC64;
MATYCASKNT VDLAIDPLIL CKLCLSECPL EDMYELEDCK CLFCEMCMRQ YLFVLISEGM
VADLTCPDAQ CRKQGRLTHK EIEKLVDRQT FLRYKRLQFE REVDLDPNRT FCPEIGCETV
CHVCSSQSHS DDGASSTSVS VKCPTCGLQF CSVCKSKWHA PMSCNDVFAA APAEEAGIPY
NNIEDAKIKR CPVCLVPIER NDGCAQMMCK RCKHIFCWYC LQSLDDDFLL RHYDKGPCKN
KLGHSRASVI WHRTQVVGIF AGFGVLLLVA SPFLLLAAPC ILCCKCKFSR CCDDEEGDVF
TT
//
