ID A0A8S3W8E3_PARAO Unreviewed; 623 AA.
AC A0A8S3W8E3;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 18-JUN-2025, entry version 13.
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=PAPOLLO_LOCUS3408 {ECO:0000313|EMBL:CAG4946657.1};
OS Parnassius apollo (Apollo butterfly) (Papilio apollo).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Parnassiinae; Parnassini; Parnassius; Parnassius.
OX NCBI_TaxID=110799 {ECO:0000313|EMBL:CAG4946657.1, ECO:0000313|Proteomes:UP000691718};
RN [1] {ECO:0000313|EMBL:CAG4946657.1}
RP NUCLEOTIDE SEQUENCE.
RA Tunstrom K.;
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:CAG4946657.1}.
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DR EMBL; CAJQZP010000212; CAG4946657.1; -; Genomic_DNA.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000691718; 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 GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProtKB-ARBA.
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 InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
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 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:UP000691718};
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 555..577
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 330..541
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 334..382
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 70..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 623 AA; 67782 MW; B84B068C6C8DB800 CRC64;
MTISWEIKEP VKTSFLHNGE FNSAAAPHRR PKCCVQNRPS LTTAAFCHAG CSRLKRALLS
KDEKKAVKES DKKTVTKQDS SESLKKALLC RQESNESAKR RDSDPKWTQR QEDLKKTDEV
KRGNDKKGLL ETDTDDTCKR IYERRIGCAR PTLPPVAERS VPSQNSPNGS PRTPGVAAVA
EGVVRWGSGL LSPKDEPRLR PARSWYGYGT LPTDGDKMGA GANGPGGRRA LELILSSGLK
SLARPARPVR RAASRDSVLS QPQPLLEGLR KCSTVLALSE RERAGEPIRA HNRLRAPSVC
SRCSSLLSLA GAGGSRYSLD GAGGVFVPAA PVNCKLCLED ATPDKVTVIS GCGCSFCTKC
MKAYVEFEVC NGAYEVSCPD ARCRVGAALS IDEISVLVEP AVLEKHLKFR LNHEVSMDSG
RAFCPRVGCD TVVSVRAASP AHCPTCRHDF CSQCNQEWHG SLSCEAAAAS SSMGGAGSPL
LPESELIKMC PMCRVPIEKD EGCAQMMCKR CKHVFCWYCL ASLDDDFLLR HYDKGPCKNK
LGHSRASVLW HRAQVVGIFA GFGLLLLVAS PLLLLAAPCI VCCKCRLCNP NTKNLEEVDE
IESISPGREE EGDEITRARY LSD
//
