ID A0A2U3X589_ODORO Unreviewed; 292 AA.
AC A0A2U3X589;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 18-JUN-2025, entry version 32.
DE RecName: Full=E3 ubiquitin-protein ligase RNF144A {ECO:0000256|ARBA:ARBA00069723};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE AltName: Full=RING finger protein 144A {ECO:0000256|ARBA:ARBA00078868};
DE AltName: Full=UbcM4-interacting protein 4 {ECO:0000256|ARBA:ARBA00075379};
DE AltName: Full=Ubiquitin-conjugating enzyme 7-interacting protein 4 {ECO:0000256|ARBA:ARBA00078433};
GN Name=RNF144A {ECO:0000313|RefSeq:XP_004417533.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004417533.1};
RN [1] {ECO:0000313|RefSeq:XP_004417533.1}
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. Mediates the ubiquitination and degradation of the DNA
CC damage kinase PRKDC during DNA damage. Positively regulates DNA virus
CC or exogenous cytosolic DNA-triggered innate immune response by
CC mediating STING1 ubiquitination and increasing its 'Lys-6'-linked
CC ubiquitination and translocation from the endoplasmic reticulum to the
CC Golgi leading to downstream signaling pathways. Plays a positive role
CC in EGF-dependent cell proliferation by prolonging EGF/EGFR signaling
CC during EGF stimulation through EGFR ubiquitination. Increases ERK
CC activity independently of EGFR signaling by promoting
CC polyubiquitination and subsequent degradation of VRK3 in the cytosol.
CC {ECO:0000256|ARBA:ARBA00054980}.
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: Self-associates. Interacts with UBE2L3.
CC {ECO:0000256|ARBA:ARBA00064341}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF144 subfamily.
CC {ECO:0000256|ARBA:ARBA00038342}.
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DR RefSeq; XP_004417533.1; XM_004417476.2.
DR AlphaFoldDB; A0A2U3X589; -.
DR STRING; 9708.A0A2U3X589; -.
DR GeneID; 101382230; -.
DR KEGG; oro:101382230; -.
DR CTD; 9781; -.
DR InParanoid; A0A2U3X589; -.
DR OrthoDB; 7426at33554; -.
DR Proteomes; UP000245340; Unplaced.
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; cd20366; BRcat_RBR_RNF144A; 1.
DR CDD; cd16777; mRING-HC-C4C4_RBR_RNF144A; 1.
DR CDD; cd20352; Rcat_RBR_RNF144; 1.
DR FunFam; 1.20.120.1750:FF:000006; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340};
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};
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 250..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..236
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 20..66
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 292 AA; 32723 MW; F2F169675C949E26 CRC64;
MTTARYRPTW DLALDPLVSC KLCLGEYPVE QMTTIAQCQC IFCTLCLKQY VELLIKEGLE
TAISCPDAAC PKQGHLQEDE IECMVAADIM QRYKKLQFER EVLLDPCRTW CPASACQAVC
QLQEMGLQTP QLVQCKACDM EFCSACKASW HPGQGCPEAL PITFLPGETS SAFKLEEDDA
PIKRCPKCKV YIERDEGCAQ MMCKNCKHAF CWYCLESLDD DFLLIHYDKG PCRNKLGHSR
ASVIWHRTQV VGIFAGFGLL LLVASPFLLL ATPFVLCCKC KCSKGDDDPL PT
//
