ID   TRI40_RAT               Reviewed;         247 AA.
AC   Q6MFY8;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=E3 ubiquitin ligase TRIM40;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q6P9F5};
DE   AltName: Full=Probable E3 NEDD8-protein ligase;
DE   AltName: Full=RING finger protein 35;
GN   Name=Trim40; Synonyms=Rnf35;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15060004; DOI=10.1101/gr.1987704;
RA   Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA   Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT   "The genomic sequence and comparative analysis of the rat major
RT   histocompatibility complex.";
RL   Genome Res. 14:631-639(2004).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that plays a role in the
CC       limitation of the innate immune response. Mediates inhibition of the
CC       RLR signaling pathway by ubiquitinating DDX58 and IFIH1 receptors,
CC       leading to their proteasomal degradation. Promotes also the neddylation
CC       of IKBKG/NEMO, stabilizing NFKBIA, and thereby inhibiting of NF-kappa-B
CC       nuclear translocation and activation. {ECO:0000250|UniProtKB:Q6P9F5}.
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:Q6P9F5};
CC   -!- SUBUNIT: Interacts with NEDD8. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR   EMBL; BX883051; CAE84059.1; -; Genomic_DNA.
DR   RefSeq; NP_001009175.1; NM_001009175.1.
DR   AlphaFoldDB; Q6MFY8; -.
DR   SMR; Q6MFY8; -.
DR   STRING; 10116.ENSRNOP00000035419; -.
DR   CarbonylDB; Q6MFY8; -.
DR   iPTMnet; Q6MFY8; -.
DR   PhosphoSitePlus; Q6MFY8; -.
DR   PaxDb; Q6MFY8; -.
DR   Ensembl; ENSRNOT00000029070; ENSRNOP00000035419; ENSRNOG00000000783.
DR   GeneID; 365528; -.
DR   KEGG; rno:365528; -.
DR   UCSC; RGD:1359645; rat.
DR   CTD; 135644; -.
DR   RGD; 1359645; Trim40.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00710000106875; -.
DR   HOGENOM; CLU_013137_3_0_1; -.
DR   InParanoid; Q6MFY8; -.
DR   OMA; PEHVSHH; -.
DR   OrthoDB; 1129525at2759; -.
DR   PhylomeDB; Q6MFY8; -.
DR   PRO; PR:Q6MFY8; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000000783; Expressed in jejunum and 5 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008385; C:IkappaB kinase complex; ISO:RGD.
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:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:RGD.
DR   GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISO:RGD.
DR   GO; GO:0045116; P:protein neddylation; ISO:RGD.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Metal-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..247
FT                   /note="E3 ubiquitin ligase TRIM40"
FT                   /id="PRO_0000056261"
FT   ZN_FING         12..55
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         64..105
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          111..148
FT                   /evidence="ECO:0000255"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ   SEQUENCE   247 AA;  28389 MW;  B72EA8A3B6ED999E CRC64;
     MVPLDKDNQD ICPICLDPLK EAVSTDCRHL FCRMCLIRHM DKASVSGVLS CPVCRKPCSE
     TVLGDNYICH THQKRVCRFC ESSRHLLCEE CLQSPEHRAH TELSIENAIS HYKERLNRRS
     RKLRKDLGDL QRLKAQEEKM LQALQVDWGS HRPRTEQQNQ DQTELQQKAL PRHWLDQRED
     PPEEVAKVFN FSEAVTQLSI LVSSLERMAK ELDASTLKDA SDLLDRSSQQ KLEGLLSHVP
     PANSKLS