ID A0A9J7EFW7_SPOLT Unreviewed; 668 AA.
AC A0A9J7EFW7;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, 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 Name=LOC111358721 {ECO:0000313|RefSeq:XP_022829748.1};
OS Spodoptera litura (Asian cotton leafworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=69820 {ECO:0000313|Proteomes:UP000301870, ECO:0000313|RefSeq:XP_022829748.1};
RN [1] {ECO:0000313|RefSeq:XP_022829748.1}
RP IDENTIFICATION.
RC STRAIN=Ishihara {ECO:0000313|RefSeq:XP_022829748.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_022829748.1};
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_022829748.1; XM_022973980.1.
DR GeneID; 111358721; -.
DR KEGG; sliu:111358721; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000301870; Chromosome 28.
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 GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProtKB-ARBA.
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.
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:UP000301870};
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 601..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 376..587
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 380..428
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..221
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 72859 MW; 93D48D95EC9996EB CRC64;
MHDRRVQLRG NSVAPLKMLR PESPLADHRS LLPRRLLPAK AQIAPADKRK NRRSLELNPP
SNDHAPYDYS KLLISKTTDS LNTECPRKLI NKQDSTDSLK RALLSKDDKK SASKESDKKG
QISKQDSSES LKKALLCRQD SNESVKRKEA EAKRTQKDEA KRVNEIKRGS DKKGLLETDI
DEPLKRIYER RTGCARPTLP PVAEKSAPSP NSPNGSPNTP SVAAVAEGLA RWGSGLLSPR
EEPRLKAARS WYGYGTLPTD SDKMGAGANG PGGRRALELI LSGGLKSLAR PAKPVRRAAS
RDSVLSQPQP LLEGLRKCST VLALTDREKS SEPMRAHNRL RAPSVCSRCS SLLSLAGAGG
SRYSLDGAGS GFVPAAPINC KLCLEDATVD KVTLISGCGC SFCTKCMKAY VEFEVCNGAY
EVSCPDARCR VGAALNLEEI SELVEPAVME KHLKFRLNHE VAMDAGRAFC PRVGCDTVVQ
VRAASPAHCP TCRHDFCSQC NQEWHGGLSC EAAAASSSMG GAGAPLLPDS ELIKLCPMCR
VPIEKDEGCA QMMCKRCKHV FCWYCLASLD DDFLLRHYDK GPCKNKLGHS RASVLWHRAQ
VVGIFAGFGL LLLVASPLLL LAAPCIVCCK CRLCNPSTKN LEEVDEIDSI SPTRDDDRDQ
QPDRYLSD
//
