ID A0A8B8Z0E5_BALMU Unreviewed; 293 AA.
AC A0A8B8Z0E5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 17.
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_036728266.1,
GN ECO:0000313|RefSeq:XP_036728267.1, ECO:0000313|RefSeq:XP_036728268.1,
GN ECO:0000313|RefSeq:XP_036728269.1, ECO:0000313|RefSeq:XP_036728271.1,
GN ECO:0000313|RefSeq:XP_036728272.1, ECO:0000313|RefSeq:XP_036728273.1,
GN ECO:0000313|RefSeq:XP_036728274.1, ECO:0000313|RefSeq:XP_036728275.1};
OS Balaenoptera musculus (Blue whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=9771 {ECO:0000313|Proteomes:UP000694857, ECO:0000313|RefSeq:XP_036728273.1};
RN [1] {ECO:0000313|RefSeq:XP_036728266.1, ECO:0000313|RefSeq:XP_036728267.1}
RP IDENTIFICATION.
RC TISSUE=Epidermis and Blubber {ECO:0000313|RefSeq:XP_036728266.1,
RC ECO:0000313|RefSeq:XP_036728267.1};
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. 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}.
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 RefSeq; XP_036728266.1; XM_036872371.1.
DR RefSeq; XP_036728267.1; XM_036872372.1.
DR RefSeq; XP_036728268.1; XM_036872373.1.
DR RefSeq; XP_036728269.1; XM_036872374.1.
DR RefSeq; XP_036728271.1; XM_036872376.1.
DR RefSeq; XP_036728272.1; XM_036872377.1.
DR RefSeq; XP_036728273.1; XM_036872378.1.
DR RefSeq; XP_036728274.1; XM_036872379.1.
DR RefSeq; XP_036728275.1; XM_036872380.1.
DR GeneID; 118905668; -.
DR KEGG; bmus:118905668; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000694857; Chromosome 13.
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:UP000694857};
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 251..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..237
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 293 AA; 32838 MW; DB89537DD59AF819 CRC64;
MTTARCRPTW DLALDPLVSC KLCLGEYPVE QMTTIAQCQC IFCTLCLKQY VELLIKEGLE
TAISCPDATC PKQGHLQENE IECMVAAEIM QRYKKLQFER EVLLDPCRTW CPASTCQAVC
QLQEMGLQTP QLVQCKACDT EFCSACKASW HPGQGCPETM PITFLPGETS SSAFPLEEDD
VPIKRCPKCK VYIERDEGCA QMMCKNCKHA FCWYCLESLD DDFLLIHYDK GPCRNKLGHS
RASVIWHRTQ VVGIFAGFGL LLLVASPFLL LATPFVLCCK CKCSKGDDDP LPT
//
