TRIM7_MOUSE
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 03-AUG-2022, entry version 140.
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase (By similarity). Mediates 'Lys-
CC 63'-linked polyubiquitination and stabilization of the JUN coactivator
CC RNF187 in response to growth factor signaling via the MEK/ERK pathway,
CC thereby regulating JUN transactivation and cellular proliferation (By
CC similarity). Promotes the TLR4-mediated signaling activation through
CC its E3 ligase domain leading to production of pro-inflammatory
CC cytokines and type I interferon (PubMed:30928727). Also plays a
CC negative role in the regulation of exogenous cytosolic DNA virus-
CC triggered immune response. Mechanistically, enhances the 'Lys-48'-
CC linked ubiquitination of STING1 leading to its proteasome-dependent
CC degradation (PubMed:32126128). {ECO:0000250|UniProtKB:Q9C029,
CC ECO:0000269|PubMed:30928727, ECO:0000269|PubMed:32126128}.
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, and heterodimers with GNIP2. Interacts with
CC GYG. Interacts with RNF187 (via C-terminus).
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 -!- 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 STRING; 10090.ENSMUSP00000104836; -.
DR iPTMnet; Q923T7; -.
DR PhosphoSitePlus; Q923T7; -.
DR PaxDb; Q923T7; -.
DR PRIDE; Q923T7; -.
DR ProteomicsDB; 298127; -. [Q923T7-1]
DR ProteomicsDB; 298128; -. [Q923T7-2]
DR ProteomicsDB; 298129; -. [Q923T7-3]
DR Antibodypedia; 29710; 157 antibodies from 27 providers.
DR DNASU; 94089; -.
DR Ensembl; ENSMUST00000109213; ENSMUSP00000104836; ENSMUSG00000040350. [Q923T7-2]
DR GeneID; 94089; -.
DR KEGG; mmu:94089; -.
DR UCSC; uc007ipd.2; mouse. [Q923T7-1]
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; DAENMQH; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q923T7; -.
DR TreeFam; TF317532; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 94089; 3 hits in 59 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 tissues.
DR ExpressionAtlas; Q923T7; baseline and differential.
DR Genevisible; Q923T7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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; 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 Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 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; 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 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW 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
