ID A0A6P7YR54_9AMPH Unreviewed; 303 AA.
AC A0A6P7YR54;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
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 Name=RNF144B {ECO:0000313|RefSeq:XP_030067458.1};
OS Microcaecilia unicolor.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Gymnophiona; Siphonopidae; Microcaecilia.
OX NCBI_TaxID=1415580 {ECO:0000313|Proteomes:UP000515156, ECO:0000313|RefSeq:XP_030067458.1};
RN [1] {ECO:0000313|RefSeq:XP_030067458.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
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}.
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DR RefSeq; XP_030067458.1; XM_030211598.1.
DR AlphaFoldDB; A0A6P7YR54; -.
DR FunCoup; A0A6P7YR54; 180.
DR GeneID; 115475675; -.
DR KEGG; muo:115475675; -.
DR InParanoid; A0A6P7YR54; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000515156; Chromosome 1.
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; cd20369; Rcat_RBR_RNF144B; 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.
DR PROSITE; PS50089; ZF_RING_2; 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:UP000515156};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 258..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..244
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 30..76
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 303 AA; 33802 MW; A99DF63F0AA45E81 CRC64;
MASAGRVCHH TLMTAMSASG ELALEPLITC RLCLGEHSRD MMMSLQECSC IFCTQCLKQY
VQLAVREGFG SPVTCPDMEC LHHGILQEAE IASLVPDDQL RLYERLKFER EVHLDPHRTW
CPAAACQAVC PVELNDPENP VSVVCQSCHL TFCSSCKSAW HPETSCQENQ PITASTKNGI
PIDPDPEAPI KQCPVCRIYI ERNEGCAQMM CRNCKHTFCW YCLHNLDNDI FLRHYDKGPC
RNKLGHSRAS VMWNRTQVVG ILVGLGIIAL VTSPLLLLAS PCIICCVCKS CRGKKKKHEP
PTT
//
