ID G3W0R5_SARHA Unreviewed; 296 AA.
AC G3W0R5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 18-JUN-2025, entry version 77.
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|Ensembl:ENSSHAP00000009020.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000009020.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000009020.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000009020.2}
RP IDENTIFICATION.
RG Ensembl;
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_031807051.1; XM_031951191.1.
DR AlphaFoldDB; G3W0R5; -.
DR STRING; 9305.ENSSHAP00000009020; -.
DR Ensembl; ENSSHAT00000009094.2; ENSSHAP00000009020.2; ENSSHAG00000007808.2.
DR GeneID; 100931005; -.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000157701; -.
DR HOGENOM; CLU_053598_1_0_1; -.
DR TreeFam; TF324777; -.
DR Proteomes; UP000007648; 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 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:UP000007648};
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 254..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..240
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 296 AA; 33482 MW; B9AF33D2770116FE CRC64;
MTMARYRPTW DLALDPLVSC KLCLGEYPLE QMTTIAQCQC IFCTLCLKQY VELLIKEGLE
TAISCPDAAC PKRGHLQENE IECMVASEIM QRYKKLQFER EVLLDPCRTW CPSSTCQAVC
QLQDMGPQTP QLVQCKACNM EFCSSCKANW HPGQSCQETM PVTFLPGETS VSHSSSFKID
EEDAPIKRCP KCRVYIERDE GCAQMMCKNC KHAFCWYCLE SLDDDFLLIH YDKGPCRNKL
GHSRASVIWH RTQVVGIFAG FGLLLLVASP FLLLATPFVL CCKCKCHKGD DDPLPT
//
