TRI41_MOUSE
ID TRI41_MOUSE Reviewed; 630 AA.
AC Q5NCC3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM41 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:30485814};
DE AltName: Full=Tripartite motif-containing protein 41;
GN Name=Trim41 {ECO:0000303|PubMed:30485814, ECO:0000312|MGI:MGI:2384814};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, AND INTERACTION WITH TRIM17.
RX PubMed=30485814; DOI=10.1016/j.celrep.2018.11.002;
RA Lassot I., Mora S., Lesage S., Zieba B.A., Coque E., Condroyer C.,
RA Bossowski J.P., Mojsa B., Marelli C., Soulet C., Tesson C.,
RA Carballo-Carbajal I., Laguna A., Mangone G., Vila M., Brice A.,
RA Desagher S.;
RT "The E3 Ubiquitin Ligases TRIM17 and TRIM41 Modulate alpha-Synuclein
RT Expression by Regulating ZSCAN21.";
RL Cell Rep. 25:2484-2496.e9(2018).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=33640899; DOI=10.1038/s41392-021-00477-8;
RA Yu Z., Li X., Yang M., Huang J., Fang Q., Jia J., Li Z., Gu Y., Chen T.,
RA Cao X.;
RT "TRIM41 is required to innate antiviral response by polyubiquitinating
RT BCL10 and recruiting NEMO.";
RL Signal Transduct. 6:90-90(2021).
CC -!- FUNCTION: E3 ligase that plays essential roles in innate antiviral
CC response (PubMed:33640899). Directly binds to influenza A virus or
CC vesicular stomatitis virus nucleoproteins and targets them for
CC ubiquitination and proteasomal degradation, thereby limiting viral
CC infections (By similarity). Activates the innate antiviral response by
CC catalyzing monoubiquitination of CGAS, thereby activating CGAS (By
CC similarity). Also involved in innate antiviral response by mediating
CC 'Lys-63'-linked polyubiquitylation of BCL10 which in turn hubs NEMO for
CC activation of NF-kappa-B and IRF3 pathways (PubMed:33640899). Catalyzes
CC the ubiquitin-mediated degradation of other substrates including
CC protein kinase C, ZSCAN21 or TOP3B suggesting additional roles besides
CC its function in immune response (PubMed:30485814).
CC {ECO:0000250|UniProtKB:Q8WV44, ECO:0000269|PubMed:30485814,
CC ECO:0000269|PubMed:33640899}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:33640899};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:33640899}.
CC -!- SUBUNIT: Interacts with PRKCA. Interacts with NOD2 (By similarity).
CC Interacts with TRIM17; this interaction prevents TRIM41 activity on
CC ZSCAN2 (PubMed:30485814). {ECO:0000250|UniProtKB:Q8WV44,
CC ECO:0000269|PubMed:30485814}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33640899}. Nucleus
CC {ECO:0000250|UniProtKB:Q8WV44}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q8WV44}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant impairs the production of
CC inflammatory cytokines and type I interferons in macrophages after
CC infection with both DNA and RNA viruses. {ECO:0000269|PubMed:33640899}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AL645849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466575; EDL33789.1; -; Genomic_DNA.
DR CCDS; CCDS36138.1; -.
DR RefSeq; NP_663352.2; NM_145377.2.
DR AlphaFoldDB; Q5NCC3; -.
DR SMR; Q5NCC3; -.
DR IntAct; Q5NCC3; 1.
DR STRING; 10090.ENSMUSP00000037055; -.
DR iPTMnet; Q5NCC3; -.
DR PhosphoSitePlus; Q5NCC3; -.
DR EPD; Q5NCC3; -.
DR MaxQB; Q5NCC3; -.
DR PaxDb; Q5NCC3; -.
DR PeptideAtlas; Q5NCC3; -.
DR PRIDE; Q5NCC3; -.
DR ProteomicsDB; 258976; -.
DR Antibodypedia; 17930; 218 antibodies from 26 providers.
DR Ensembl; ENSMUST00000047145; ENSMUSP00000037055; ENSMUSG00000040365.
DR GeneID; 211007; -.
DR KEGG; mmu:211007; -.
DR UCSC; uc007ipc.1; mouse.
DR CTD; 90933; -.
DR MGI; MGI:2384814; Trim41.
DR VEuPathDB; HostDB:ENSMUSG00000040365; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154294; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q5NCC3; -.
DR OMA; WDTPMRE; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q5NCC3; -.
DR TreeFam; TF342569; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 211007; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Trim41; mouse.
DR PRO; PR:Q5NCC3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5NCC3; protein.
DR Bgee; ENSMUSG00000040365; Expressed in retinal neural layer and 255 other tissues.
DR ExpressionAtlas; Q5NCC3; baseline and differential.
DR Genevisible; Q5NCC3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd13741; SPRY_PRY_TRIM41; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR042828; TRIM41_SPRY_PRY.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..630
FT /note="E3 ubiquitin-protein ligase TRIM41"
FT /id="PRO_0000386643"
FT DOMAIN 413..630
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 20..61
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 222..263
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 51..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 281..374
FT /evidence="ECO:0000255"
FT COMPBIAS 51..74
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..167
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WV44"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WV44"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WV44"
SQ SEQUENCE 630 AA; 71818 MW; 3CAD7D459DF882DE CRC64;
MAAVAMTPNP VQTLQEEAVC AICLDYFTDP VSIGCGHNFC RVCVTQLWGG EDEEDRDELD
REEEEEEVGE EEEVEAVGAG GGWDTPMREE DYEGDMEEEA EEEEEVFWSS GIGGSNWDNM
DYVWEEEEEE EEEELDYYLG DVADLRGEDE DEEEEVLEED EEEELDPITQ LPPPPAPRRC
FTCPQCRKSF PRRSFRPNLQ LANMVQVIRQ MHPTPGRGSR VNEQGICPRH QEALKLFCEV
DEEAICVVCR ESRSHKQHSV VPLEEVVQEY KAKLQGHVEP LRKHLEAVQK MKAKEERRVT
ELKSQMKSEL AAVASEFGRL TRFLAEEQAG LERRLREMHE AQLGRAGAAA NRLEEQAAQL
SRLLAEAQER SQQGGLRLLQ DIKETFNRCE EIQLQPPEIW SPDPCQPHSH DFLTDAIVRK
MSRMFCQAAR VDLTLDPDTA HPALLLSPDR RGVRLAERRQ EVPEHSKRFS ADCCVLGAQG
FRSGRHYWEV EVGGRRGWAV GAARESTHHK EKVGSGGSSV SSGDASSSRH HHRRRRLHLP
QQLLLQREVW CVGTHGKRYQ AQSSTEQTLL SPCEKPRRFG VYLDYEAGRL GFYNADTLAH
VHTFSAAFLG ERVFPFFRVL SKGTRIKLCP
