ID TRIM7_MOUSE Reviewed; 510 AA.
AC Q923T7; Q5NCB6; Q99PQ5;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM7 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9C029};
DE AltName: Full=Glycogenin-interacting protein;
DE AltName: Full=Tripartite motif-containing protein 7;
GN Name=Trim7; Synonyms=Gnip;
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 [MRNA] (ISOFORM 3).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C3H/HeJ;
RA Skurat A.V., Dietrich A.D., Zhai L., Roach P.J.;
RT "Identification of human skeletal muscle proteins which interact with
RT glycogenin.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
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 [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30928727; DOI=10.1016/j.molimm.2019.01.015;
RA Lu M., Zhu X., Yang Z., Zhang W., Sun Z., Ji Q., Chen X., Zhu J., Wang C.,
RA Nie S.;
RT "E3 ubiquitin ligase tripartite motif 7 positively regulates the TLR4-
RT mediated immune response via its E3 ligase domain in macrophages.";
RL Mol. Immunol. 109:126-133(2019).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32126128; DOI=10.1371/journal.ppat.1008387;
RA Yang B., Liu Y., Cui Y., Song D., Zhang G., Ma S., Liu Y., Chen M.,
RA Chen F., Wang H., Wang J.;
RT "RNF90 negatively regulates cellular antiviral responses by targeting MITA
RT for degradation.";
RL PLoS Pathog. 16:e1008387-e1008387(2020).
RN [6]
RP FUNCTION.
RX PubMed=35972292; DOI=10.1128/jvi.00707-22;
RA Sullender M.E., Pierce L.R., Annaswamy Srinivas M., Crockett S.L.,
RA Dunlap B.F., Rodgers R., Schriefer L.A., Kennedy E.A., Stewart B.M.,
RA Doench J.G., Baldridge M.T., Orchard R.C.;
RT "Selective Polyprotein Processing Determines Norovirus Sensitivity to
RT Trim7.";
RL J. Virol. 96:e0070722-e0070722(2022).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that have both tumor-promoting
CC and tumor-suppressing activities and functions in several biological
CC processes including innate immunity, regulation of ferroptosis as well
CC as cell proliferation and migration. Acts as an antiviral effector
CC against multiple viruses by targeting specific viral proteins for
CC ubiquitination and degradation including norovirus NTPase protein.
CC Mechanistically, recognizes the C-terminal glutamine-containing motif
CC generated by viral proteases that process the polyproteins and trigger
CC their ubiquitination and subsequent degradation (PubMed:35972292).
CC Mediates 'Lys-63'-linked polyubiquitination and stabilization of the
CC JUN coactivator RNF187 in response to growth factor signaling via the
CC MEK/ERK pathway, thereby regulating JUN transactivation and cellular
CC proliferation (By similarity). Promotes the TLR4-mediated signaling
CC activation through its E3 ligase domain leading to production of pro-
CC inflammatory cytokines and type I interferon (PubMed:30928727). Also
CC plays a negative role in the regulation of exogenous cytosolic DNA
CC virus-triggered immune response. Mechanistically, enhances the 'Lys-
CC 48'-linked ubiquitination of STING1 leading to its proteasome-dependent
CC degradation. Mediates the ubiquitination of the SIN3-HDAC chromatin
CC remodeling complex component BRMS1. Modulates NCOA4-mediated
CC ferritinophagy and ferroptosis in glioblastoma cells by ubiquitinating
CC NCOA4, leading to its degradation (PubMed:32126128).
CC {ECO:0000250|UniProtKB:Q9C029, ECO:0000269|PubMed:30928727,
CC ECO:0000269|PubMed:32126128, ECO:0000269|PubMed:35972292}.
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:0000250|UniProtKB:Q9C029};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9C029}.
CC -!- SUBUNIT: Forms homodimers. Interacts with GNIP2. Interacts with GYG1.
CC Interacts with RNF187 (via C-terminus). {ECO:0000250|UniProtKB:Q9C029}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9C029}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9C029}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9C029}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q923T7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q923T7-2; Sequence=VSP_012289;
CC Name=3;
CC IsoId=Q923T7-3; Sequence=VSP_012290, VSP_012291;
CC -!- TISSUE SPECIFICITY: Highly expressed in antigen-presenting cells.
CC {ECO:0000269|PubMed:30928727}.
CC -!- DOMAIN: The B30.2 domain mediates interaction with GYG.
CC {ECO:0000250|UniProtKB:Q9C029}.
CC -!- DOMAIN: The coiled-coil region mediates homodimerization and
CC heterodimerization. {ECO:0000250|UniProtKB:Q9C029}.
CC -!- PTM: Phosphorylated at Ser-106 by RPS6KA5/MSK1, which stimulates the
CC ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q9C029}.
CC -!- PTM: Auto-ubiquitinates via 'Lys-63'-linked polyubiquitination.
CC {ECO:0000250|UniProtKB:Q9C029}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant protects mice from DNA virus
CC infection. {ECO:0000269|PubMed:32126128}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF220033; AAG53487.1; -; mRNA.
DR EMBL; AF396656; AAK85382.1; -; mRNA.
DR EMBL; AL645849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48779.1; -. [Q923T7-2]
DR CCDS; CCDS83797.1; -. [Q923T7-1]
DR RefSeq; NP_444396.2; NM_053166.2. [Q923T7-2]
DR RefSeq; XP_006534638.1; XM_006534575.3. [Q923T7-2]
DR AlphaFoldDB; Q923T7; -.
DR SMR; Q923T7; -.
DR BioGRID; 220444; 2.
DR STRING; 10090.ENSMUSP00000039011; -.
DR GlyGen; Q923T7; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q923T7; -.
DR PhosphoSitePlus; Q923T7; -.
DR PaxDb; 10090-ENSMUSP00000104836; -.
DR ProteomicsDB; 298127; -. [Q923T7-1]
DR ProteomicsDB; 298128; -. [Q923T7-2]
DR ProteomicsDB; 298129; -. [Q923T7-3]
DR Antibodypedia; 29710; 174 antibodies from 27 providers.
DR DNASU; 94089; -.
DR Ensembl; ENSMUST00000109213.9; ENSMUSP00000104836.3; ENSMUSG00000040350.17. [Q923T7-2]
DR GeneID; 94089; -.
DR KEGG; mmu:94089; -.
DR UCSC; uc007ipd.2; mouse. [Q923T7-1]
DR AGR; MGI:2137353; -.
DR CTD; 81786; -.
DR MGI; MGI:2137353; Trim7.
DR VEuPathDB; HostDB:ENSMUSG00000040350; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT01030000234669; -.
DR HOGENOM; CLU_013137_0_0_1; -.
DR InParanoid; Q923T7; -.
DR OMA; DMKMHIC; -.
DR PhylomeDB; Q923T7; -.
DR TreeFam; TF317532; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 94089; 3 hits in 62 CRISPR screens.
DR ChiTaRS; Trim7; mouse.
DR PRO; PR:Q923T7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q923T7; Protein.
DR Bgee; ENSMUSG00000040350; Expressed in right kidney and 125 other cell types or tissues.
DR ExpressionAtlas; Q923T7; baseline and differential.
DR Genevisible; Q923T7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA: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:0140374; P:antiviral innate immune response; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd19762; Bbox2_TRIM7-like; 1.
DR CDD; cd16594; RING-HC_TRIM7-like_C-IV; 1.
DR CDD; cd13740; SPRY_PRY_TRIM7; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR000315; Znf_B-box.
DR InterPro; IPR020457; Znf_B-box_chordata.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF689; E3 UBIQUITIN-PROTEIN LIGASE TRIM7; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF15227; zf-C3HC4_4; 1.
DR PRINTS; PR01406; BBOXZNFINGER.
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; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 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 2: Evidence at transcript level;
KW Alternative splicing; Antiviral defense; Coiled coil; Cytoplasm;
KW Golgi apparatus; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..510
FT /note="E3 ubiquitin-protein ligase TRIM7"
FT /id="PRO_0000056205"
FT DOMAIN 323..510
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 29..81
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 124..165
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 165..275
FT /evidence="ECO:0000255"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 106
FT /note="Phosphoserine; by RPS6KA5"
FT /evidence="ECO:0000250|UniProtKB:Q9C029"
FT VAR_SEQ 1..207
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012289"
FT VAR_SEQ 206..243
FT /note="KQMAAEKEKVGAEFQALRAFLVEQEGRLLSRLEVLSRE -> VSPSVRSIGL
FT WMTKAERERERERERERERERERIWLKQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_012290"
FT VAR_SEQ 244..510
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_012291"
SQ SEQUENCE 510 AA; 57021 MW; 01335C644BFFA4E3 CRC64;
MATVGPRTGP NAGAEALALA AELQGEATCS ICLEFFREPV SVECGHSFCR ACIMRCWERP
GAGTGTATRT LPCPLPCPQC REPARPSQLR PNRQLAAVVS LLRRFSLPPT APGERGTPAV
PARAAAARCS QHGEQLKLYC QDDGRAICVV CDRAREHRSH AVLPLEEAVQ EAKELLDSRL
RALKKVLEDY EAFRSTEERE SKELLKQMAA EKEKVGAEFQ ALRAFLVEQE GRLLSRLEVL
SREVTQKQNE NLAQLEGEIT QLSKLSGQIQ ETAQKPDLDF LQEFKSTLSK CSSVPSSKPT
TVSSEMKNKV WNVSLKSFVL KGLLKKFKED LQGELEKEEK VELTLDPDTA NPRLILSLDL
KSVRLGQRAQ DLPNHPRRFD TNTRVLASCG FSSGRHHWEV EVGSKDGWAF GVARESVRRK
GLTPFTPEEG VWAMQLNNGQ YWAVTSPERT QLNCGHLSRV RVALDLEVGA VSFYAVEDMR
HLYTFRVNFQ ERVFPLFSVC STGTYLRIWP
//
